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Purification and characterization of a chloride ion-dependent alpha-glucosidase from the midgut gland of Japanese scallop (Patinopecten yessoensis)

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/64647

Title: Purification and characterization of a chloride ion-dependent alpha-glucosidase from the midgut gland of Japanese scallop (Patinopecten yessoensis)
Authors: Masuda, Yasushi Browse this author
Okuyama, Masayuki Browse this author →KAKEN DB
Iizuka, Takahisa Browse this author
Nakai, Hiroyuki Browse this author
Saburi, Wataru Browse this author →KAKEN DB
Fukukawa, Taro Browse this author
Maneesan, Janjira Browse this author
Tagami, Takayoshi Browse this author
Naraoka, Tetsushi Browse this author
Mori, Haruhide Browse this author →KAKEN DB
Kimura, Atsuo Browse this author →KAKEN DB
Keywords: scallop -glucosidase
chloride ion dependent
substrate specificity
Issue Date: 4-Mar-2016
Publisher: Taylor & Francis
Journal Title: Bioscience biotechnology and biochemistry
Volume: 80
Issue: 3
Start Page: 479
End Page: 485
Publisher DOI: 10.1080/09168451.2015.1116926
PMID: 26645800
Abstract: Marine glycoside hydrolases hold enormous potential due to their habitat-related characteristics such as salt tolerance, barophilicity, and cold tolerance. We purified an -glucosidase (PYG) from the midgut gland of the Japanese scallop (Patinopecten yessoensis) and found that this enzyme has unique characteristics. The use of acarbose affinity chromatography during the purification was particularly effective, increasing the specific activity 570-fold. PYG is an interesting chloride ion-dependent enzyme. Chloride ion causes distinctive changes in its enzymatic properties, increasing its hydrolysis rate, changing the pH profile of its enzyme activity, shifting the range of its pH stability to the alkaline region, and raising its optimal temperature from 37 to 55 degrees C. Furthermore, chloride ion altered PYG's substrate specificity. PYG exhibited the highest V-max/K-m value toward maltooctaose in the absence of chloride ion and toward maltotriose in the presence of chloride ion.
Rights: This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience biotechnology and biochemistry on 2016-03-04, available online: http://wwww.tandfonline.com/10.1080/09168451.2015.1116926.
Type: article (author version)
URI: http://hdl.handle.net/2115/64647
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 木村 淳夫

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