TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Stanić, Dragana
AU  - Stojadinović, Marija M.
AU  - Ognjenović, Jana
AU  - Mihajlovic, Luka
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4328
AB  - beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.
PB  - Elsevier
T2  - Food Chemistry
T1  - Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics
VL  - 125
IS  - 1
SP  - 84
EP  - 91
DO  - 10.1016/j.foodchem.2010.08.040
ER  - 

@article{
author = "Tantoush, Ziyad and Stanić, Dragana and Stojadinović, Marija M. and Ognjenović, Jana and Mihajlovic, Luka and Atanasković-Marković, Marina and Ćirković-Veličković, Tanja",
year = "2011",
abstract = "beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics",
volume = "125",
number = "1",
pages = "84-91",
doi = "10.1016/j.foodchem.2010.08.040"
}

Tantoush, Z., Stanić, D., Stojadinović, M. M., Ognjenović, J., Mihajlovic, L., Atanasković-Marković, M.,& Ćirković-Veličković, T.. (2011). Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. in Food Chemistry
Elsevier., 125(1), 84-91.
https://doi.org/10.1016/j.foodchem.2010.08.040

Tantoush Z, Stanić D, Stojadinović MM, Ognjenović J, Mihajlovic L, Atanasković-Marković M, Ćirković-Veličković T. Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. in Food Chemistry. 2011;125(1):84-91.
doi:10.1016/j.foodchem.2010.08.040 .

Tantoush, Ziyad, Stanić, Dragana, Stojadinović, Marija M., Ognjenović, Jana, Mihajlovic, Luka, Atanasković-Marković, Marina, Ćirković-Veličković, Tanja, "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics" in Food Chemistry, 125, no. 1 (2011):84-91,
https://doi.org/10.1016/j.foodchem.2010.08.040 . .

TY  - JOUR
AU  - Zarić, Božidarka
AU  - Jovanović, Vesna B.
AU  - Stojanović, Srđan
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/924
AB  - The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Theoretical Biology
T1  - Non-covalent interactions across subunit interfaces in Sm proteins
VL  - 271
IS  - 1
SP  - 18
EP  - 26
DO  - 10.1016/j.jtbi.2010.11.025
ER  - 

@article{
author = "Zarić, Božidarka and Jovanović, Vesna B. and Stojanović, Srđan",
year = "2011",
abstract = "The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Theoretical Biology",
title = "Non-covalent interactions across subunit interfaces in Sm proteins",
volume = "271",
number = "1",
pages = "18-26",
doi = "10.1016/j.jtbi.2010.11.025"
}

Zarić, B., Jovanović, V. B.,& Stojanović, S.. (2011). Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology
Academic Press Ltd- Elsevier Science Ltd, London., 271(1), 18-26.
https://doi.org/10.1016/j.jtbi.2010.11.025

Zarić B, Jovanović VB, Stojanović S. Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology. 2011;271(1):18-26.
doi:10.1016/j.jtbi.2010.11.025 .

