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Exploring novel ultrafine Eri silk bioscaffold for enzyme stabilisation in cellobiose hydrolysis
- Verma, Madan L., Rajkhowa, Rangam, Wang, Xungai, Barrow, Colin J., Puri, Munish
- Bioresource technology 2013 v.145 pp. 302-306
- protective effect, thermal stability, Aspergillus niger, immobilized enzymes, cellobiose, denaturation, pH, hydrolysis, adsorption
- 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 0.27mM 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 20h. Crystalline ultrafine Eri silk particles were found to be a promising viable, environmentally sound and stable matrix for binding BGL for cellobiose hydrolysis.