TY  - JOUR
AU  - Zelenović, Nevena
AU  - Kojadinovic, Milica
AU  - Filipović, Lidija
AU  - Vucic, Vesna
AU  - Milčić, Miloš
AU  - Arsić, Aleksndra
AU  - Popović, Milica
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7223
AB  - Backgound/Objectives Urolithins (UROs) are the metabolites derived from the gut microbial action on ellagitannins and ellagic acid-rich foods. Following their absorption in the intestine, UROs are transported through the systemic circulation to various tissues where they can express their biological function as antimicrobial, anti-inflammatory, and anticancer agents. In addition to blood plasma, where they can be found as glucuronide and sulfate conjugates, they are also found in urine. Therefore, the interactions of UROs with serum proteins are of great clinical interest. Methods A powerful technique for examining these urolithin-serum protein interactions is fluorescence spectroscopy. Bovine serum albumin (BSA) is a particularly suitable model protein because it is readily available, affordable, and similar to human serum albumin. This work aimed to study the binding of UROs (urolithin A, UROA and urolithin B, UROB) and their glucuronide conjugates (UROAG and UROBG) to BSA by quenching the intrinsic fluorescence of protein. Results The spectra obtained showed that the binding process is influenced by the polyphenol's structure and the conjugation process with the glucuronide. The calculated Stern Vollmer binding constants (Ksv): UROA and UROB Ksv were 59236   ±   5706 and 69653   ±   14922, respectively, while for UROAG and UROBG, these values were 15179   ±   2770 and 9462   ±   1955, respectively, which showed that the binding affinity decreased with glucuronidation. Molecular docking studies confirmed that all of the studied molecules will bind favorably to BSA. The preferential binding site for both UROs and UROGs is Sudlow I, while UROs will also bind to Sudlow II. URO-Gs can bind to BSA in the cleft region with lower binding scores than for the Sudlow I binding site. Conclusion The aglycone's higher hydrophobicity increases the binding affinity to BSA, thus reducing its bioavailability in the blood.
PB  - SAGE Publications
T2  - Natural Product Communications
T1  - Interactions of Different Urolithins With Bovine Serum Albumin
VL  - 18
IS  - 5
SP  - 1934578X2311693
DO  - 10.1177/1934578X231169366
ER  - 

@article{
author = "Zelenović, Nevena and Kojadinovic, Milica and Filipović, Lidija and Vucic, Vesna and Milčić, Miloš and Arsić, Aleksndra and Popović, Milica",
year = "2023",
abstract = "Backgound/Objectives Urolithins (UROs) are the metabolites derived from the gut microbial action on ellagitannins and ellagic acid-rich foods. Following their absorption in the intestine, UROs are transported through the systemic circulation to various tissues where they can express their biological function as antimicrobial, anti-inflammatory, and anticancer agents. In addition to blood plasma, where they can be found as glucuronide and sulfate conjugates, they are also found in urine. Therefore, the interactions of UROs with serum proteins are of great clinical interest. Methods A powerful technique for examining these urolithin-serum protein interactions is fluorescence spectroscopy. Bovine serum albumin (BSA) is a particularly suitable model protein because it is readily available, affordable, and similar to human serum albumin. This work aimed to study the binding of UROs (urolithin A, UROA and urolithin B, UROB) and their glucuronide conjugates (UROAG and UROBG) to BSA by quenching the intrinsic fluorescence of protein. Results The spectra obtained showed that the binding process is influenced by the polyphenol's structure and the conjugation process with the glucuronide. The calculated Stern Vollmer binding constants (Ksv): UROA and UROB Ksv were 59236   ±   5706 and 69653   ±   14922, respectively, while for UROAG and UROBG, these values were 15179   ±   2770 and 9462   ±   1955, respectively, which showed that the binding affinity decreased with glucuronidation. Molecular docking studies confirmed that all of the studied molecules will bind favorably to BSA. The preferential binding site for both UROs and UROGs is Sudlow I, while UROs will also bind to Sudlow II. URO-Gs can bind to BSA in the cleft region with lower binding scores than for the Sudlow I binding site. Conclusion The aglycone's higher hydrophobicity increases the binding affinity to BSA, thus reducing its bioavailability in the blood.",
publisher = "SAGE Publications",
journal = "Natural Product Communications",
title = "Interactions of Different Urolithins With Bovine Serum Albumin",
volume = "18",
number = "5",
pages = "1934578X2311693",
doi = "10.1177/1934578X231169366"
}

Zelenović, N., Kojadinovic, M., Filipović, L., Vucic, V., Milčić, M., Arsić, A.,& Popović, M.. (2023). Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications
SAGE Publications., 18(5), 1934578X2311693.
https://doi.org/10.1177/1934578X231169366

Zelenović N, Kojadinovic M, Filipović L, Vucic V, Milčić M, Arsić A, Popović M. Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications. 2023;18(5):1934578X2311693.
doi:10.1177/1934578X231169366 .