Zarić, Božidarka, Jovanović, Vesna B., Stojanović, Srđan, "Non-covalent interactions across subunit interfaces in Sm proteins" in Journal of Theoretical Biology, 271, no. 1 (2011):18-26,
https://doi.org/10.1016/j.jtbi.2010.11.025 . .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Dobrijevic, Dragana
AU  - Jadranin, Milka
AU  - Blanusa, Milan
AU  - Vukmirica, Jelena
AU  - Ćirković Veličković, Tanja
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/709
AB  - BACKGROUND: The major peanut allergens are Ara h 1, Ara h 2 and Ara h 6. Proteolytic processing has been shown to be required for the maturation process of Ara h 6. The aim of this study was to examine whether Ara h 2 undergoes proteolytic processing and, if so, whether proteolytic processing influences its ability to bind human immunoglobulin E (IgE). RESULTS: Ara h 2 isolated from peanut extract under conditions of protease inhibition revealed a single additional peak for its two known isoforms (Ara h 2.01 and Ara h 2.02), corresponding to a C-terminally truncated form lacking a dipeptide (RY). Ara h 2 isolated in the absence of protease inhibition, however, yielded two additional peaks, identified as C-terminally truncated forms lacking either a dipeptide (RY) or a single tyrosine residue. The IgE-binding capacity of the Ara h 2 truncated forms was not altered. CONCLUSION: Ara h 2 undergoes proteolytic processing by peanut proteases that involves C-terminal removal of a dipeptide. Hence Ara h 2 isolated from peanut extract is a complex mixture of two isoforms expressed by different genes, Ara h 2.01 and Ara h 2.02, as well as truncated forms generated by the proteolytic processing of these isoforms.
PB  - John Wiley & Sons Ltd, Chichester
T2  - Journal of the Science of Food and Agriculture
T1  - Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases
VL  - 90
IS  - 10
SP  - 1702
EP  - 1708
DO  - 10.1002/jsfa.4005
ER  - 

@article{
author = "Radosavljević, Jelena and Dobrijevic, Dragana and Jadranin, Milka and Blanusa, Milan and Vukmirica, Jelena and Ćirković Veličković, Tanja",
year = "2010",
abstract = "BACKGROUND: The major peanut allergens are Ara h 1, Ara h 2 and Ara h 6. Proteolytic processing has been shown to be required for the maturation process of Ara h 6. The aim of this study was to examine whether Ara h 2 undergoes proteolytic processing and, if so, whether proteolytic processing influences its ability to bind human immunoglobulin E (IgE). RESULTS: Ara h 2 isolated from peanut extract under conditions of protease inhibition revealed a single additional peak for its two known isoforms (Ara h 2.01 and Ara h 2.02), corresponding to a C-terminally truncated form lacking a dipeptide (RY). Ara h 2 isolated in the absence of protease inhibition, however, yielded two additional peaks, identified as C-terminally truncated forms lacking either a dipeptide (RY) or a single tyrosine residue. The IgE-binding capacity of the Ara h 2 truncated forms was not altered. CONCLUSION: Ara h 2 undergoes proteolytic processing by peanut proteases that involves C-terminal removal of a dipeptide. Hence Ara h 2 isolated from peanut extract is a complex mixture of two isoforms expressed by different genes, Ara h 2.01 and Ara h 2.02, as well as truncated forms generated by the proteolytic processing of these isoforms.",
publisher = "John Wiley & Sons Ltd, Chichester",
journal = "Journal of the Science of Food and Agriculture",
title = "Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases",
volume = "90",
number = "10",
pages = "1702-1708",
doi = "10.1002/jsfa.4005"
}

Radosavljević, J., Dobrijevic, D., Jadranin, M., Blanusa, M., Vukmirica, J.,& Ćirković Veličković, T.. (2010). Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases. in Journal of the Science of Food and Agriculture
John Wiley & Sons Ltd, Chichester., 90(10), 1702-1708.
https://doi.org/10.1002/jsfa.4005

Radosavljević J, Dobrijevic D, Jadranin M, Blanusa M, Vukmirica J, Ćirković Veličković T. Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases. in Journal of the Science of Food and Agriculture. 2010;90(10):1702-1708.
doi:10.1002/jsfa.4005 .

Radosavljević, Jelena, Dobrijevic, Dragana, Jadranin, Milka, Blanusa, Milan, Vukmirica, Jelena, Ćirković Veličković, Tanja, "Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases" in Journal of the Science of Food and Agriculture, 90, no. 10 (2010):1702-1708,
https://doi.org/10.1002/jsfa.4005 . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Monogioudi, Evanthia
AU  - Dilek, Ercili
AU  - Radosavljević, Jelena
AU  - Atanasković-Marković, Marina
AU  - Vuckovic, Olga
AU  - Raija, Lantto
AU  - Mattinen, Maija
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4168
AB  - Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.
PB  - Wiley
T2  - Molecular Nutrition and Food Research
T1  - Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein
VL  - 54
IS  - 9
SP  - 1273
EP  - 1284
DO  - 10.1002/mnfr.200900184
ER  - 

