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
No coin nor oath required. For personal study only.
✦ 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.
📜 SIMILAR VOLUMES
Secretion of a nonglycosylated form of human prourokinase, also known as single-chain urinary plasminogen activator (scu-PA), from Saccharomyces cerevisiae is de- scribed. A "supersecreting" yeast strain harboring multiple copies of integrated plasmids was grown batchwise and at constant respiratory
The INU genes o f Kluyveromyces marxianus encode inulinases which are readily secreted from Saccharomyces cerevisiaeinto the culture medium. To evaluate the utility of the INU signal peptides for the secretion of heterologous proteins from S. cerevisiae, a variety of expression and secretion vectors