Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: its catalytic properties and deduced amino acid sequence |
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Authors: | Tohru Kobayashi Yuji Hatada Atsushi Suzumatsu Katsuhisa Saeki Yoshihiro Hakamada S Ito |
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Institution: | (1) Tochigi Research Laboratories, Kao Corporation, 2606 Akabane, Ichikai, Haga, Tochigi 321-3497, Japan Tel. +81-285-68-7304; Fax +81-285-68-7305 e-mail: 153419@kastanet.kao.co.jp, JP |
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Abstract: | The gene for a highly alkaline pectate lyase, Pel-4A, from alkaliphilic Bacillus sp. strain P-4-N was cloned, sequenced, and overexpressed in Bacillus subtilis cells. The deduced amino acid sequence of the mature enzyme (318 amino acids, 34 805 Da) showed moderate homology to those
of known pectate lyases in the polysaccharide lyase family 1. The purified recombinant enzyme had an isoelectric point of
pH 9.7 and a molecular mass of 34 kDa, and exhibited a very high specific activity compared with known pectate lyases reported
so far. The enzyme activity was stimulated 1.6 fold by addition of NaCl at an optimum of 100 mM. When Pel-4A was stored at
50°C for 60 h, striking stabilization by 100 mM NaCl was observed in a pH range from 5 to 11.5, whereas it was stable only
around pH 11 in the absence of NaCl.
Received: June 10, 2000 / Accepted: October 3, 2000 |
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Keywords: | Alkaliphile Pectate lyase Cloning Bacillus Salt dependency |
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