@article{
author = "Stanić, Dragana and Monogioudi, Evanthia and Dilek, Ercili and Radosavljević, Jelena and Atanasković-Marković, Marina and Vuckovic, Olga and Raija, Lantto and Mattinen, Maija and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2010",
abstract = "Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.",
publisher = "Wiley",
journal = "Molecular Nutrition and Food Research",
title = "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein",
volume = "54",
number = "9",
pages = "1273-1284",
doi = "10.1002/mnfr.200900184"
}

Stanić, D., Monogioudi, E., Dilek, E., Radosavljević, J., Atanasković-Marković, M., Vuckovic, O., Raija, L., Mattinen, M., Buchert, J.,& Ćirković-Veličković, T.. (2010). Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research
Wiley., 54(9), 1273-1284.
https://doi.org/10.1002/mnfr.200900184

Stanić D, Monogioudi E, Dilek E, Radosavljević J, Atanasković-Marković M, Vuckovic O, Raija L, Mattinen M, Buchert J, Ćirković-Veličković T. Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research. 2010;54(9):1273-1284.
doi:10.1002/mnfr.200900184 .

Stanić, Dragana, Monogioudi, Evanthia, Dilek, Ercili, Radosavljević, Jelena, Atanasković-Marković, Marina, Vuckovic, Olga, Raija, Lantto, Mattinen, Maija, Buchert, Johanna, Ćirković-Veličković, Tanja, "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein" in Molecular Nutrition and Food Research, 54, no. 9 (2010):1273-1284,
https://doi.org/10.1002/mnfr.200900184 . .

TY  - JOUR
AU  - Dimitrijević, Rajna
AU  - Jadranin, Milka
AU  - Burazer, Lidija
AU  - Ostojić, Sanja
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/743
AB  - The thermal stability of recombinant mannose-specific banana lectin (rBanLec), as well as its stability under conditions of simulated gastro-intestinal fluid (SGF), was investigated. rBanLec was heterologously produced in Escherichia coli, Molecular mass of rBanLec, assessed by ESI-TOF mass spectrometry, was 15972.2 Da. Thermodynamic parameters for rBanLec denaturation, obtained by differential scanning calorimetry (DSC), revealed a transition maximum temperature (T-m) of 60.8 degrees C, calorimetric enthalpy (H-cal) of 136.17 kcal/mol and van't Hoff enthalpy (H-VH) of 50.27 kcal/mol. rBanLec was stable following an incubation for 2 h in SGF, and then for I h, in the simulated intestinal fluid (SIF). Intact primary structure, biological and immunological reactivity of rBanLec were all preserved following treatment under SGF and SIF conditions. In conclusion, rBanLec is a good candidate for the novel bioadhesive lectin-based drug delivery systems to the gastro-intestinal tract (GIT).
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Evaluation of the thermal stability and digestibility of heterologously produced banana lectin
VL  - 120
IS  - 4
SP  - 1113
EP  - 1118
DO  - 10.1016/j.foodchem.2009.11.062
ER  - 

