Highly active pectinases from newly isolated Aspergillus tubingensis strain
Аутори
Pavlović, MarijaStojanović, Sanja
Dojnov, Biljana
Božić, Nataša
Vujčić, Zoran
Margetić, Aleksandra
Конференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Pectinolytic enzymes represent a large group of enzymes that catalyze the reactions of depolymerization and deesterification of pectin polysaccharides1. Saprophytic fungi produce pectinases on a large scale for industrial purposes. These enzymes have a various biotechnological application and their global annual production represents 25% of total industrial enzymes 1,2. Agro-waste is widely used as economical substrate for the production of pectinases by solid state fermentation 3. In this study, sugar beet pulp, as a good source of pectin3, was used as a substrate for enzyme production by Aspergillus tubingensis. This strain was isolated from the quince fruit and identified by the molecular DNA marker calmodulin (CaM). SSF was performed with this strain on sugar beet pulp (80%) in combination with wheat bran (20%), a potent substrate for pectinase production 3. The obtained high pectinolytic activity (15 U/mL), determined by 3,5-dinitrosalicylic acid reagent, was in the range of comme...rcial pectinases. Zymography detection, using Ruthenium Red to visualize endo-pectinase activity and pectin-methyl esterase activity revealed several pectinase activity bands. Hydrolysis of different pectin substrates with the obtained pectinase complex was analyzed by thin layer chromatography in order to detect different products such as pectic oligosaccharides, which are emerging prebiotics superior to intact pectin.
Кључне речи:
pectin / pectinases / Aspergillus tubingensisИзвор:
Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia, 2021, 124-125Издавач:
- University of Belgrade - Faculty of Chemistry
- Serbian Biochemical Society
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200026 (Универзитет у Београду, Институт за хемију, технологију и металургију - ИХТМ) (RS-200026)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-200168)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200017 (Универзитет у Београду, Институт за нуклеарне науке Винча, Београд-Винча) (RS-200017)
Институција/група
IHTMTY - CONF AU - Pavlović, Marija AU - Stojanović, Sanja AU - Dojnov, Biljana AU - Božić, Nataša AU - Vujčić, Zoran AU - Margetić, Aleksandra PY - 2021 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/5834 AB - Pectinolytic enzymes represent a large group of enzymes that catalyze the reactions of depolymerization and deesterification of pectin polysaccharides1. Saprophytic fungi produce pectinases on a large scale for industrial purposes. These enzymes have a various biotechnological application and their global annual production represents 25% of total industrial enzymes 1,2. Agro-waste is widely used as economical substrate for the production of pectinases by solid state fermentation 3. In this study, sugar beet pulp, as a good source of pectin3, was used as a substrate for enzyme production by Aspergillus tubingensis. This strain was isolated from the quince fruit and identified by the molecular DNA marker calmodulin (CaM). SSF was performed with this strain on sugar beet pulp (80%) in combination with wheat bran (20%), a potent substrate for pectinase production 3. The obtained high pectinolytic activity (15 U/mL), determined by 3,5-dinitrosalicylic acid reagent, was in the range of commercial pectinases. Zymography detection, using Ruthenium Red to visualize endo-pectinase activity and pectin-methyl esterase activity revealed several pectinase activity bands. Hydrolysis of different pectin substrates with the obtained pectinase complex was analyzed by thin layer chromatography in order to detect different products such as pectic oligosaccharides, which are emerging prebiotics superior to intact pectin. PB - University of Belgrade - Faculty of Chemistry PB - Serbian Biochemical Society C3 - Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia T1 - Highly active pectinases from newly isolated Aspergillus tubingensis strain SP - 124 EP - 125 UR - https://hdl.handle.net/21.15107/rcub_cer_5834 ER -
@conference{ author = "Pavlović, Marija and Stojanović, Sanja and Dojnov, Biljana and Božić, Nataša and Vujčić, Zoran and Margetić, Aleksandra", year = "2021", abstract = "Pectinolytic enzymes represent a large group of enzymes that catalyze the reactions of depolymerization and deesterification of pectin polysaccharides1. Saprophytic fungi produce pectinases on a large scale for industrial purposes. These enzymes have a various biotechnological application and their global annual production represents 25% of total industrial enzymes 1,2. Agro-waste is widely used as economical substrate for the production of pectinases by solid state fermentation 3. In this study, sugar beet pulp, as a good source of pectin3, was used as a substrate for enzyme production by Aspergillus tubingensis. This strain was isolated from the quince fruit and identified by the molecular DNA marker calmodulin (CaM). SSF was performed with this strain on sugar beet pulp (80%) in combination with wheat bran (20%), a potent substrate for pectinase production 3. The obtained high pectinolytic activity (15 U/mL), determined by 3,5-dinitrosalicylic acid reagent, was in the range of commercial pectinases. Zymography detection, using Ruthenium Red to visualize endo-pectinase activity and pectin-methyl esterase activity revealed several pectinase activity bands. Hydrolysis of different pectin substrates with the obtained pectinase complex was analyzed by thin layer chromatography in order to detect different products such as pectic oligosaccharides, which are emerging prebiotics superior to intact pectin.", publisher = "University of Belgrade - Faculty of Chemistry, Serbian Biochemical Society", journal = "Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia", title = "Highly active pectinases from newly isolated Aspergillus tubingensis strain", pages = "124-125", url = "https://hdl.handle.net/21.15107/rcub_cer_5834" }
Pavlović, M., Stojanović, S., Dojnov, B., Božić, N., Vujčić, Z.,& Margetić, A.. (2021). Highly active pectinases from newly isolated Aspergillus tubingensis strain. in Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia University of Belgrade - Faculty of Chemistry., 124-125. https://hdl.handle.net/21.15107/rcub_cer_5834
Pavlović M, Stojanović S, Dojnov B, Božić N, Vujčić Z, Margetić A. Highly active pectinases from newly isolated Aspergillus tubingensis strain. in Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia. 2021;:124-125. https://hdl.handle.net/21.15107/rcub_cer_5834 .
Pavlović, Marija, Stojanović, Sanja, Dojnov, Biljana, Božić, Nataša, Vujčić, Zoran, Margetić, Aleksandra, "Highly active pectinases from newly isolated Aspergillus tubingensis strain" in Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia (2021):124-125, https://hdl.handle.net/21.15107/rcub_cer_5834 .