Zelenović, Nevena, Kojadinovic, Milica, Filipović, Lidija, Vucic, Vesna, Milčić, Miloš, Arsić, Aleksndra, Popović, Milica, "Interactions of Different Urolithins With Bovine Serum Albumin" in Natural Product Communications, 18, no. 5 (2023):1934578X2311693,
https://doi.org/10.1177/1934578X231169366 . .

TY  - JOUR
AU  - Zelenović, Nevena
AU  - Filipović, Lidija
AU  - Popović, Milica
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7216
AB  - Biotechnological and biomedical applications of antibodies have been on a steady rise since the 1980s. As unique and highly specific bioreagents, monoclonal antibodies (mAbs) have been widely exploited and approved as therapeutic agents. However, the use of mAbs has limitations for therapeutic applications. Antibody fragments (AbFs) with preserved antigen-binding sites have a significant potential to overcome the disadvantages of conventional mAbs, such as heterogeneous tissue distribution after systemic administration, especially in solid tumors, and Fc-mediated bystander activation of the immune system. AbFs possess better biodistribution coefficient due to lower molecular weight. They preserve the functional features of mAbs, such as antigen specificity and binding, while at the same time, ensuring much better tissue penetration. An additional benefit of AbFs is the possibility of their production in bacterial and yeast cells due to the small size, more robust structure, and lack of posttranslational modifications. In this review, we described current approaches to the AbF production with recent examples of AbF synthesis in bacterial and yeast expression systems and methods for the production optimization.
PB  - Springer
T2  - Biochemistry (Moscow)
T1  - Recent Developments in Bioprocessing of Recombinant Antibody Fragments
VL  - 88
IS  - 9
SP  - 1191
EP  - 1204
DO  - 10.1134/S0006297923090018
ER  - 

@article{
author = "Zelenović, Nevena and Filipović, Lidija and Popović, Milica",
year = "2023",
abstract = "Biotechnological and biomedical applications of antibodies have been on a steady rise since the 1980s. As unique and highly specific bioreagents, monoclonal antibodies (mAbs) have been widely exploited and approved as therapeutic agents. However, the use of mAbs has limitations for therapeutic applications. Antibody fragments (AbFs) with preserved antigen-binding sites have a significant potential to overcome the disadvantages of conventional mAbs, such as heterogeneous tissue distribution after systemic administration, especially in solid tumors, and Fc-mediated bystander activation of the immune system. AbFs possess better biodistribution coefficient due to lower molecular weight. They preserve the functional features of mAbs, such as antigen specificity and binding, while at the same time, ensuring much better tissue penetration. An additional benefit of AbFs is the possibility of their production in bacterial and yeast cells due to the small size, more robust structure, and lack of posttranslational modifications. In this review, we described current approaches to the AbF production with recent examples of AbF synthesis in bacterial and yeast expression systems and methods for the production optimization.",
publisher = "Springer",
journal = "Biochemistry (Moscow)",
title = "Recent Developments in Bioprocessing of Recombinant Antibody Fragments",
volume = "88",
number = "9",
pages = "1191-1204",
doi = "10.1134/S0006297923090018"
}

Zelenović, N., Filipović, L.,& Popović, M.. (2023). Recent Developments in Bioprocessing of Recombinant Antibody Fragments. in Biochemistry (Moscow)
Springer., 88(9), 1191-1204.
https://doi.org/10.1134/S0006297923090018

Zelenović N, Filipović L, Popović M. Recent Developments in Bioprocessing of Recombinant Antibody Fragments. in Biochemistry (Moscow). 2023;88(9):1191-1204.
doi:10.1134/S0006297923090018 .

Zelenović, Nevena, Filipović, Lidija, Popović, Milica, "Recent Developments in Bioprocessing of Recombinant Antibody Fragments" in Biochemistry (Moscow), 88, no. 9 (2023):1191-1204,
https://doi.org/10.1134/S0006297923090018 . .

