TY  - CONF
AU  - Gligorijević, Nikola
AU  - Lujić, Tamara
AU  - Mutić, Tamara
AU  - Vasović, Tamara
AU  - de Guzman, Maria Krishna
AU  - Aćimović, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6898
AB  - Ovalbumin (OVA), a main protein of egg white, has characteristic structural fold of a
serpin-family of proteins, propensity to fibril formation and stability to digestion.
Microplastics (MPs) contaminating our food can interact with food proteins in the food
matrix and during digestion. In this study adsorption of OVA to polystyrene (PS) (110 μm
and 260 μm), polyethylene terephthalate (PET) (140 μm) MPs were investigated in acidic
(pH 3) and neutral (pH 7) conditions. Formations of corona on MPs were investigated
using isolated OVA and egg white protein extract comparatively. OVA adsorption depends
on MPs size, polymer chemistry and pH, being highest in acidic pH and higher for PS.
Adsorption of OVA to PS and PET reaches dynamic equilibrium after 4h resulting in
disruption of tertiary structure and formation of hard and soft corona around MPs. Shorter
fragments of OVA populate hard corona, while soft corona exclusively consist of full
length OVA, albeit in its non-native conformation. The conformational changes resemble
those induced by heat treatment with re-arrangement of α-β secondary structures.
Structural changes are striking for the OVA in corona around MPs. Soft corona OVA
preserves thermal and proteolytic stability, but loses ability to form fibrils upon heating.
OVA is abundantly present in corona around MPs also in the presence of other egg white
proteins. MPs contaminating food may bind and change structure and functional properties
of main egg white protein.
PB  - Kragujevac, Srbija : Prirodno-matematički fakultet, Univerzitet u Kragujevcu /  Kragujevac, Serbia : Faculty of Science, University of Kragujevac
C3  - VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs,
T1  - Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate
SP  - OP10
EP  - OP10
UR  - https://hdl.handle.net/21.15107/rcub_cer_6898
ER  - 

@conference{
author = "Gligorijević, Nikola and Lujić, Tamara and Mutić, Tamara and Vasović, Tamara and de Guzman, Maria Krishna and Aćimović, Jelena and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2023",
abstract = "Ovalbumin (OVA), a main protein of egg white, has characteristic structural fold of a
serpin-family of proteins, propensity to fibril formation and stability to digestion.
Microplastics (MPs) contaminating our food can interact with food proteins in the food
matrix and during digestion. In this study adsorption of OVA to polystyrene (PS) (110 μm
and 260 μm), polyethylene terephthalate (PET) (140 μm) MPs were investigated in acidic
(pH 3) and neutral (pH 7) conditions. Formations of corona on MPs were investigated
using isolated OVA and egg white protein extract comparatively. OVA adsorption depends
on MPs size, polymer chemistry and pH, being highest in acidic pH and higher for PS.
Adsorption of OVA to PS and PET reaches dynamic equilibrium after 4h resulting in
disruption of tertiary structure and formation of hard and soft corona around MPs. Shorter
fragments of OVA populate hard corona, while soft corona exclusively consist of full
length OVA, albeit in its non-native conformation. The conformational changes resemble
those induced by heat treatment with re-arrangement of α-β secondary structures.
Structural changes are striking for the OVA in corona around MPs. Soft corona OVA
preserves thermal and proteolytic stability, but loses ability to form fibrils upon heating.
OVA is abundantly present in corona around MPs also in the presence of other egg white
proteins. MPs contaminating food may bind and change structure and functional properties
of main egg white protein.",
publisher = "Kragujevac, Srbija : Prirodno-matematički fakultet, Univerzitet u Kragujevcu /  Kragujevac, Serbia : Faculty of Science, University of Kragujevac",
journal = "VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs,",
title = "Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate",
pages = "OP10-OP10",
url = "https://hdl.handle.net/21.15107/rcub_cer_6898"
}

Gligorijević, N., Lujić, T., Mutić, T., Vasović, T., de Guzman, M. K., Aćimović, J., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2023). Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate. in VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs,
Kragujevac, Srbija : Prirodno-matematički fakultet, Univerzitet u Kragujevcu /  Kragujevac, Serbia : Faculty of Science, University of Kragujevac., OP10-OP10.
https://hdl.handle.net/21.15107/rcub_cer_6898

Gligorijević N, Lujić T, Mutić T, Vasović T, de Guzman MK, Aćimović J, Stanić-Vučinić D, Ćirković Veličković T. Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate. in VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs,. 2023;:OP10-OP10.
https://hdl.handle.net/21.15107/rcub_cer_6898 .