@article{
author = "Dimitrijević, Rajna and Jadranin, Milka and Burazer, Lidija and Ostojić, Sanja and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "The thermal stability of recombinant mannose-specific banana lectin (rBanLec), as well as its stability under conditions of simulated gastro-intestinal fluid (SGF), was investigated. rBanLec was heterologously produced in Escherichia coli, Molecular mass of rBanLec, assessed by ESI-TOF mass spectrometry, was 15972.2 Da. Thermodynamic parameters for rBanLec denaturation, obtained by differential scanning calorimetry (DSC), revealed a transition maximum temperature (T-m) of 60.8 degrees C, calorimetric enthalpy (H-cal) of 136.17 kcal/mol and van't Hoff enthalpy (H-VH) of 50.27 kcal/mol. rBanLec was stable following an incubation for 2 h in SGF, and then for I h, in the simulated intestinal fluid (SIF). Intact primary structure, biological and immunological reactivity of rBanLec were all preserved following treatment under SGF and SIF conditions. In conclusion, rBanLec is a good candidate for the novel bioadhesive lectin-based drug delivery systems to the gastro-intestinal tract (GIT).",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Evaluation of the thermal stability and digestibility of heterologously produced banana lectin",
volume = "120",
number = "4",
pages = "1113-1118",
doi = "10.1016/j.foodchem.2009.11.062"
}

Dimitrijević, R., Jadranin, M., Burazer, L., Ostojić, S.,& Gavrović-Jankulović, M.. (2010). Evaluation of the thermal stability and digestibility of heterologously produced banana lectin. in Food Chemistry
Elsevier Sci Ltd, Oxford., 120(4), 1113-1118.
https://doi.org/10.1016/j.foodchem.2009.11.062

Dimitrijević R, Jadranin M, Burazer L, Ostojić S, Gavrović-Jankulović M. Evaluation of the thermal stability and digestibility of heterologously produced banana lectin. in Food Chemistry. 2010;120(4):1113-1118.
doi:10.1016/j.foodchem.2009.11.062 .

Dimitrijević, Rajna, Jadranin, Milka, Burazer, Lidija, Ostojić, Sanja, Gavrović-Jankulović, Marija, "Evaluation of the thermal stability and digestibility of heterologously produced banana lectin" in Food Chemistry, 120, no. 4 (2010):1113-1118,
https://doi.org/10.1016/j.foodchem.2009.11.062 . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Burazer, Lidija M.
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4327
AB  - Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v I that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified ammo groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids.
AB  - Art v1 je glavni alergen polena crnog pelina (Artemisia vulgaris), značajnog uzročnika polenske groznice širom Evrope. Alergen-specifična imunoterapija je za sada jedini delotvoran način za tretiranje alergija, pri čemu primena modifikovanih alergena čini ovakav tretman bezbednijim i efikasnijim. U ovom radu, dva od tri (anhidrid cis-akonitne, citrakonske i 2,3-dimetilmaleinske kiseline) ispitivana anhidrida su se pokazala pogodnim za hemijske modifikacije alergena. Art v 1 je modifikovan cis-akonitilovanjem i citrakonilovanjem u cilju dobijanja derivata Art v 1 pogodnih za dalje imunološke testove. Acilovanjem Art v 1 dobijeni su derivati (caaArt v 1 i citArt v 1) sa oko 80 % izmodifikovanih amino grupa. Dobijeni derivati su monomerni, sa molekulskom masom sličnom nativnom Art v 1, ali sa dramatično smanjenim pI vrednostima. Oba derivata su relativno stabilna u neutralnoj, dok se u kiseloj sredini acil grupe hidrolizuju. Modifikacija alergena cis-akonitilovanjem i citrakonilovanjem može biti novi način za dobijanje alergoida.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation
T1  - Hemijske modifikacije Art v 1, glavnog alergena Artemisia vulgaris, cis-akonitilovanjem i citrakonilovanjem
VL  - 74
IS  - 4
SP  - 359
EP  - 366
DO  - 10.2298/JSC0904359S
ER  - 

