The phytase subfamily of histidine acid phosphatases: Isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila

被引：185

作者：

Mitchell, DB ^{[1
]}

Vogel, K ^{[1
]}

Weimann, BJ ^{[1
]}

Pasamontes, L ^{[1
]}

vanLoon, APGM ^{[1
]}

机构：

[1] F HOFFMANN LA ROCHE & CIE AG, VITAMINS & FINE CHEM DIV, BIOTECHNOL SECT, CH-4070 BASEL, SWITZERLAND

来源：

MICROBIOLOGY-SGM | 1997年 / 143卷

关键词：

Aspergillus terreus; Myceliophthora thermophila; gene isolation; histidine acid phosphatase; phytase;

D O I：

10.1099/00221287-143-1-245

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Phytases catalyse the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate. In this study genes encoding novel phytases from two different filamentous fungi, Aspergillus terreus strain 9A-1 and Myceliophthora thermophila were isolated. The encoded PhyA phytase proteins show 60% (A. terreus) and 48% (M. thermophila) identity, respectively, to the PhyA of Aspergillus niger and have 21-29% identity compared to other histidine acid phosphatases. All three PhyA proteins, in contrast to the A. niger pH 2 . 5-optimum acid phosphatase, prefer phytic acid as substrate and show enzyme activity at a broad range of acidic pH values. Based on their enzyme characteristics and protein sequence homology, the phytases form a novel subclass of the histidine acid phosphatase family.

引用

页码：245 / 252

页数：8

共 22 条

[1] STRUCTURAL-ANALYSIS OF THE 2 TANDEMLY REPEATED ACID-PHOSPHATASE GENES IN YEAST [J].