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- W2019810130 abstract "The suitability of optimised ultrafine Eri silk microparticles as novel enzyme supports was studied for potential application in biofuel production. β-glucosidase (BGL) from Aspergillus niger was immobilised on Eri silk fibrion particles via an adsorption method resulting in a 62% immobilisation yield. Soluble and immobilised enzymes exhibited pH-optima at pH 4.0 and 5.0, respectively with optimum activity at 60°C. The Michaelis constant (K(M)) was 0.16 and 0.27 mM for soluble and immobilised BGL respectively. The immobilisation support has a protective effect on the enzyme by increasing rigidity; this is reflected by an increase in stability under thermal denaturation at 70°C. Immobilised enzyme retained more than 50% of initial activity for up to eight cycles. Maximum cellobiose hydrolysis by immobilised BGL was achieved at 20 h. Crystalline ultrafine Eri silk particles were found to be a promising viable, environmentally sound and stable matrix for binding BGL for cellobiose hydrolysis." @default.
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- W2019810130 date "2013-10-01" @default.
- W2019810130 modified "2023-10-12" @default.
- W2019810130 title "Exploring novel ultrafine Eri silk bioscaffold for enzyme stabilisation in cellobiose hydrolysis" @default.
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- W2019810130 doi "https://doi.org/10.1016/j.biortech.2013.01.065" @default.
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