Secretion of an enzymatically active Trichoderma harzianum endochitinase by Saccharomyces cerevisiae

被引：3

作者：

Draborg, H ^{[1
]}

Halkier, T ^{[1
]}

Dalboge, H ^{[1
]}

Christgau, S ^{[1
]}

Rasmussen, G ^{[1
]}

Kauppinen, S ^{[1
]}

机构：

[1] NOVO NORDISK AS, GENESEARCH, DK-2880 BAGSVAERD, DENMARK

来源：

CURRENT GENETICS | 1996年 / 29卷 / 04期

关键词：

biocontrol; secretion; chitinase; expression cloning; Saccharomyces cerevisiae; Trichoderma harzianum;

D O I：

暂无

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

A novel endochitinase agar-plate assay has been developed and used to identify 11 full-length cDNAs encoding endochitinase I (ENCI) from a Trichoderma harzianum cDNA library by expression in yeast. The 1473-bp chiI cDNA encodes a 424-residue precursor protein including both a signal sequence and a propeptide. The deduced ENC I amino-acid sequence is homologous to other fungal and bacterial chitinases, and the enzyme cross-reacts with a polyclonal antiserum raised against chitinase A1 from Bacillus circulans. The T. harzianum endochitinase I was secreted into the culture medium by the yeast Saccharomyces cerevisiae in a functionally active form. The purified recombinant enzyme had a molecular mass of 44 kDa, an isoelectric point of 6.3, a pH optimum of 7.0 and a temperature optimum of 20 degrees C.

引用

页码：404 / 409

页数：6

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