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Efficient Sporulation of Saccharomyces cerevisiae in a 96 Multiwell Format
Published on: September 17, 2016
Spontaneous and protein-induced secretion of proteinases from Saccharomyces cerevisiae
Anita Kurucová1, Ester Farkasová, L'udovít Varecka
1Department of Biochemistry and Microbiology, Institute of Biochemistry, Nutrition and Health Protection, Faculty of Chemical and Food Technology, Slovak University of Technology, 812 37 Bratislava, Slovak Republic.
Abstract:
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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