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Isolation and characterization of two types of β-1,3-glucanases from the common sea hare Aplysia kurodai

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Title: Isolation and characterization of two types of β-1,3-glucanases from the common sea hare Aplysia kurodai
Authors: Kumagai, Yuya Browse this author
Ojima, Takao Browse this author →KAKEN DB
Keywords: sea hare
Issue Date: Feb-2010
Publisher: Elsevier
Journal Title: Comparative Biochemistry and Physiology. Part B, Biochemistry and Molecular Biology
Volume: 155
Issue: 2
Start Page: 138
End Page: 144
Publisher DOI: 10.1016/j.cbpb.2009.10.013
PMID: 19883786
Abstract: Two types of β-1,3-glucanases, AkLam36 and AkLam33 with the molecular masses of 36 kDa and 33 kDa, respectively, were isolated from the digestive fluid of the common sea hare Aplysia kurodai. AkLam36 was regarded as an endolytic enzyme (EC degrading laminarin and laminarioligosaccharides to laminaritriose, laminaribiose, and glucose, while AkLam33 was regarded as an exolytic enzyme (EC directly producing glucose from polymer laminarin. AkLam36 showed higher activity toward β-1,3-glucans with a few β-1,6-linked glucose branches such as Laminaria digitata laminarin (LLam) than highly branched β-1,3-glucans such as Eisenia bicyclis laminarin (ELam). AkLam33 showed moderate activity toward both ELam and LLam and high activity toward smaller substrates such as laminaritetraose and laminaritriose. Although both enzymes did not degrade laminaribiose as a sole substrate, they were capable of degrading it via transglycosylation reaction with laminaritriose. The N-terminal amino-acid sequences of AkLam36 and AkLam33 indicated that both enzymes belong to the glycosyl hydrolase family 16 like other molluscan β-1,3-glucanases.
Type: article (author version)
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 尾島 孝男

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