TY  - CONF
AU  - Šokarda Slavić, Marinela
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Pavlović, Marija
AU  - Stojanović, Sanja
AU  - Drulović, Nenad
AU  - Vujčić, Zoran
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6028
AB  - Fish processing generates a large amount of waste products; nearly 75 % of the total fish weight consists of scales, skins, heads, viscera, and bones. These waste by-products are often dumped in landfills or the ocean, contributing to environmental pollution. Solid fish waste has a high collagen content and can be utilized for the extraction of different products such as gelatine, which can be used in different food and pharmaceutical industries. Fish gelatine contains all biogenic amino acids and can be used as a dietary supplement, thus increasing the utilization of fish waste and reducing environmental pollution.
Recently, a strong worldwide focus has been directed towards the discovery of new microbial proteases for industrial applications. For that purpose, the Bacillus sp. strains from the laboratory bank were screened for the ability to secrete alkaline proteases. Bacterial strains that produced a larger clear zone on the gelatine agar plate were selected for further study. Selected bacterial strains were cultivated under submerged conditions for the purpose of producing proteases. The supernatant from each isolate was used as a crude enzyme extract for testing gelatine proteolytic activity and hydrolysis products. Bacillus sp. strains 12B, 16A, 17B and 24B showed a high degree of hydrolysis of the gelatine waste and the ability to form proteins of small molecular masses after one hour of hydrolysis. Of these, sp. 12B was the most potent, having twice the proteolytic activity determined by the TNBS method.
PB  - European Federation of Biotechnology
C3  - Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online
T1  - Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation
SP  - 66
EP  - 66
UR  - https://hdl.handle.net/21.15107/rcub_cer_6028
ER  - 

@conference{
author = "Šokarda Slavić, Marinela and Margetić, Aleksandra and Ristović, Marina and Pavlović, Marija and Stojanović, Sanja and Drulović, Nenad and Vujčić, Zoran",
year = "2023",
abstract = "Fish processing generates a large amount of waste products; nearly 75 % of the total fish weight consists of scales, skins, heads, viscera, and bones. These waste by-products are often dumped in landfills or the ocean, contributing to environmental pollution. Solid fish waste has a high collagen content and can be utilized for the extraction of different products such as gelatine, which can be used in different food and pharmaceutical industries. Fish gelatine contains all biogenic amino acids and can be used as a dietary supplement, thus increasing the utilization of fish waste and reducing environmental pollution.
Recently, a strong worldwide focus has been directed towards the discovery of new microbial proteases for industrial applications. For that purpose, the Bacillus sp. strains from the laboratory bank were screened for the ability to secrete alkaline proteases. Bacterial strains that produced a larger clear zone on the gelatine agar plate were selected for further study. Selected bacterial strains were cultivated under submerged conditions for the purpose of producing proteases. The supernatant from each isolate was used as a crude enzyme extract for testing gelatine proteolytic activity and hydrolysis products. Bacillus sp. strains 12B, 16A, 17B and 24B showed a high degree of hydrolysis of the gelatine waste and the ability to form proteins of small molecular masses after one hour of hydrolysis. Of these, sp. 12B was the most potent, having twice the proteolytic activity determined by the TNBS method.",
publisher = "European Federation of Biotechnology",
journal = "Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online",
title = "Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation",
pages = "66-66",
url = "https://hdl.handle.net/21.15107/rcub_cer_6028"
}

Šokarda Slavić, M., Margetić, A., Ristović, M., Pavlović, M., Stojanović, S., Drulović, N.,& Vujčić, Z.. (2023). Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation. in Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online
European Federation of Biotechnology., 66-66.
https://hdl.handle.net/21.15107/rcub_cer_6028

Šokarda Slavić M, Margetić A, Ristović M, Pavlović M, Stojanović S, Drulović N, Vujčić Z. Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation. in Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online. 2023;:66-66.
https://hdl.handle.net/21.15107/rcub_cer_6028 .

Šokarda Slavić, Marinela, Margetić, Aleksandra, Ristović, Marina, Pavlović, Marija, Stojanović, Sanja, Drulović, Nenad, Vujčić, Zoran, "Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation" in Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online (2023):66-66,
https://hdl.handle.net/21.15107/rcub_cer_6028 .

