open access

https://hdl.handle.net/2115/64647

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

英語

substrate specificity

2016-03-04

Taylor & Francis

Bioscience biotechnology and biochemistry

80(3)

479-485

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.

学術雑誌論文

Accepted Manuscript

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.

0916-8451