@article{
author = "Stanić, Dragana and Burazer, Lidija M. and Gavrović-Jankulović, Marija and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v I that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified ammo groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids., Art v1 je glavni alergen polena crnog pelina (Artemisia vulgaris), značajnog uzročnika polenske groznice širom Evrope. Alergen-specifična imunoterapija je za sada jedini delotvoran način za tretiranje alergija, pri čemu primena modifikovanih alergena čini ovakav tretman bezbednijim i efikasnijim. U ovom radu, dva od tri (anhidrid cis-akonitne, citrakonske i 2,3-dimetilmaleinske kiseline) ispitivana anhidrida su se pokazala pogodnim za hemijske modifikacije alergena. Art v 1 je modifikovan cis-akonitilovanjem i citrakonilovanjem u cilju dobijanja derivata Art v 1 pogodnih za dalje imunološke testove. Acilovanjem Art v 1 dobijeni su derivati (caaArt v 1 i citArt v 1) sa oko 80 % izmodifikovanih amino grupa. Dobijeni derivati su monomerni, sa molekulskom masom sličnom nativnom Art v 1, ali sa dramatično smanjenim pI vrednostima. Oba derivata su relativno stabilna u neutralnoj, dok se u kiseloj sredini acil grupe hidrolizuju. Modifikacija alergena cis-akonitilovanjem i citrakonilovanjem može biti novi način za dobijanje alergoida.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation, Hemijske modifikacije Art v 1, glavnog alergena Artemisia vulgaris, cis-akonitilovanjem i citrakonilovanjem",
volume = "74",
number = "4",
pages = "359-366",
doi = "10.2298/JSC0904359S"
}

Stanić, D., Burazer, L. M., Gavrović-Jankulović, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 74(4), 359-366.
https://doi.org/10.2298/JSC0904359S

Stanić D, Burazer LM, Gavrović-Jankulović M, Jankov RM, Ćirković-Veličković T. Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation. in Journal of the Serbian Chemical Society. 2009;74(4):359-366.
doi:10.2298/JSC0904359S .

Stanić, Dragana, Burazer, Lidija M., Gavrović-Jankulović, Marija, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation" in Journal of the Serbian Chemical Society, 74, no. 4 (2009):359-366,
https://doi.org/10.2298/JSC0904359S . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Radosavljevic, J.
AU  - Polović, Natalija
AU  - Jadranin, Milka
AU  - Popović, M.
AU  - Vuckovic, O.
AU  - Burazer, L.
AU  - Jankov, R.
AU  - Ćirković Veličković, Tanja
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/608
AB  - The use of enzymes may improve the functional properties of various food ingredients. The aim of this study was to examine the effects of proteolytic contaminants in phenol oxidases on β-lactoglobulin (BLG). In the presence of Trametes versicolor laccase and Agaricus bisporus tyrosinase, both variants of BLG (A and B) underwent removal of a peptide from the N-terminus. The truncated forms were more susceptible to digestion by pepsin. The truncation of BLG resulted from contaminating proteases and not due to the action of phenol oxidases. The removal of N-terminal peptides proceeded quickly, while the rest of the globular protein remained resistant to proteolysis for up to 3 h. In the case of the application of enzymes in food bioprocessing, it may be important to carefully monitor the effects of contaminating proteases in enzyme preparations used.
T2  - International Dairy Journal
T1  - Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation
VL  - 19
IS  - 12
SP  - 746
EP  - 752
DO  - 10.1016/j.idairyj.2009.05.008
ER  - 

@article{
author = "Stanić, Dragana and Radosavljevic, J. and Polović, Natalija and Jadranin, Milka and Popović, M. and Vuckovic, O. and Burazer, L. and Jankov, R. and Ćirković Veličković, Tanja",
year = "2009",
abstract = "The use of enzymes may improve the functional properties of various food ingredients. The aim of this study was to examine the effects of proteolytic contaminants in phenol oxidases on β-lactoglobulin (BLG). In the presence of Trametes versicolor laccase and Agaricus bisporus tyrosinase, both variants of BLG (A and B) underwent removal of a peptide from the N-terminus. The truncated forms were more susceptible to digestion by pepsin. The truncation of BLG resulted from contaminating proteases and not due to the action of phenol oxidases. The removal of N-terminal peptides proceeded quickly, while the rest of the globular protein remained resistant to proteolysis for up to 3 h. In the case of the application of enzymes in food bioprocessing, it may be important to carefully monitor the effects of contaminating proteases in enzyme preparations used.",
journal = "International Dairy Journal",
title = "Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation",
volume = "19",
number = "12",
pages = "746-752",
doi = "10.1016/j.idairyj.2009.05.008"
}

