1403/01/09
باقر سیدعلیپور

باقر سیدعلیپور

مرتبه علمی: دانشیار
ارکید: http://orcid.org/0000-0002-3854-9328
تحصیلات: دکترای تخصصی
اسکاپوس: https://www.scopus.com/authid/detail.uri?authorId=56725735600
دانشکده: دانشکده علوم پایه
نشانی: دانشگاه مازندران-دانشکده علوم پایه-گروه زیست سلولی و مولکولی
تلفن: 01135302405

مشخصات پژوهش

عنوان
Lipase immobilization on a novel class of Zr-MOF/electrospun nanofibrous polymers: Biochemical characterization and efficient biodiesel production
نوع پژوهش
JournalPaper
کلیدواژه‌ها
Zr-MOF/PVP nanocomposite , Electrospun nanofbers Ultrasound-assisted synthesis, Lipase MG10, Immobilization, Biodiesel production
سال
2021
مجله International Journal of Biological Macromolecules
شناسه DOI
پژوهشگران Arastoo Badoei-Dalfard ، Arezoo Shahba ، Fatemeh Zaare ، Ghasem Sargazi ، Bagher Seyedalipour ، Zahra Zahra Karami

چکیده

In this study, due to the favorable properties of MOF compounds and fbrous materials, new nanostructures of ZrMOF/PVP nanofbrous composites were synthesized by electrospinning procedure. The related features of these samples were characterized by relevant analyzes, including SEM, BET surface area analysis, XRD, and FTIR spectroscopy. The fnal product showed signifcant properties such as small particle size distribution, large surface area, and high crystallinity. This strategy for producing these nanostructures could lead to new compounds as novel alternative materials for biological applications. Lipase MG10 was successfully immobilized on the mentioned nanofbrous composites and biochemically characterized. The lipase activity of free and immobilized lipases was considered by measuring the absorbance of pNPP (500 μM in 40 mM Tris/HCl buffer, pH 7.8, and 0.01% Triton X100) at 37 ◦C for 30 min. Different concentrations of glutaraldehyde, different crosslinking times, different times of immobilization, different enzyme loading, and different pH values have been optimized. Results showed that the optimized immobilization condition was achieved in 2.5% glutaraldehyde, after 2 h of crosslinking time, after 6 h immobilization time, using 180 mg protein/g support at pH 9.0. The immobilized enzyme was also totally stable after 180 min incubation at 60 ◦C. The free enzyme showed the maximum activity at pH 9.0, but the optimal pH of the immobilized lipase was shifted about 1.5 pH units to the alkaline area. The immobilized lipase showed about 2.7 folds (78%) higher stability than the free enzyme at 50 ◦C. Some divalent metal ions, including Cu2+ (22%), Co2+ (37%), Mg2+ (12%), Hg2+ (11%), and Mn2+ (17%) enhanced the enzyme activity of immobilized enzyme. The maximum biodiesel production (27%) from R. communis oil was obtained after 18 h of incubation by lipase MG10. The immobilized lipase displayed high potency in biodiesel production, about 83% after 12 h of incubation. These