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Mineralization of Lipase from Thermomyces lanuginosus Immobilized on Methacrylate Beads Bearing Octadecyl Groups to Improve Enzyme Features

التفاصيل البيبلوغرافية
العنوان: Mineralization of Lipase from Thermomyces lanuginosus Immobilized on Methacrylate Beads Bearing Octadecyl Groups to Improve Enzyme Features
المؤلفون: José R. Guimarães, Diego Carballares, Javier Rocha-Martin, Paulo W. Tardioli, Roberto Fernandez-Lafuente
المصدر: Catalysts, Vol 12, Iss 12, p 1552 (2022)
بيانات النشر: MDPI AG, 2022.
سنة النشر: 2022
المجموعة: LCC:Chemical technology
LCC:Chemistry
مصطلحات موضوعية: lipase immobilization, immobilization on Purolite C18, mineralization of immobilized lipase, modulation of lipase hydrolytic activity, lipase stabilization, Chemical technology, TP1-1185, Chemistry, QD1-999
الوصف: Lipase from Thermomyces lanuginosus (TLL) has been immobilized on Purolite Lifetech® ECR8806F (viz. methacrylate macroporous resin containing octadecyl groups, designated as Purolite C18-TLL), and the enzyme performance has been compared to that of the enzyme immobilized on octyl-agarose, designated as agarose C8-TLL. The hydrolytic activity versus p-nitrophenol butyrate decreased significantly, and to a lower extent versus S-methyl mandelate (more than twofold), while versus triacetin and R-methyl mandelate, the enzyme activity was higher for the biocatalyst prepared using Purolite C18 (up to almost five-fold). Regarding the enzyme stability, Purolite C18-TLL was significantly more stable than the agarose C8-TLL. Next, the biocatalysts were mineralized using zinc, copper or cobalt phosphates. Mineralization increased the hydrolytic activity of Purolite C18-TLL versus triacetin and R-methyl mandelate, while this activity decreased very significantly versus the S-isomer, while the effects using agarose C8-TLL were more diverse (hydrolytic activity increase or decrease was dependent on the metal and substrate). The zinc salt treatment increased the stability of both biocatalysts, but with a lower impact for Purolite C18-TLL than for agarose-C8-TLL. On the contrary, the copper and cobalt salt treatments decreased enzyme stability, but more intensively using Purolite C18-TLL. The results show that even using enzymes immobilized following the same strategy, the differences in the enzyme conformation cause mineralization to have diverse effects on enzyme stability, hydrolytic activity, and specificity.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2073-4344
Relation: https://www.mdpi.com/2073-4344/12/12/1552; https://doaj.org/toc/2073-4344
DOI: 10.3390/catal12121552
URL الوصول: https://doaj.org/article/07564e046be34d4dabc954845c6c17da
رقم الأكسشن: edsdoj.07564e046be34d4dabc954845c6c17da
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20734344
DOI:10.3390/catal12121552