Chainia Penicillin V Acylase: Strain Characteristics, Enzyme Immobilization, and Kinetic Studies |
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| Authors: | Sanjay Chauhan Anuradha Nichkawade MRS Iyengar Bharat B Chattoo |
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| Institution: | (1) Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi-110067, India , IN;(2) Genetic Engineering Unit, Center for Biotechnology, Jawaharlal Nehru University, New Delhi-110067, India , IN;(3) Microbiological Research and Development Laboratories, Alembic Chemical Works Co. Ltd, Baroda-390002, India , IN;(4) Department of Microbiology and Biotechnology Center, M.S. University of Baroda, Baroda-390002, India , IN |
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| Abstract: | Aerobic cultures of an actinomycete were found to produce penicillin V acylase (PVA) (PA, EC-3.5.1.11) extracellularly. The
presence of L-2-3 diamino-propionic acid in cell wall and formation of sclerotia on culture media led to its identification
as Chainia, a sclerotial Streptomyces. Partially purified acylase was adsorbed on kieselguhr and entrapped in polyacrylamide gel. The immobilized preparation proved
effective with respect to retention of enzyme and enzyme activity even after 15 successful cycles. The pH optimum for crude
enzyme was in the range of pH 7.5–8.0, and for the (NH4)2 SO4 fraction it was pH 8.5. The immobilized enzyme showed maximal activity at pH 9.5. The optimum temperature for acylase activity
was at 55°C. The crude enzyme, ammonium sulfate fraction, and immobilized enzyme showed K
m
value for penicillin V of 6.13 mM, 14.3 mM, and 17.1 mM, respectively.
Received: 11 December 1997 / Accepted: 9 April 1998 |
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