Low-molecular-weight xylanase from Trichoderma viride

Journal Article · Sat Jun 01 00:00:00 EDT 1991 · Applied and Environmental Microbiology; (United States)

OSTI ID:5272438

Ujiie, M; Roy, C; Yaguchi, M ^[1]

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1. Inst. of Biological Sciences, Ottawa (Canada)

An endo-1,4-{beta}-xylanase (1,4-{beta}-D-xylan xylanohydrolase, EC 3.2.1.8) has been isolated from a commercial proparation of Trichoderma viride. The molecular weight was 22,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the pI value was 9.3. The xylanase was a true xylanase without cellulase activity. When the N-terminal amino acid sequence of thew first 50 residues was compared with that of a xylanase from Schizophyllum commune, strong evidence for homology was found, with more than 50% amino acid identity. T. viride xylanase also possessed extensive identity with a proposed amino-terminal consensus sequence of xylanases from bacteria.

• OSTI ID: 5272438
• Journal Information: Applied and Environmental Microbiology; (United States), Vol. 57:6; ISSN 0099-2240
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
TRICHODERMA VIRIDE
ENZYME ACTIVITY
XYLANASE
STRUCTURE-ACTIVITY RELATIONSHIPS
AMINO ACID SEQUENCE
PROTEIN STRUCTURE
ENZYMES
EUMYCOTA
FUNGI
GLYCOSYL HYDROLASES
HYDROLASES
MOLECULAR STRUCTURE
O-GLYCOSYL HYDROLASES
PLANTS
TRICHODERMA
550200* - Biochemistry