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Zelenović, Nevena
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3028
AB  - Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.
PB  - Springer
T2  - Macromolecular Research
T1  - Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation
VL  - 27
IS  - 8
SP  - 764
EP  - 771
DO  - 10.1007/s13233-019-7111-7
ER  - 

@article{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Zelenović, Nevena and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2019",
abstract = "Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.",
publisher = "Springer",
journal = "Macromolecular Research",
title = "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation",
volume = "27",
number = "8",
pages = "764-771",
doi = "10.1007/s13233-019-7111-7"
}

Spasojević, D., Prokopijević, M., Prodanović, O., Zelenović, N., Polović, N., Radotić, K.,& Prodanović, R.. (2019). Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research
Springer., 27(8), 764-771.
https://doi.org/10.1007/s13233-019-7111-7

Spasojević D, Prokopijević M, Prodanović O, Zelenović N, Polović N, Radotić K, Prodanović R. Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research. 2019;27(8):764-771.
doi:10.1007/s13233-019-7111-7 .

Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Zelenović, Nevena, Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation" in Macromolecular Research, 27, no. 8 (2019):764-771,
https://doi.org/10.1007/s13233-019-7111-7 . .

TY  - JOUR
AU  - Tadić, Vojin
AU  - Balaž, Ana Marija
AU  - Petrić, Marija
AU  - Milošević, Snežana M.
AU  - Zelenović, Nevena
AU  - Raspor, Martin Z.
AU  - Tadić, Jovan
AU  - Prodanović, Radivoje
PY  - 2015
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1644
AB  - We have cloned the gene for carbohydrate oxidase (CHO) from Lactuca sativa in two species of yeasts (Saccharomyces cerevisiae and Pichia pastoris). The synthetic gene Department for Plant Physiology, Institute for Biological Research 'Siniša Stanković', drate oxidase (1821 bp) from L. sativa cloned into the vector pUC57 and inserted into plasmids pYES2 and pGAP using Escherichia coli DH5α strain. The P. pastoris strain X-33 and the S. cerevisiae strain InvSC1 were used for extracellular expression of CHO. After transformation of P. pastoris X-33 with CHO-pGAP construct none of the colonies showed CHO activity. Two samples displayed a band which did not exist in the sample with the empty vector similar to the molecular weight of CHO. The S. cerevisiae stran InvSC1 has been also transformed with CHO-pYES constructs. Three colonies grew on the plate with cells transformed with the construct. One of the samples showed a band corresponding to about 110 kDa, but no CHO activity was recorded in this case either. Cloning of the foreign genes and heterologous expression in yeasts is widely used in biotechnology, but sometimes can be very dependent on the gene sequence and strain used. In order to obtain active CHO enzyme the further studies on purification and refolding of expressed protein are necessary.
AB  - Ugljeni hidrat-oksidaza (CHO) iz zelene salate (Lactuca sativa) je enzim koji je do danas nedovoljno ispitan. Vrlo se malo zna o njegovoj strukturi i funkciji. CHO pripada velikoj familiji ugljenihidrat-oksidaza, koje oksiduju šećere. Svaki od članova ove velike familije dobio je ime po supstratu koji oksiduje. Oksidaze iz ove familije enzima imaju kako sličnu ulogu tako i sličnu strukutru. Sve ili većina ovih enzima su monomeri, čiji se polipeptidni lanac uvija u dva domena. Jedan od domena vezuje flavinski kofaktor, a drugi domen je supstrat vezujući. Većina njih oksidaciju supstrata vrši po takozvanom ping-pong mehanizmu. Sve oksidaze iz karbohidrat-oksidaza familije, pa među njima i enzim koji je predmet ove studije (CHO), danas su našle veliku primenu u industriji. CHO se može primenjivati kako u medicinskoj djagnostici, konkretno u biosenzorima za određivanje glukoze u krvi, u prehrambenoj industriji, poljoprivredi, proizvodnji hleba, deterdženata i u raznim drugim industrijskim oblastima. Problem sa ovim enzimom, kao i sa ostalim članovima ove familije, jeste niska koncentracija u prirodnim izvorima. Zato su danas razvijene različite metode rekombinantne tehnologije, kojima se dobijaju ovi enzimi. U ovom radu opisano je kloniranje gena za CHO iz zelene salate u dve vrste kvasaca (Saccharomyces cerevisiae i Pichia pastoris). Sintetički gen za CHO (1821 bp) iz zelene salate kloniran je u vektor pUC57. Escherichia coli soj DH5α korišćen je za kloniranje gena i održavanje plazmida. P. pastoris soj X-33 i S. cerevisiae soj InvSC1 korišćeni su za ekstracelularnu ekspresiju CHO. Aktivnost CHO određena je ABST esejom, a promena absorbance merena je na 405 nm. Potvrda prisustva enzima rađena je na DNK agaroznoj elektroforezi i SDS-PAGE. Posle transformacije P. pastoris X-33, nijedan od klonova nije pokazivao aktivnost CHO. Posle prve fermentacije, kolonije su testirane na SDS-PAGE. Kako su dva uzorka pokazala trake, koje ne postoje na praznom vektoru, ove trake bi mogle odgovarati željenom enzimu, CHO. Traka se nalazi na molekulskoj masi koja je veća od teoretske (više od 120 kDa). Enzim bi mogao biti glikolizovan i zbog toga pokazivati ovako velike vrednosti za molekulsku masu. S. cerevisiae soj InvSC1 transformisan je konstruktom CHO-pZES. Posle 24 sata, tri kolonije su porasle na ploči na kojoj su bile ćelije transformisane pomenutim konstruktom. Uzorci su testirani na SDS-PAGE. Jedan uzorak je pokazao traku na oko 110 kDa, ali aktivnost CHO nije potvrđena takođe. Cilj ove studije je bio kloniranje CHO u kvascima S. cerevisiae i P. pastoris, kao i njena ekspresija u ovim, danas široko primenjivanim ekspresionim sistemima.
PB  - Assoc Chemical Engineers Serbia, Belgrade
T2  - Hemijska industrija
T1  - Cloning of the gene for a carbohydrate oxidase from Lactuca sativa in the yeasts Saccharomyces cerevisiae and Pichia pastoris
T1  - Kloniranje gena za ugljeni hidrat oksidazu iz biljke Lactuca sativa u kvasce saccharomyces cerevisiae i Pichia pastoris
VL  - 69
IS  - 6
SP  - 689
EP  - 701
DO  - 10.2298/HEMIND140823003T
ER  - 

