Journal of Applied Glycoscience
Online ISSN : 1880-7291
Print ISSN : 1344-7882
ISSN-L : 1344-7882
Note
Effective Purification of 1,4-β-Endoglucanase (EG66) from a Marine Mollusc, Patinopecten yessoensis, by Cellulose Column Chromatography
Ken SakaiKyohei OhtakiHideyo KoizumiShota SatoHisaoki SuzukiNobutaka TachibanaTetsuo OhmachiTakashi Yoshida
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2009 Volume 56 Issue 1 Pages 13-16

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Abstract

1,4-β-Endoglucanase was purified from the hepatopancreas of the marine mollusc, Patinopecten yessoensis, by cellulose column chromatography. The enzyme (EG66) showed the Mr of 66K on SDS-PAGE, and the hydrolytic activity was maximal at pH 6.0. EG66 readily hydrolyzed glucomannan and β-1,3-1,4-glucan as well as CMC and hydroxyethyl cellulose. On the other hand, crystalline cellulose, xylan, xyloglucan, laminarin, β-1,3-1,6-glucan, galactomannan, alginate, methyl cellulose and hydroxypropylmethyl cellulose were not hydrolyzed at all. N-Terminal amino acid sequence of EG66, which was determined as GATNVQIT NEWPGGFQGTF, had a motif common to the other molluscan endoglucanases.

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© 2009 by The Japanese Society of Applied Glycoscience
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