Gligorijević, Nikola, Lujić, Tamara, Mutić, Tamara, Vasović, Tamara, de Guzman, Maria Krishna, Aćimović, Jelena, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate" in VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs, (2023):OP10-OP10,
https://hdl.handle.net/21.15107/rcub_cer_6898 .

TY  - CONF
AU  - Lujić, Tamara
AU  - Gligorijević, Nikola
AU  - Jovanović, Vesna B.
AU  - Aćimović, Jelena
AU  - Mitić, Dragana
AU  - Vasović, Tamara
AU  - Stojadinović, Marija
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7473
AB  - Microplastics is abundant in the environment, food and beverages and get ingested by humans.
Its complex interplay with proteins lead to formation of corona. Tightly bound proteins represent
hard corona, while weaker binding partners are found in soft corona. Separation of hard and soft
corona of allergenic proteins of shrimps, eggs and cow’s milk, tropomyosin (TPM), ovalbumin
(OVA) and beta-lactoglobulin (BLG) and identification of binding partners by proteomics was
aim of our study.
Allergenic proteins were purified from egg white, shrimps and cow’s milk. Binding to
polyethylene terephthalate microplastics (PET) (70-100 m) was probed at pH 7 for purified
allergens and egg white proteins. After establishment of binding equilibrium, soft and hard
corona were separated and analyzed by SDS PAGE, followed by identification of bound
proteins by nanoLC-HRMS. Binding of all allergenic proteins was observed in both soft and
hard corona. Soft corona contains exclusively intact, full length OVA, TPM and BLG. Hard
corona is enriched for truncated OVA and oligomers of TPM. OVA fragments are partially or
fully enfolded and have higher level of exposed hydrophobic patches resulting in higher affinity
for PET microplastics. In comparison to OVA and TPM, hard corona of BLG is less abundant
under similar conditions. BLG is compact globular protein with lower level of exposed
hydrophobic patches in comparison to ovalbumin and tropomyosin. In hard corona, trace
amounts of contaminating alfa-lactalbumin become enriched. In the presence of egg white
protein extract OVA forms both SC and HC on microplastics, being the dominant protein of
hard corona (with ovotransferrin). Lysozyme and ovomucin are present only in hard corona.
Both proteins are known for their strong bioactivity and represent a small fraction of total egg
white proteins.
Our results show that allergenic proteins form hard corona on PET microplastics. Among egg
white proteins, minor proteins such as lysozyme and ovomucin become enriched. Denaturing
effect of strong binding to microplastics may change functional characteristics of allergens and
bioactive proteins of foods and should be further investigated in functional assays.
PB  - Italian Proteomics Association
C3  - XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy
T1  - Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics
SP  - 11
EP  - 11
UR  - https://hdl.handle.net/21.15107/rcub_cer_7473
ER  - 

