Isolation from the marine mollusk Lambis sp. and catalytic properties of an alginate lyase with rare substrate specificity

Isolation from the marine mollusk Lambis sp. and catalytic properties of an alginate lyase with rare substrate specificity

Homogeneous alginate lyase with rare specificity exhibiting maximum activity at pH 5.0 and temperature range 40–55°C that catalyzed cleavage of 1→4 glycoside bonds between α-L-guluronic acid residues was isolated from liver-pancreas of the marine gastropod mollusk Lambis sp. The alginate lyase was c...

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Bibliographic Details
Published in:Chemistry of natural compounds Vol. 49; no. 2; pp. 215 - 218
Main Authors: Sil′chenko, A. S., Kusaikin, M. I., Zakharenko, A. M., Zvyagintseva, T. N.
Format: Journal Article
Language:English
Published: Boston Springer US 01-05-2013
Springer
Subjects:
Medicine
Organic Chemistry
Pharmacy
Plant Sciences
alginate lyase
polyguluronic acid
marine invertebrates
sp
substrate specificity
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Summary:Homogeneous alginate lyase with rare specificity exhibiting maximum activity at pH 5.0 and temperature range 40–55°C that catalyzed cleavage of 1→4 glycoside bonds between α-L-guluronic acid residues was isolated from liver-pancreas of the marine gastropod mollusk Lambis sp. The alginate lyase was classified as a poly-1→4-α-L-guluronate lyase (EC 4.2.2.11).
ISSN:0009-3130
1573-8388
DOI:10.1007/s10600-013-0564-6