Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/4582
Title: Endopeptidases of <i style="">Bacillus subtilis</i> IBTC-3 and <i style="">B. alcalophilus</i> PB92 in synthesis of precursors of biologically active peptides
Authors: Głowacka, Agnieszka E
Szczesna-Antczak, Mirosława H
Piotrowicz-Wasiak, Małgorzata
Antczak, Tadeusz Z
Keywords: Subtilisin
Alkaline peptidase PB92
Immobilization
Amino acid esters
Peptides
Non-aqueous enzymology
Issue Date: Jun-2009
Publisher: CSIR
Abstract: Two endopeptidases (from <i style="">Bacillus subtilis</i> IBTC-3 and from <i style="">B. alcalophilus</i> PB92-commercial preparation) efficiently synthesized amino acid esters (NAc-Tyr-OEt and NAc-Phe-OEt) and dipeptides (NAc-Tyr-Gly-NH<sub>2</sub> and NAc-Tyr-Arg-NH<sub>2</sub>) in organic solvent/water systems. The rate of NAc-Tyr-OEt synthesis mediated by the native subtilisin IBTC-3 was maximum (0.23 Umg<sup>-1</sup>)<sup> </sup>in ethanol/5-7% w/v water system, while the highest activity of the freeze-dried enzyme (0.18 Umg<sup>-1</sup>) was achieved, when water content was 9-10% w/v. The preferred system for dipeptide synthesis (using NAc-Tyr-OEt as acyl donor) by both the enzymes was acetonitrile/4% w/v water. In this system, the maximum yield of NAc-Tyr-GlyNH<sub>2</sub> was 71 and 80% and that of NAc-Tyr-Arg-NH<sub>2</sub> was 53 and 40% for subtilisin IBTC-3 and peptidase PB92, respectively. In contrast to the peptidase PB92, the subtilisin efficiently catalyzed esterification of NAc-Tyr with 1-butanol and isopropanol.
Description: 213-220
URI: http://hdl.handle.net/123456789/4582
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.46(3) [June 2009]

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