@conference{
author = "Lujić, Tamara and Gligorijević, Nikola and Jovanović, Vesna B. and Aćimović, Jelena and Mitić, Dragana and Vasović, Tamara and Stojadinović, Marija and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "Microplastics is abundant in the environment, food and beverages and get ingested by humans.
Its complex interplay with proteins lead to formation of corona. Tightly bound proteins represent
hard corona, while weaker binding partners are found in soft corona. Separation of hard and soft
corona of allergenic proteins of shrimps, eggs and cow’s milk, tropomyosin (TPM), ovalbumin
(OVA) and beta-lactoglobulin (BLG) and identification of binding partners by proteomics was
aim of our study.
Allergenic proteins were purified from egg white, shrimps and cow’s milk. Binding to
polyethylene terephthalate microplastics (PET) (70-100 m) was probed at pH 7 for purified
allergens and egg white proteins. After establishment of binding equilibrium, soft and hard
corona were separated and analyzed by SDS PAGE, followed by identification of bound
proteins by nanoLC-HRMS. Binding of all allergenic proteins was observed in both soft and
hard corona. Soft corona contains exclusively intact, full length OVA, TPM and BLG. Hard
corona is enriched for truncated OVA and oligomers of TPM. OVA fragments are partially or
fully enfolded and have higher level of exposed hydrophobic patches resulting in higher affinity
for PET microplastics. In comparison to OVA and TPM, hard corona of BLG is less abundant
under similar conditions. BLG is compact globular protein with lower level of exposed
hydrophobic patches in comparison to ovalbumin and tropomyosin. In hard corona, trace
amounts of contaminating alfa-lactalbumin become enriched. In the presence of egg white
protein extract OVA forms both SC and HC on microplastics, being the dominant protein of
hard corona (with ovotransferrin). Lysozyme and ovomucin are present only in hard corona.
Both proteins are known for their strong bioactivity and represent a small fraction of total egg
white proteins.
Our results show that allergenic proteins form hard corona on PET microplastics. Among egg
white proteins, minor proteins such as lysozyme and ovomucin become enriched. Denaturing
effect of strong binding to microplastics may change functional characteristics of allergens and
bioactive proteins of foods and should be further investigated in functional assays.",
publisher = "Italian Proteomics Association",
journal = "XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy",
title = "Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics",
pages = "11-11",
url = "https://hdl.handle.net/21.15107/rcub_cer_7473"
}

Lujić, T., Gligorijević, N., Jovanović, V. B., Aćimović, J., Mitić, D., Vasović, T., Stojadinović, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2023). Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics. in XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy
Italian Proteomics Association., 11-11.
https://hdl.handle.net/21.15107/rcub_cer_7473

Lujić T, Gligorijević N, Jovanović VB, Aćimović J, Mitić D, Vasović T, Stojadinović M, Stanić-Vučinić D, Ćirković-Veličković T. Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics. in XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy. 2023;:11-11.
https://hdl.handle.net/21.15107/rcub_cer_7473 .

Lujić, Tamara, Gligorijević, Nikola, Jovanović, Vesna B., Aćimović, Jelena, Mitić, Dragana, Vasović, Tamara, Stojadinović, Marija, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics" in XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy (2023):11-11,
https://hdl.handle.net/21.15107/rcub_cer_7473 .

TY  - JOUR
AU  - Aćimović, Jelena M.
AU  - Stanimirovic, Bojana D.
AU  - Todorović, Nina
AU  - Jovanović, Vesna B.
AU  - Mandić, Ljuba M.
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/719
AB  - Methylglyoxal (MG), a reactive alpha-oxoaldehyde that is produced in higher quantities in diabetes, uremia, oxidative stress, aging and inflammation, reacts with the thiol groups (in addition to the amino and guanidino groups) of proteins. This causes protein modification, formation of advanced glycated end products (AGEs) and cross-linking. Low molecular mass thiols can be used as competitive targets for MG, preventing the reactions mentioned above. Therefore, this paper investigated how the microenvironment of the thiol group in low molecular mass thiols (cysteine, N-acetylcysteine (NAcCys), carboxymethylcysteine (CMC) and glutathione (GSH)) and human serum albumin (HSA) affected the thiol reaction with MG. The SH group reaction course was monitored by H-1-NMR spectroscopy and spectrophotometric quantification. Changes in the HSA molecules were monitored by SDS-PAGE. The microenvironment of the SH group had a major effect on its reactivity and on the product yield. The reactivity of SH groups decreased in the order Cys > GSH > NAcCys. CMC did not react. The percentages of the reacted SH groups in the equilibrium state were almost equal, regardless of the ratio of thiol compound/MG (1:1, 1:2, 1:5): 38.1 +/- 0.9%; 38.2 +/- 0.7% and 39.0 +/- 0.8% for Cys; 26.5 +/- 0.6%; 26.6 +/- 2.6% and 27.4 +/- 2.5% for GSH; 10.8 +/- 0.9%; and 11.2 +/- 0.7% and 12.2 +/- 0.9% for NAcCys, respectively. Our results explain why substances containing alpha-amino-beta-mercapto-ethane as a pharmacophore are successful scavengers of MG. In equilibrium, HSA SH reacted in high percentages both with an insufficient amount and with an excess of MG (55% and 65%, respectively). An analysis of the hydrophobicity of the microenvironment of the SH group on the HSA surface showed that it could contribute to high levels of SH modification, leading to an increase in the scavenging activity of the albumin thiol.
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-Biological Interactions
T1  - Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal
VL  - 188
IS  - 1
SP  - 21
EP  - 30
DO  - 10.1016/j.cbi.2010.07.013
ER  - 

