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Spontaneous and protein-induced secretion of proteinases from Saccharomyces cerevisiae

✍ Scribed by Anita Kurucová; Ester Farkašová; Ľudovít Varečka; Martin Šimkovič


Book ID
102392809
Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
484 KB
Volume
49
Category
Article
ISSN
0233-111X

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✦ Synopsis


Many fungi are capable of secreting the wide spectrum of hydrolytic enzymes. We characterized an inducible proteinase secretion in yeasts, Saccharomyces cerevisiae. The proteinase secretion by S. cerevisiae was induced in the presence of yeast extract, or of purified proteins, such as bovine serum albumin, casein, or ovalbumin, and some proteolytic activity was present also without protein inducer. We found that properties of proteinases induced under cultivation conditions were different in various aspects (temperature-and pH-dependencies, substrate specificities, sensitivities to proteinase inhibitors). Proteinase activities were also characterized by gelatin zymography. Multiple proteinase bands with wide-molecular weights (ranging from 45 to 240 kDa) were detected and patterns of proteinase bands were different. S. cerevisiae cells were able to retain the information about previous contacts with protein inducer resulting in faster and more intensive proteinase secretion response after repeated induction.


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