TY  - CONF
AU  - Pavlović, Marija
AU  - Šokarda Slavić, Marinela
AU  - Kojić, Milan
AU  - Ristović, Marina
AU  - Momčilović, Miloš
AU  - Drulović, Nenad
AU  - Vujčić, Zoran
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7136
AB  - Pectinases are widely used in the fruit juice industry for clarification, liquefaction and stabilization of juices. Primarily, these enzymes are responsible for the breakdown of long and complex molecules in the fruit pulp (pectin). Unlike the combination of polygalacturonase (PG) and pectin esterase (PE) commonly found in commercial products, pectin lyase (PNL) is the only known pectinase capable of breaking down highly esterified pectins (such those found in fruits) into short molecules via a β-elimination mechanism without producing methanol. Methanol is toxic and can be harmful to health. Commercial preparations with PNL as the major component are preferable in juices and wine processing because it avoids the production of methanol, precipitation of pectin partially de-esterified with endogenous calcium, and damage of the volatile ester content responsible for the specific aroma of various fruits. This study reports the first cloning and characterization of a PNL gene, ppr, from Bacillus velezensis, and the deduced amino acid sequence is compared with those of other lyases. In this work, the gene encoding the pectin lyase (PNL; EC 4.2.2.10) from Bacillus velezensis was successfully expressed under optimized conditions for high soluble protein expressions as soluble PNL-6His in E. coli M15[pREP4]. After expression, purification of 6xHis-labeled PNL was performed according to QIAGEN instructions. IMAC fractions were analyzed using SDS-PAGE. After purification, 3-fold purification was observed with a yield of 82%. In this study, we report for the first time a method to express PNL in E. coli and purify it as a pure native enzyme. The cloned PLN was used to clarify and liquefy apple and orange juices and to improve the flavor of these juices. In this way, pulp waste after juice extraction is reduced. Methanol content was determined by gas-liquid chromatography and was not detectable in the clarified juices.
PB  - Elsevier
C3  - Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany
T1  - Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis
SP  - P3.015
UR  - https://hdl.handle.net/21.15107/rcub_cer_7136
ER  - 

@conference{
author = "Pavlović, Marija and Šokarda Slavić, Marinela and Kojić, Milan and Ristović, Marina and Momčilović, Miloš and Drulović, Nenad and Vujčić, Zoran",
year = "2023",
abstract = "Pectinases are widely used in the fruit juice industry for clarification, liquefaction and stabilization of juices. Primarily, these enzymes are responsible for the breakdown of long and complex molecules in the fruit pulp (pectin). Unlike the combination of polygalacturonase (PG) and pectin esterase (PE) commonly found in commercial products, pectin lyase (PNL) is the only known pectinase capable of breaking down highly esterified pectins (such those found in fruits) into short molecules via a β-elimination mechanism without producing methanol. Methanol is toxic and can be harmful to health. Commercial preparations with PNL as the major component are preferable in juices and wine processing because it avoids the production of methanol, precipitation of pectin partially de-esterified with endogenous calcium, and damage of the volatile ester content responsible for the specific aroma of various fruits. This study reports the first cloning and characterization of a PNL gene, ppr, from Bacillus velezensis, and the deduced amino acid sequence is compared with those of other lyases. In this work, the gene encoding the pectin lyase (PNL; EC 4.2.2.10) from Bacillus velezensis was successfully expressed under optimized conditions for high soluble protein expressions as soluble PNL-6His in E. coli M15[pREP4]. After expression, purification of 6xHis-labeled PNL was performed according to QIAGEN instructions. IMAC fractions were analyzed using SDS-PAGE. After purification, 3-fold purification was observed with a yield of 82%. In this study, we report for the first time a method to express PNL in E. coli and purify it as a pure native enzyme. The cloned PLN was used to clarify and liquefy apple and orange juices and to improve the flavor of these juices. In this way, pulp waste after juice extraction is reduced. Methanol content was determined by gas-liquid chromatography and was not detectable in the clarified juices.",
publisher = "Elsevier",
journal = "Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany",
title = "Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis",
pages = "P3.015",
url = "https://hdl.handle.net/21.15107/rcub_cer_7136"
}

Pavlović, M., Šokarda Slavić, M., Kojić, M., Ristović, M., Momčilović, M., Drulović, N.,& Vujčić, Z.. (2023). Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis. in Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany
Elsevier., P3.015.
https://hdl.handle.net/21.15107/rcub_cer_7136

Pavlović M, Šokarda Slavić M, Kojić M, Ristović M, Momčilović M, Drulović N, Vujčić Z. Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis. in Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany. 2023;:P3.015.
https://hdl.handle.net/21.15107/rcub_cer_7136 .

Pavlović, Marija, Šokarda Slavić, Marinela, Kojić, Milan, Ristović, Marina, Momčilović, Miloš, Drulović, Nenad, Vujčić, Zoran, "Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis" in Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany (2023):P3.015,
https://hdl.handle.net/21.15107/rcub_cer_7136 .