@article{
author = "Aćimović, Jelena M. and Stanimirovic, Bojana D. and Todorović, Nina and Jovanović, Vesna B. and Mandić, Ljuba M.",
year = "2010",
abstract = "Methylglyoxal (MG), a reactive alpha-oxoaldehyde that is produced in higher quantities in diabetes, uremia, oxidative stress, aging and inflammation, reacts with the thiol groups (in addition to the amino and guanidino groups) of proteins. This causes protein modification, formation of advanced glycated end products (AGEs) and cross-linking. Low molecular mass thiols can be used as competitive targets for MG, preventing the reactions mentioned above. Therefore, this paper investigated how the microenvironment of the thiol group in low molecular mass thiols (cysteine, N-acetylcysteine (NAcCys), carboxymethylcysteine (CMC) and glutathione (GSH)) and human serum albumin (HSA) affected the thiol reaction with MG. The SH group reaction course was monitored by H-1-NMR spectroscopy and spectrophotometric quantification. Changes in the HSA molecules were monitored by SDS-PAGE. The microenvironment of the SH group had a major effect on its reactivity and on the product yield. The reactivity of SH groups decreased in the order Cys > GSH > NAcCys. CMC did not react. The percentages of the reacted SH groups in the equilibrium state were almost equal, regardless of the ratio of thiol compound/MG (1:1, 1:2, 1:5): 38.1 +/- 0.9%; 38.2 +/- 0.7% and 39.0 +/- 0.8% for Cys; 26.5 +/- 0.6%; 26.6 +/- 2.6% and 27.4 +/- 2.5% for GSH; 10.8 +/- 0.9%; and 11.2 +/- 0.7% and 12.2 +/- 0.9% for NAcCys, respectively. Our results explain why substances containing alpha-amino-beta-mercapto-ethane as a pharmacophore are successful scavengers of MG. In equilibrium, HSA SH reacted in high percentages both with an insufficient amount and with an excess of MG (55% and 65%, respectively). An analysis of the hydrophobicity of the microenvironment of the SH group on the HSA surface showed that it could contribute to high levels of SH modification, leading to an increase in the scavenging activity of the albumin thiol.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-Biological Interactions",
title = "Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal",
volume = "188",
number = "1",
pages = "21-30",
doi = "10.1016/j.cbi.2010.07.013"
}

Aćimović, J. M., Stanimirovic, B. D., Todorović, N., Jovanović, V. B.,& Mandić, L. M.. (2010). Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal. in Chemico-Biological Interactions
Elsevier Ireland Ltd, Clare., 188(1), 21-30.
https://doi.org/10.1016/j.cbi.2010.07.013

Aćimović JM, Stanimirovic BD, Todorović N, Jovanović VB, Mandić LM. Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal. in Chemico-Biological Interactions. 2010;188(1):21-30.
doi:10.1016/j.cbi.2010.07.013 .

Aćimović, Jelena M., Stanimirovic, Bojana D., Todorović, Nina, Jovanović, Vesna B., Mandić, Ljuba M., "Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal" in Chemico-Biological Interactions, 188, no. 1 (2010):21-30,
https://doi.org/10.1016/j.cbi.2010.07.013 . .

