Inactivation of Saccharomyces cerevisiae and Escherichia coli enzymes by high hydrostatic pressure

초록

Inactivation of Saccharomyces cerevisiae (ATCC 16664) and Escherichia coli (ATCC 1229) enzymes by high hydrostatic pressure (HHP) was investigated. Prior to HHP treatments of S. cerevisiae and E. coli, thirteen active enzymes were detected in both S. cerevisiae and E. coli by the APIZYME system (BioMerieux Vitek, Inc., Hazelwood, MO). When S. cerevisiae and E. coli were treated with pressure at 65 Kpsi for 30 sec at 23°C, lipase, cystine arylamidase, and chymotrypsin were completely inactivated in S. cerevisiae. Esterase, esterase lipase, lipase, valine arylamidase, cystine arylamidase, trypsin, α-glucosidase, and β-glucuronidase were completely inactivated in E. coli. Leucine arylamidase, valine arylamidase, β -glucosidase and α -mannosidase were not completely inactivated in S. cerevisiae. Leucine arylamidase and β -galactosidase were not completely inactivated in E. coli. However, alkaline phosphatase, acid phosphatase, and naphthol-AS-BI-phosphohydrolase activities in both microorganisms remained active after HHP treatment.