Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 72, Issue 12, Pages 3142-3147Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.80316
Keywords
cellulase; cellobiohydrolase; Irpex lacteus; Pichia pastoris; endoglucanase
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Kyowa Hakko Co., Ltd.
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A gene (cel4) coding for a cellobiohydrolase H (Ex-4) was isolated from the white rot basidiomycete, Irpex lacteus strain MC-2. The cel4 ORF was composed of 452 amino acid residues and was interrupted by eight introns. Its deduced amino acid sequence revealed a multi domain structure composed of a cellulose-binding domain, a linker, and a catalytic domain belonging to family 6 of glycosyl hydrolases, from the N-terminus. cel4 cDNA was successfully expressed in the yeast Pichia pastoris. Recombinant Ex-4 showed endo-processive degrading activity towards cellulosic substrates, and a synergistic effect in the degradation of Avicel was observed when the enzyme acted together with either cellobiohydrolase I (Ex-1) or endoglucanase (En-1) produced by I. lacteus MC-2.
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