Stanić, D., Radosavljevic, J., Polović, N., Jadranin, M., Popović, M., Vuckovic, O., Burazer, L., Jankov, R.,& Ćirković Veličković, T.. (2009). Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation. in International Dairy Journal, 19(12), 746-752.
https://doi.org/10.1016/j.idairyj.2009.05.008

Stanić D, Radosavljevic J, Polović N, Jadranin M, Popović M, Vuckovic O, Burazer L, Jankov R, Ćirković Veličković T. Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation. in International Dairy Journal. 2009;19(12):746-752.
doi:10.1016/j.idairyj.2009.05.008 .

Stanić, Dragana, Radosavljevic, J., Polović, Natalija, Jadranin, Milka, Popović, M., Vuckovic, O., Burazer, L., Jankov, R., Ćirković Veličković, Tanja, "Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation" in International Dairy Journal, 19, no. 12 (2009):746-752,
https://doi.org/10.1016/j.idairyj.2009.05.008 . .

TY  - JOUR
AU  - Perovic, I.
AU  - Milovanovic, M.
AU  - Stanić, Dragana
AU  - Burazer, Lidija M.
AU  - Petrović, D.
AU  - Milčić-Matić, Natalija
AU  - Gafvelin, Guro
AU  - van Hage, Marianne
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4324
AB  - Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.
PB  - Wiley-Blackwell Publishing, Inc, Malden
T2  - Clinical and Experimental Allergy
T1  - Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation
VL  - 39
IS  - 3
SP  - 435
EP  - 446
DO  - 10.1111/j.1365-2222.2008.03158.x
ER  - 

@article{
author = "Perovic, I. and Milovanovic, M. and Stanić, Dragana and Burazer, Lidija M. and Petrović, D. and Milčić-Matić, Natalija and Gafvelin, Guro and van Hage, Marianne and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Clinical and Experimental Allergy",
title = "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation",
volume = "39",
number = "3",
pages = "435-446",
doi = "10.1111/j.1365-2222.2008.03158.x"
}

Perovic, I., Milovanovic, M., Stanić, D., Burazer, L. M., Petrović, D., Milčić-Matić, N., Gafvelin, G., van Hage, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy
Wiley-Blackwell Publishing, Inc, Malden., 39(3), 435-446.
https://doi.org/10.1111/j.1365-2222.2008.03158.x

Perovic I, Milovanovic M, Stanić D, Burazer LM, Petrović D, Milčić-Matić N, Gafvelin G, van Hage M, Jankov RM, Ćirković-Veličković T. Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy. 2009;39(3):435-446.
doi:10.1111/j.1365-2222.2008.03158.x .

Perovic, I., Milovanovic, M., Stanić, Dragana, Burazer, Lidija M., Petrović, D., Milčić-Matić, Natalija, Gafvelin, Guro, van Hage, Marianne, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation" in Clinical and Experimental Allergy, 39, no. 3 (2009):435-446,
https://doi.org/10.1111/j.1365-2222.2008.03158.x . .

TY  - JOUR
AU  - Milosavić, Nenad B.
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan M.
AU  - Vujčić, Zoran
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4264
AB  - We succeeded in the immobilization of 190 mg of periodate oxidized glucoamylase per gram of macroporous polymer. The covalently immobilized enzyme had a specific activity of 1100 U/g. The temperature and pH optimum as well as kinetic parameters were determined. The immobilized enzyme was tested in different types of reactors for hydrolysis of concentrated maltose and starch hydrolysate syrups. The DE value of 98.6, obtained the immobilized enzyme, was slightly higher than that for the soluble form, when acting on 20% substrates.During continuous use in a packed bed reactor over a period of 4 weeks the immobilized enzyme produced 1300 kg of glucose per 1 L of reactor volume without any decrease in its activity.
PB  - Elsevier
T2  - Enzyme and Microbial Technology
T1  - Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)
VL  - 40
IS  - 5
SP  - 1422
EP  - 1426
DO  - 10.1016/j.enzmictec.2006.10.018
ER  - 

