Purification and characterization of a chloride ion-dependent α-glucosidase from the midgut gland of Japanese scallop (Patinopecten yessoensis)
Autor: | Wataru Saburi, Masayuki Okuyama, Taro Fukukawa, Atsuo Kimura, Haruhide Mori, Janjira Maneesan, Tetsushi Naraoka, Iizuka Takahisa, Hiroyuki Nakai, Takayoshi Tagami, Yasushi Masuda |
---|---|
Rok vydání: | 2015 |
Předmět: |
0301 basic medicine
Patinopecten yessoensis Applied Microbiology and Biotechnology Biochemistry Chloride Analytical Chemistry Substrate Specificity 03 medical and health sciences Hydrolysis chemistry.chemical_compound Affinity chromatography Chlorides medicine Maltotriose Animals Glycoside hydrolase Molecular Biology chemistry.chemical_classification Chromatography 030102 biochemistry & molecular biology biology Organic Chemistry Temperature alpha-Glucosidases General Medicine Hydrogen-Ion Concentration biology.organism_classification Enzyme assay Kinetics Pectinidae 030104 developmental biology Enzyme chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Electrophoresis Polyacrylamide Gel Biotechnology medicine.drug |
Zdroj: | Bioscience, biotechnology, and biochemistry. 80(3) |
ISSN: | 1347-6947 |
Popis: | Marine glycoside hydrolases hold enormous potential due to their habitat-related characteristics such as salt tolerance, barophilicity, and cold tolerance. We purified an α-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 °C. Furthermore, chloride ion altered PYG’s substrate specificity. PYG exhibited the highest Vmax/Km value toward maltooctaose in the absence of chloride ion and toward maltotriose in the presence of chloride ion. |
Databáze: | OpenAIRE |
Externí odkaz: |