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Biotechnology and Applied Biochemistry (2002) 35, (165–169) (Printed in Great Britain)

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Bioaffinity immobilization of tannase from Aspergillus niger on concanavalin A–Sepharose CL-4B

Shweta Sharma*, Tej Krishan Bhat† and Munishwar Nath Gupta*¹

*Chemistry Department, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi 110016, India, and †I.V.R.I. Regional Station Palampur, H.P. 176061, India

Key words: gallic acid production, non-covalent immobilization, tannin hydrolysis.

Abbreviation used: Con A, concanavalin A.

¹To whom correspondence should be addressed (e-mail mn_gupta@hotmail.com).

Tannase from Aspergillus niger van Teighem was immobilized on concanavalin A–Sepharose via bioaffinity interaction. The immobilized enzyme showed a pH optimum similar to that of the free enzyme. K_m values for free and immobilized enzyme were 0.3 and 0.6 mM respectively. V_max changed from 0.013 to 0.02 µmol·min^-1 upon immobilization. The immobilized preparation was quite stable to reuse, there was no loss of enzyme activity after three cycles and it retained 81% activity even after the sixth cycle. Ester hydrolysis using the immobilized enzyme led to a 40% conversion into gallic acid as compared with 30% obtained with the free enzyme.

Received 16 October 2001/29 January 2002; accepted 8 February 2002

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