Exploring novel ultrafine Eri silk bioscaffold for enzyme stabilisation in cellobiose hydrolysis

Madan Verma, Rangam Rajkhowa, Xungai Wang, Colin Barrow, Munish Puri

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    40 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)302-306
    Number of pages5
    JournalBioresource Technology
    Publication statusPublished - 2013


    • Biofuel
    • Immobilisation
    • Lignocellulose
    • Nanobiotechnology
    • β-Gucosidase


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