TY  - CONF
AU  - Mišić, Milan
AU  - Drulović, Nenad
AU  - Margetić, Aleksandra
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5841
AB  - Polyphenols are a large group of natural organic compounds mainly found in plants, in whom they have diverse protective and metabolic functions. It’s also known that phenolic compounds, especially tannins, interact with proteins in various significant and distinct ways. Tannins also complex proteins, which generally precipitates them and it’s their most important industrially utilised characteristic. This study, which was a continuation of our previous work, focused on interactions of aqueous tea plant extracts with laccase from Trametes 63ersicolour and β-amylase from Ipomoea batatas. Tea plants used in this study wereSaturejamontana, Menthapiperita, Salvia officinalis, Matricariachamomilla, Camellia cinensis and Arctostaphylosuva-ursi. Total phenolic content was determined using Folin-Ciocalteu reagent, which showed us that chosen plants vary considerably in their total phenolic content and the highest concentration was found to be in Arctostaphylosuva-ursi. Protein interactions between tea plant extracts were measured using spectrophotometric, spectrofluorimetric and electrophoretic methods. These methods showed that tea plant extracts lead to various structural changes within the protein, nature of which require 
further research. Finally, it was also found that all tea plant extracts, except Matricariachamomillaextract, reversibly precipitate β-amylase – whilst retaining most of 
its enzymatic activity after dissolving.Best results were obtained using Arctostaphylosuva-ursi extract, which precipitated the highest quantity of β-amylase, with highest activity retention. Although being an interesting phenomenon, furtherresearch is necessary to determine the nature andimportance of reversible tannic enzyme precipitation.
PB  - Serbian Chemical Society
C3  - Book of Abstracts, Proceedings - 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, June 9-10, 2022 / Kratki izvodi radova, kjniga radova - 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine
T1  - Protein interactions of six tea plant extracts
SP  - 63
UR  - https://hdl.handle.net/21.15107/rcub_cer_5841
ER  - 

@conference{
author = "Mišić, Milan and Drulović, Nenad and Margetić, Aleksandra and Vujčić, Zoran and Vujčić, Miroslava",
year = "2022",
abstract = "Polyphenols are a large group of natural organic compounds mainly found in plants, in whom they have diverse protective and metabolic functions. It’s also known that phenolic compounds, especially tannins, interact with proteins in various significant and distinct ways. Tannins also complex proteins, which generally precipitates them and it’s their most important industrially utilised characteristic. This study, which was a continuation of our previous work, focused on interactions of aqueous tea plant extracts with laccase from Trametes 63ersicolour and β-amylase from Ipomoea batatas. Tea plants used in this study wereSaturejamontana, Menthapiperita, Salvia officinalis, Matricariachamomilla, Camellia cinensis and Arctostaphylosuva-ursi. Total phenolic content was determined using Folin-Ciocalteu reagent, which showed us that chosen plants vary considerably in their total phenolic content and the highest concentration was found to be in Arctostaphylosuva-ursi. Protein interactions between tea plant extracts were measured using spectrophotometric, spectrofluorimetric and electrophoretic methods. These methods showed that tea plant extracts lead to various structural changes within the protein, nature of which require 
further research. Finally, it was also found that all tea plant extracts, except Matricariachamomillaextract, reversibly precipitate β-amylase – whilst retaining most of 
its enzymatic activity after dissolving.Best results were obtained using Arctostaphylosuva-ursi extract, which precipitated the highest quantity of β-amylase, with highest activity retention. Although being an interesting phenomenon, furtherresearch is necessary to determine the nature andimportance of reversible tannic enzyme precipitation.",
publisher = "Serbian Chemical Society",
journal = "Book of Abstracts, Proceedings - 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, June 9-10, 2022 / Kratki izvodi radova, kjniga radova - 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine",
title = "Protein interactions of six tea plant extracts",
pages = "63",
url = "https://hdl.handle.net/21.15107/rcub_cer_5841"
}

Mišić, M., Drulović, N., Margetić, A., Vujčić, Z.,& Vujčić, M.. (2022). Protein interactions of six tea plant extracts. in Book of Abstracts, Proceedings - 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, June 9-10, 2022 / Kratki izvodi radova, kjniga radova - 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine
Serbian Chemical Society., 63.
https://hdl.handle.net/21.15107/rcub_cer_5841

Mišić M, Drulović N, Margetić A, Vujčić Z, Vujčić M. Protein interactions of six tea plant extracts. in Book of Abstracts, Proceedings - 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, June 9-10, 2022 / Kratki izvodi radova, kjniga radova - 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine. 2022;:63.
https://hdl.handle.net/21.15107/rcub_cer_5841 .

Mišić, Milan, Drulović, Nenad, Margetić, Aleksandra, Vujčić, Zoran, Vujčić, Miroslava, "Protein interactions of six tea plant extracts" in Book of Abstracts, Proceedings - 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, June 9-10, 2022 / Kratki izvodi radova, kjniga radova - 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine (2022):63,
https://hdl.handle.net/21.15107/rcub_cer_5841 .