TY  - CONF
AU  - Ivanovska, J.
AU  - Mladenović, S.
AU  - Nastasijević, B.
AU  - Miletić, Srđan
AU  - Aćimović, Jelena M.
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5127
AB  - The chemical composition of malt is of crucial importance for wort quality and together with conditions of fermentation process, they determine beer quality. Commercial enzymes preparations compensate enzymes naturally present in the malt. As substitutes for malt, originally made from malted barley, we used corn grits, rice and unmalted barley mixtures as adjunct for wort, and Ceremix and Termamil enzyme preparations (microbial origin). Wort quality was monitored by following parameters: filterability speed, a-amino-nitrogen, total sugars, and degree of saccharification. Beer quality is assessed, beside usual parameters, by presence and levels
of highly volatile alcohol and esters, such as 3-methyl butanol, 1-propanol, phenyl ethanol and ethyl acetate that dictate flavour and taste of beer. Higher values of these substances were found in all samples of wort supplemented with enzymes, in comparison with those without adding of Termamyl and Ceremix. Although these preparations increase efficiency of saccarification process,
their usage concomitantly with enzymes from malt leads to elevation of substances that negatively contribute to beer flavour and taste. Addition of these enzyme preparations meets requests for
good beer quality wherever enzymes from malt are not present in sufficient quantity. For optimal results 0.5% of Termamyl and Ceremix should be added, while in all other cases where malted
substance is present with at least 50%, their usage should be strictly controlled.
PB  - Blackwell Publishing
C3  - FEBS Journal
T1  - Efficiency of commercial enzymatic preparations in grain hydrolysis for preparation of substrates for beer fermentation
VL  - 274
SP  - 224
UR  - https://hdl.handle.net/21.15107/rcub_cer_5127
ER  - 

@conference{
author = "Ivanovska, J. and Mladenović, S. and Nastasijević, B. and Miletić, Srđan and Aćimović, Jelena M.",
year = "2007",
abstract = "The chemical composition of malt is of crucial importance for wort quality and together with conditions of fermentation process, they determine beer quality. Commercial enzymes preparations compensate enzymes naturally present in the malt. As substitutes for malt, originally made from malted barley, we used corn grits, rice and unmalted barley mixtures as adjunct for wort, and Ceremix and Termamil enzyme preparations (microbial origin). Wort quality was monitored by following parameters: filterability speed, a-amino-nitrogen, total sugars, and degree of saccharification. Beer quality is assessed, beside usual parameters, by presence and levels
of highly volatile alcohol and esters, such as 3-methyl butanol, 1-propanol, phenyl ethanol and ethyl acetate that dictate flavour and taste of beer. Higher values of these substances were found in all samples of wort supplemented with enzymes, in comparison with those without adding of Termamyl and Ceremix. Although these preparations increase efficiency of saccarification process,
their usage concomitantly with enzymes from malt leads to elevation of substances that negatively contribute to beer flavour and taste. Addition of these enzyme preparations meets requests for
good beer quality wherever enzymes from malt are not present in sufficient quantity. For optimal results 0.5% of Termamyl and Ceremix should be added, while in all other cases where malted
substance is present with at least 50%, their usage should be strictly controlled.",
publisher = "Blackwell Publishing",
journal = "FEBS Journal",
title = "Efficiency of commercial enzymatic preparations in grain hydrolysis for preparation of substrates for beer fermentation",
volume = "274",
pages = "224",
url = "https://hdl.handle.net/21.15107/rcub_cer_5127"
}

Ivanovska, J., Mladenović, S., Nastasijević, B., Miletić, S.,& Aćimović, J. M.. (2007). Efficiency of commercial enzymatic preparations in grain hydrolysis for preparation of substrates for beer fermentation. in FEBS Journal
Blackwell Publishing., 274, 224.
https://hdl.handle.net/21.15107/rcub_cer_5127

Ivanovska J, Mladenović S, Nastasijević B, Miletić S, Aćimović JM. Efficiency of commercial enzymatic preparations in grain hydrolysis for preparation of substrates for beer fermentation. in FEBS Journal. 2007;274:224.
https://hdl.handle.net/21.15107/rcub_cer_5127 .

Ivanovska, J., Mladenović, S., Nastasijević, B., Miletić, Srđan, Aćimović, Jelena M., "Efficiency of commercial enzymatic preparations in grain hydrolysis for preparation of substrates for beer fermentation" in FEBS Journal, 274 (2007):224,
https://hdl.handle.net/21.15107/rcub_cer_5127 .