Isolation and purification of yeast polypeptides and efficacy of cosmetics

doi:10.14088/j.cnki.issn0439-8114.2020.07.037

Abstract

Abstract: yeast protein was extracted from yeast cells by means of repeated freeze-thaw and ultrasonic crushing. The supernatant of yeast fermentation and yeast cell fluid were purified by isoelectric point precipitation method. Crude protein was obtained, and the antioxidant capacity of protein and tyrosinase inhibition ability were studied. The results showed that the supernatant of saccharomyces cerevisiae, yellow wine yeast and sake yeast had good DPPH scavenging ability, and the concentration of 2.6g /L could reach 72%. The supernatant of saccharomyces cerevisiae among the three yeast supernatant proteins had better inhibitory effect on tyrosinase. The three yeast crude proteins basically had no DPPH free radical scavenging ability at about 0.45g /L, and the inhibition rate of saccharomyces cerevisiae crude proteins on tyrosinase was better than that of other yeast crude proteins. The DPPH radical scavenging rate and tyrosinase inhibition rate of 3 kinds of yeast polypeptides with 3.5 g/L were about 50% and 12% respectively.

Key words: yeast, polypeptide, antioxidant, whitening

CLC Number:

TQ658

FU Hao, LIU Ping-ping, ZHU Jian-feng, LI Yan-long, LI Meng, WANG Chang-tao. Isolation and purification of yeast polypeptides and efficacy of cosmetics[J]. HUBEI AGRICULTURAL SCIENCES, 2020, 59(7): 184-187.

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