@article{
author = "Tadić, Vojin and Balaž, Ana Marija and Petrić, Marija and Milošević, Snežana M. and Zelenović, Nevena and Raspor, Martin Z. and Tadić, Jovan and Prodanović, Radivoje",
year = "2015",
abstract = "We have cloned the gene for carbohydrate oxidase (CHO) from Lactuca sativa in two species of yeasts (Saccharomyces cerevisiae and Pichia pastoris). The synthetic gene Department for Plant Physiology, Institute for Biological Research 'Siniša Stanković', drate oxidase (1821 bp) from L. sativa cloned into the vector pUC57 and inserted into plasmids pYES2 and pGAP using Escherichia coli DH5α strain. The P. pastoris strain X-33 and the S. cerevisiae strain InvSC1 were used for extracellular expression of CHO. After transformation of P. pastoris X-33 with CHO-pGAP construct none of the colonies showed CHO activity. Two samples displayed a band which did not exist in the sample with the empty vector similar to the molecular weight of CHO. The S. cerevisiae stran InvSC1 has been also transformed with CHO-pYES constructs. Three colonies grew on the plate with cells transformed with the construct. One of the samples showed a band corresponding to about 110 kDa, but no CHO activity was recorded in this case either. Cloning of the foreign genes and heterologous expression in yeasts is widely used in biotechnology, but sometimes can be very dependent on the gene sequence and strain used. In order to obtain active CHO enzyme the further studies on purification and refolding of expressed protein are necessary., Ugljeni hidrat-oksidaza (CHO) iz zelene salate (Lactuca sativa) je enzim koji je do danas nedovoljno ispitan. Vrlo se malo zna o njegovoj strukturi i funkciji. CHO pripada velikoj familiji ugljenihidrat-oksidaza, koje oksiduju šećere. Svaki od članova ove velike familije dobio je ime po supstratu koji oksiduje. Oksidaze iz ove familije enzima imaju kako sličnu ulogu tako i sličnu strukutru. Sve ili većina ovih enzima su monomeri, čiji se polipeptidni lanac uvija u dva domena. Jedan od domena vezuje flavinski kofaktor, a drugi domen je supstrat vezujući. Većina njih oksidaciju supstrata vrši po takozvanom ping-pong mehanizmu. Sve oksidaze iz karbohidrat-oksidaza familije, pa među njima i enzim koji je predmet ove studije (CHO), danas su našle veliku primenu u industriji. CHO se može primenjivati kako u medicinskoj djagnostici, konkretno u biosenzorima za određivanje glukoze u krvi, u prehrambenoj industriji, poljoprivredi, proizvodnji hleba, deterdženata i u raznim drugim industrijskim oblastima. Problem sa ovim enzimom, kao i sa ostalim članovima ove familije, jeste niska koncentracija u prirodnim izvorima. Zato su danas razvijene različite metode rekombinantne tehnologije, kojima se dobijaju ovi enzimi. U ovom radu opisano je kloniranje gena za CHO iz zelene salate u dve vrste kvasaca (Saccharomyces cerevisiae i Pichia pastoris). Sintetički gen za CHO (1821 bp) iz zelene salate kloniran je u vektor pUC57. Escherichia coli soj DH5α korišćen je za kloniranje gena i održavanje plazmida. P. pastoris soj X-33 i S. cerevisiae soj InvSC1 korišćeni su za ekstracelularnu ekspresiju CHO. Aktivnost CHO određena je ABST esejom, a promena absorbance merena je na 405 nm. Potvrda prisustva enzima rađena je na DNK agaroznoj elektroforezi i SDS-PAGE. Posle transformacije P. pastoris X-33, nijedan od klonova nije pokazivao aktivnost CHO. Posle prve fermentacije, kolonije su testirane na SDS-PAGE. Kako su dva uzorka pokazala trake, koje ne postoje na praznom vektoru, ove trake bi mogle odgovarati željenom enzimu, CHO. Traka se nalazi na molekulskoj masi koja je veća od teoretske (više od 120 kDa). Enzim bi mogao biti glikolizovan i zbog toga pokazivati ovako velike vrednosti za molekulsku masu. S. cerevisiae soj InvSC1 transformisan je konstruktom CHO-pZES. Posle 24 sata, tri kolonije su porasle na ploči na kojoj su bile ćelije transformisane pomenutim konstruktom. Uzorci su testirani na SDS-PAGE. Jedan uzorak je pokazao traku na oko 110 kDa, ali aktivnost CHO nije potvrđena takođe. Cilj ove studije je bio kloniranje CHO u kvascima S. cerevisiae i P. pastoris, kao i njena ekspresija u ovim, danas široko primenjivanim ekspresionim sistemima.",
publisher = "Assoc Chemical Engineers Serbia, Belgrade",
journal = "Hemijska industrija",
title = "Cloning of the gene for a carbohydrate oxidase from Lactuca sativa in the yeasts Saccharomyces cerevisiae and Pichia pastoris, Kloniranje gena za ugljeni hidrat oksidazu iz biljke Lactuca sativa u kvasce saccharomyces cerevisiae i Pichia pastoris",
volume = "69",
number = "6",
pages = "689-701",
doi = "10.2298/HEMIND140823003T"
}

