Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential
Конференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Enzyme catalyzed reactions have been extensively exploited for a wide range of applications in biotechnology. In spite of a broad implementation of enzymes in different fields, some constraints referred to their cost and process stability still exists. To overcome a limit related to short catalytic lifetime of enzymes in process conditions, a spectrum of immobilization methods have been extensively studied to increase stability and enhance reuse, offer easier separation, making production economically viable.
Извор:
RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro, 2017, 75-Издавач:
- RAD Centre, Niš, Serbia
Напомена:
- V International Conference on Radiation in Various Fields of Research : RAD 2017 : book of abstracts; June 12-16, 2017; Budva, Montenegro
Колекције
Институција/група
VinčaTY - CONF AU - Izrael Živković, Lidija AU - Živković, Ljiljana S. PY - 2017 UR - https://vinar.vin.bg.ac.rs/handle/123456789/11194 AB - Enzyme catalyzed reactions have been extensively exploited for a wide range of applications in biotechnology. In spite of a broad implementation of enzymes in different fields, some constraints referred to their cost and process stability still exists. To overcome a limit related to short catalytic lifetime of enzymes in process conditions, a spectrum of immobilization methods have been extensively studied to increase stability and enhance reuse, offer easier separation, making production economically viable. PB - RAD Centre, Niš, Serbia C3 - RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro T1 - Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential SP - 75 UR - https://hdl.handle.net/21.15107/rcub_vinar_11194 ER -
@conference{ author = "Izrael Živković, Lidija and Živković, Ljiljana S.", year = "2017", abstract = "Enzyme catalyzed reactions have been extensively exploited for a wide range of applications in biotechnology. In spite of a broad implementation of enzymes in different fields, some constraints referred to their cost and process stability still exists. To overcome a limit related to short catalytic lifetime of enzymes in process conditions, a spectrum of immobilization methods have been extensively studied to increase stability and enhance reuse, offer easier separation, making production economically viable.", publisher = "RAD Centre, Niš, Serbia", journal = "RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro", title = "Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential", pages = "75", url = "https://hdl.handle.net/21.15107/rcub_vinar_11194" }
Izrael Živković, L.,& Živković, L. S.. (2017). Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential. in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro RAD Centre, Niš, Serbia., 75. https://hdl.handle.net/21.15107/rcub_vinar_11194
Izrael Živković L, Živković LS. Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential. in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro. 2017;:75. https://hdl.handle.net/21.15107/rcub_vinar_11194 .
Izrael Živković, Lidija, Živković, Ljiljana S., "Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential" in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro (2017):75, https://hdl.handle.net/21.15107/rcub_vinar_11194 .