The purification and characterization of a Trichoderma harzianum exochitinase

被引：42

作者：

Deane, EE

Whipps, JM

Lynch, JM

Peberdy, JF

机构：

[1] Univ Nottingham, Dept Life Sci, Microbiol Grp, Nottingham NG7 2RD, England

[2] Hort Res Int, Dept Microbiol & Plant Pathol, Warwick CV35 9EF, England

[3] Univ Surrey, Sch Biol Sci, Guildford GU2 5XH, Surrey, England

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1383卷 / 01期

基金：

英国生物技术与生命科学研究理事会;

关键词：

exochitinase; purification strategy; (Trichoderma harzianum);

D O I：

10.1016/S0167-4838(97)00183-0

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 chitinolytic enzyme was purified from the culture filtrate of T. harzianum (T198) by precipitation with ammonium sulphate followed by affinity binding to swollen chitin and release with 10% (v/v) acetic acid. The molecular weight of the enzyme was calculated to be 28 and 27.5 kD by gel filtration chromatography and SDS-PAGE, respectively. The isoelectric point of the enzyme was 7.4. The pH optimum for activity was 3.5 and maximum activity was obtained at 50 degrees C, The enzyme displayed activity on a wide array of chitin substrates of more than two N-acetylglucosamine units in length. HPLC analysis of hydrolysis products demonstrated that the enzyme was an exochitinase releasing N-acetylglucosamine only. (C) 1998 Elsevier Science B.V.

引用

页码：101 / 110

页数：10

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