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- Title
Purification of an extracellular carboxypeptidase from Pseudozyma hubeiensis 31-B and its characterization as a food additive.
- Authors
Tamio Mase; Sachiyo Shitasue; Tetsuya Kondo; Maaya Tanaka; Riho Takada; Miyo Hiwatashi; Shinobu Isshiki; Junko Kawai
- Abstract
A newly isolated yeast strain, Pseudozyma hubeiensis 31-B, produced an extracellular carboxypeptidase but no detectable proteinase activity. The carboxypeptidase was purified from filtered culture medium by ammonium sulfate precipitation and successive four column chromatography steps: TOYOPEARL DEAE-650M, TOYOPEARL Butyl-650M, hydroxylapatite, and TOYOPEARL HW-55 chromatography. The final enzyme preparation appeared homogeneous on SDS-polyacrylamide gel electrophoresis. The enzyme had a molecular mass of 70.5 kDa. The optimum temperature and pH of the purified enzyme were approximately 50°C and 5.0, respectively. The purified carboxypeptidase preferentially hydrolyzed Z-Phe-Leu, and its activity was inhibited by diisopropyl fluorophosphate. The carboxypeptidase produced by P. hubeiensis 31-B has potential applications in the food industry as a food additive.
- Subjects
CARBOXYPEPTIDASES; COLUMN chromatography; FOOD additives; FOOD industry; POLYACRYLAMIDE gel electrophoresis
- Publication
Japanese Journal of Food Chemistry & Safety, 2017, Vol 24, Issue 1, p39
- ISSN
1341-2094
- Publication type
Article