Journal
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
Volume 155, Issue 2, Pages 138-144Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpb.2009.10.013
Keywords
Sea hare; Mollusks; Gastropod; beta-1,3-glucanase; Laminarinase; Laminarin; Laminarioligosaccharide; Transglycosylation
Categories
Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [19380117]
- Grants-in-Aid for Scientific Research [19380117] Funding Source: KAKEN
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Two types of beta-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 32.1.6) degrading laminarin and laminarioligosaccharides to laminaritriose, laminaribiose, and glucose, while AkLam33 was regarded as an exolytic enzyme (EC 32.1.58) directly producing glucose from polymer laminarin. AkLam36 showed higher activity toward beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin (LLam) than highly branched beta-1,3-glucans such as Eisenia bicyclis laminarin (ELam). AkLam33 showed moderate activity toward both Ram 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 beta-1,3-glucanases. (C) 2009 Elsevier Inc. All rights reserved.
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