@article{
author = "Milosavić, Nenad B. and Prodanović, Radivoje and Jovanović, Slobodan M. and Vujčić, Zoran",
year = "2007",
abstract = "We succeeded in the immobilization of 190 mg of periodate oxidized glucoamylase per gram of macroporous polymer. The covalently immobilized enzyme had a specific activity of 1100 U/g. The temperature and pH optimum as well as kinetic parameters were determined. The immobilized enzyme was tested in different types of reactors for hydrolysis of concentrated maltose and starch hydrolysate syrups. The DE value of 98.6, obtained the immobilized enzyme, was slightly higher than that for the soluble form, when acting on 20% substrates.During continuous use in a packed bed reactor over a period of 4 weeks the immobilized enzyme produced 1300 kg of glucose per 1 L of reactor volume without any decrease in its activity.",
publisher = "Elsevier",
journal = "Enzyme and Microbial Technology",
title = "Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)",
volume = "40",
number = "5",
pages = "1422-1426",
doi = "10.1016/j.enzmictec.2006.10.018"
}

Milosavić, N. B., Prodanović, R., Jovanović, S. M.,& Vujčić, Z.. (2007). Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA). in Enzyme and Microbial Technology
Elsevier., 40(5), 1422-1426.
https://doi.org/10.1016/j.enzmictec.2006.10.018

Milosavić NB, Prodanović R, Jovanović SM, Vujčić Z. Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA). in Enzyme and Microbial Technology. 2007;40(5):1422-1426.
doi:10.1016/j.enzmictec.2006.10.018 .

Milosavić, Nenad B., Prodanović, Radivoje, Jovanović, Slobodan M., Vujčić, Zoran, "Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)" in Enzyme and Microbial Technology, 40, no. 5 (2007):1422-1426,
https://doi.org/10.1016/j.enzmictec.2006.10.018 . .

TY  - JOUR
AU  - Ahmedi, Khaled S. O. H
AU  - Milosavić, Nenad
AU  - Popović, Milica
AU  - Prodanović, Radivoje M.
AU  - Knežević-Jugović, Zorica D.
AU  - Jankov, Ratko M.
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4302
AB  - α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase.
AB  - Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae
T1  - Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae
VL  - 72
IS  - 12
SP  - 1255
EP  - 1263
DO  - 10.2298/JSC0712255A
ER  - 

@article{
author = "Ahmedi, Khaled S. O. H and Milosavić, Nenad and Popović, Milica and Prodanović, Radivoje M. and Knežević-Jugović, Zorica D. and Jankov, Ratko M.",
year = "2007",
abstract = "α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase., Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae, Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae",
volume = "72",
number = "12",
pages = "1255-1263",
doi = "10.2298/JSC0712255A"
}

Ahmedi, K. S. O. H., Milosavić, N., Popović, M., Prodanović, R. M., Knežević-Jugović, Z. D.,& Jankov, R. M.. (2007). Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 72(12), 1255-1263.
https://doi.org/10.2298/JSC0712255A

Ahmedi KSOH, Milosavić N, Popović M, Prodanović RM, Knežević-Jugović ZD, Jankov RM. Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society. 2007;72(12):1255-1263.
doi:10.2298/JSC0712255A .

Ahmedi, Khaled S. O. H, Milosavić, Nenad, Popović, Milica, Prodanović, Radivoje M., Knežević-Jugović, Zorica D., Jankov, Ratko M., "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1255-1263,
https://doi.org/10.2298/JSC0712255A . .