Purification and characterization of an alkaline serine endopeptidase from a feather-degrading Xanthomonas maltophilia strain

被引：52

作者：

De Toni, CH

Richter, MF

Chagas, JR

Henriques, JAP

Termignoni, C

机构：

[1] Univ Fed Rio Grande do Sul, Dept Bioquim, BR-91501970 Porto Alegre, RS, Brazil

[2] Univ Fed Rio Grande do Sul, Ctr Biotecnol, BR-91501970 Porto Alegre, RS, Brazil

[3] Univ Mogi das Cruzes, BR-08708911 Mogi das Cruzes, SP, Brazil

[4] Univ Fed Rio Grande do Sul, Dept Biofis, BR-91501970 Porto Alegre, RS, Brazil

[5] Univ Fed Rio Grande do Sul, Ctr Biotecnol, BR-91501970 Porto Alegre, RS, Brazil

来源：

CANADIAN JOURNAL OF MICROBIOLOGY | 2002年 / 48卷 / 04期

关键词：

serine endopeptidase; Xanthomonas maltophilia; keratinase; alkaline endopeptidase;

D O I：

10.1139/w02-027

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis. This enzyme has a molecular mass of 36 kDa, an optimum pH of 9.0, and an optimum temperature of 60degreesC. The inhibitory profile using protease inhibitors shows that this enzyme is a serine endopeptidase. Besides keratin, the enzyme is active upon the substrates azokeratin, azocasein, and the following fluorogenic peptide substrates: Abz-Leu-Gly-Met-Ile-Ser-Leu-Met-Lys-Arg-Pro-Gln-EDDnp, Abz-Lys-Leu-Cys(SBzl)-Gly-Pro-Lys-Gln-EDDnp, and Abz-Lys-Pro-Cys(SBzl)-Phe-Ser-Lys-Gln-EDDnp.

引用

页码：342 / 348

页数：7

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