Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate
Imobilizacija invertaze preko ugljenohidratnog dela na makroporozni glicidil metakrilat
Апстракт
Immobilization via carbohydrate moiety is suitable for immobilization of glycoenzymes because it has little effect on enzyme active site. Macroporous glycidyl methacrylate is better support for enzyme immobilization from the much more used polystyrene because of its lesser hydrophobicity. We found optimal conditions for invertase immobilization via its carbohydrate moiety on macroporous glycidyl methacryate by varying enzyme concentration. We obtained immobilized enzyme with specific activity of 5500 lU/g, which is the highest activity reported in the literature. Immobilized enzyme has Km=43 mmol/l, temperature optimum of 60ºC, and pH optimum between 3.5 and 5.5.
Imobilizacija preko šećernog dela je pogodna za glikoenzime zato što ima malo uticaja na aktivno mesto enzima. Makroporozni glicidil metakrilat je bolji nosač za imobilizaciju enzima od više korišćenog polistirena zbog svoje hidrofilnosti. Utvrđeni su optimalni uslovi za imobilizaciju invertaze preko šećernog dela na makroporozni glicidil metalkrilat variranjem koncentracije enizima. Dobijen je imobilizovani enzim specifične aktivnosti 5000 IU/g, što je najveća aktivnost do sada opisana u literaturi. Imobilizovani enzim je imao Km 43 mmol/l, temperaturni optimum na 60ºC i pH optimum između 4 i 5.
Кључне речи:
invertase / periodate / immobilization / macroporous / glycidyl methacrylateИзвор:
Acta periodica technologica, 2001, 32, 151-156Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Prodanović, Radivoje AU - Jovanović, Slobodan M. AU - Vujčić, Zoran PY - 2001 UR - https://cherry.chem.bg.ac.rs/handle/123456789/208 AB - Immobilization via carbohydrate moiety is suitable for immobilization of glycoenzymes because it has little effect on enzyme active site. Macroporous glycidyl methacrylate is better support for enzyme immobilization from the much more used polystyrene because of its lesser hydrophobicity. We found optimal conditions for invertase immobilization via its carbohydrate moiety on macroporous glycidyl methacryate by varying enzyme concentration. We obtained immobilized enzyme with specific activity of 5500 lU/g, which is the highest activity reported in the literature. Immobilized enzyme has Km=43 mmol/l, temperature optimum of 60ºC, and pH optimum between 3.5 and 5.5. AB - Imobilizacija preko šećernog dela je pogodna za glikoenzime zato što ima malo uticaja na aktivno mesto enzima. Makroporozni glicidil metakrilat je bolji nosač za imobilizaciju enzima od više korišćenog polistirena zbog svoje hidrofilnosti. Utvrđeni su optimalni uslovi za imobilizaciju invertaze preko šećernog dela na makroporozni glicidil metalkrilat variranjem koncentracije enizima. Dobijen je imobilizovani enzim specifične aktivnosti 5000 IU/g, što je najveća aktivnost do sada opisana u literaturi. Imobilizovani enzim je imao Km 43 mmol/l, temperaturni optimum na 60ºC i pH optimum između 4 i 5. T2 - Acta periodica technologica T1 - Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate T1 - Imobilizacija invertaze preko ugljenohidratnog dela na makroporozni glicidil metakrilat IS - 32 SP - 151 EP - 156 UR - https://hdl.handle.net/21.15107/rcub_cherry_208 ER -
@article{ author = "Prodanović, Radivoje and Jovanović, Slobodan M. and Vujčić, Zoran", year = "2001", abstract = "Immobilization via carbohydrate moiety is suitable for immobilization of glycoenzymes because it has little effect on enzyme active site. Macroporous glycidyl methacrylate is better support for enzyme immobilization from the much more used polystyrene because of its lesser hydrophobicity. We found optimal conditions for invertase immobilization via its carbohydrate moiety on macroporous glycidyl methacryate by varying enzyme concentration. We obtained immobilized enzyme with specific activity of 5500 lU/g, which is the highest activity reported in the literature. Immobilized enzyme has Km=43 mmol/l, temperature optimum of 60ºC, and pH optimum between 3.5 and 5.5., Imobilizacija preko šećernog dela je pogodna za glikoenzime zato što ima malo uticaja na aktivno mesto enzima. Makroporozni glicidil metakrilat je bolji nosač za imobilizaciju enzima od više korišćenog polistirena zbog svoje hidrofilnosti. Utvrđeni su optimalni uslovi za imobilizaciju invertaze preko šećernog dela na makroporozni glicidil metalkrilat variranjem koncentracije enizima. Dobijen je imobilizovani enzim specifične aktivnosti 5000 IU/g, što je najveća aktivnost do sada opisana u literaturi. Imobilizovani enzim je imao Km 43 mmol/l, temperaturni optimum na 60ºC i pH optimum između 4 i 5.", journal = "Acta periodica technologica", title = "Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate, Imobilizacija invertaze preko ugljenohidratnog dela na makroporozni glicidil metakrilat", number = "32", pages = "151-156", url = "https://hdl.handle.net/21.15107/rcub_cherry_208" }
Prodanović, R., Jovanović, S. M.,& Vujčić, Z.. (2001). Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate. in Acta periodica technologica(32), 151-156. https://hdl.handle.net/21.15107/rcub_cherry_208
Prodanović R, Jovanović SM, Vujčić Z. Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate. in Acta periodica technologica. 2001;(32):151-156. https://hdl.handle.net/21.15107/rcub_cherry_208 .
Prodanović, Radivoje, Jovanović, Slobodan M., Vujčić, Zoran, "Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate" in Acta periodica technologica, no. 32 (2001):151-156, https://hdl.handle.net/21.15107/rcub_cherry_208 .