Purification and partial characterization of exopolygalacturonase I from Penicillium frequentans

被引：15

作者：

Chellegatti, MAD ^{[1
]}

Fonseca, MJV ^{[1
]}

Said, S ^{[1
]}

机构：

[1] Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Dept Ciencias Farmaceut, BR-14040903 Ribeirao Preto, SP, Brazil

来源：

MICROBIOLOGICAL RESEARCH | 2002年 / 157卷 / 01期

基金：

巴西圣保罗研究基金会;

关键词：

Brazilian soil; exopolygalacturonase; pectic enzyme; polygalacturonase;

D O I：

10.1078/0944-5013-00127

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A polygalacturonase with a molecular mass of 74 kDa, an isoelectric point around pH 4.2 and pH - and temperature optima of 3.9 and 50degreesC, respectively, was purified from a culture fluid of Penicillium frequentans. The enzyme was characterized as an exo-alpha-1,4-polygalacturonase (exo-PG 1). K-m and V-max for sodium polypectate hydrolysis were 0.68 g/l and 596.8 U x mg(-1), respectively. The enzyme, a glycoprotein with a carbohydrate content of 81 %. is probably the main pectinase of Penicillium frequentans responsible for cleaving monomer units from the non-reducing end of pectin.

引用

页码：19 / 24

页数：6

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