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Characterization and mode of action of exo-1,3-β-d-glucanase from Aspergillus saitoi

✍ Scribed by Shin Kasahara; Tasuku Nakajima; Chikara Miyamoto; Kenji Wada; Yasuhiro Furuichi; Eiji Ichishima


Book ID
113396779
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
202 KB
Volume
74
Category
Article
ISSN
0922-338X

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✍ Naohito Ohno; Isao Nono; Toshiro Yadomae 📂 Article 📅 1989 🏛 Elsevier Science 🌐 English ⚖ 588 KB

An exo-(143)/3-D-glucanase, isolated from a commercial lytic enzyme preparation "kitalase", had mol. wt. 74,000, isoelectric point pH 8.1, optimum pH 5.6, optimum temperature 53", pH stability 5.0-8.0, and temperature stability up to 65". The enzyme contained 703 amino acids, including 10 Cys, 7 Trp