Tadić, V., Balaž, A. M., Petrić, M., Milošević, S. M., Zelenović, N., Raspor, M. Z., Tadić, J.,& Prodanović, R.. (2015). Cloning of the gene for a carbohydrate oxidase from Lactuca sativa in the yeasts Saccharomyces cerevisiae and Pichia pastoris. in Hemijska industrija
Assoc Chemical Engineers Serbia, Belgrade., 69(6), 689-701.
https://doi.org/10.2298/HEMIND140823003T

Tadić V, Balaž AM, Petrić M, Milošević SM, Zelenović N, Raspor MZ, Tadić J, Prodanović R. Cloning of the gene for a carbohydrate oxidase from Lactuca sativa in the yeasts Saccharomyces cerevisiae and Pichia pastoris. in Hemijska industrija. 2015;69(6):689-701.
doi:10.2298/HEMIND140823003T .

Tadić, Vojin, Balaž, Ana Marija, Petrić, Marija, Milošević, Snežana M., Zelenović, Nevena, Raspor, Martin Z., Tadić, Jovan, Prodanović, Radivoje, "Cloning of the gene for a carbohydrate oxidase from Lactuca sativa in the yeasts Saccharomyces cerevisiae and Pichia pastoris" in Hemijska industrija, 69, no. 6 (2015):689-701,
https://doi.org/10.2298/HEMIND140823003T . .