کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
681065 | 1459998 | 2013 | 5 صفحه PDF | دانلود رایگان |
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 (KM) 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.
► Ultrafine Eri silk particles (size 5 μm) were prepared in short milling time without pre-treatment.
► Environment friendly Eri silk scaffold is used for immobilisation of β-glucosidase.
► Eri-silk bioscaffold protects the enzyme by increasing its rigidity and stability.
► Immobilised enzyme retained more than 50% of initial activity for up to eight cycles.
Journal: Bioresource Technology - Volume 145, October 2013, Pages 302–306