Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis
XM Tang, FM Lakay, W Shen, WL Shao, HY Fang… - Biotechnology …, 2004 - Springer
XM Tang, FM Lakay, W Shen, WL Shao, HY Fang, BA Prior, ZX Wang, J Zhuge
Biotechnology letters, 2004•SpringerAn extracellular alkaline protease produced by Bacillus licheniformis AP-1 was purified 76-
fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at
60° C (assayed over 10 min). The protease was completely inhibited by
phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca
2+ and Mg 2+ addition.
fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at
60° C (assayed over 10 min). The protease was completely inhibited by
phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca
2+ and Mg 2+ addition.
Abstract
An extracellular alkaline protease produced by Bacillus licheniformis AP-1 was purified 76-fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at 60°C (assayed over 10 min). The protease was completely inhibited by phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca2+ and Mg2+ addition.
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