Extracellular Acid and Alkaline Proteases from Candida olea
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چکیده
منابع مشابه
Acid and Alkaline Extracellular Proteases of Yarrowia lipolytica
XPR2 and AXP1, coding for alkaline (AEP) and acid (AXP) extracellular proteases, have been sequenced for several strains. For XPR2, the three sequenced strains are not closely related and produce significantly different levels of AEP, yet the coding sequences are identical, and there is only a single nucleotide difference in one promoter suggesting that host physiology, not promoter differences...
متن کاملpH-regulated expression of the acid and alkaline extracellular proteases of Yarrowia lipolytica.
The pH-regulated expression of the acid (AXP) and alkaline (AEP) extracellular proteases of the yeast Yarrowia lipolytica 148 was analysed. Expression in batch and continuous cultures was determined at the mRNA level by Northern blotting, and at the enzyme level by enzyme assays and Western blotting. Culture pH regulated AEP and AXP expression predominantly at the level of mRNA content. Highest...
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Thermophilic Bacillus sp. GUS1, isolated from a soil sample obtained from citrus garden, produced at least three proteases as detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and zymogram analysis. The enzymes were stable in the alkaline pH range (8.0-12.0), with the optimum temperature and pH range of the proteases being 70ºC and 6.0-12.0, respectively. All th...
متن کاملCharacterization of extracellular alkaline proteases and collagenase induction in Vibrio alginolyticus.
The number and approximate molecular weights of extracellular alkaline proteases produced by Vibrio alginolyticus were determined by gelatin-PAGE. Three major bands of protease activity with apparent molecular weights of approximately 28 000, 22 500 and 19 500 (proteases 1, 2 and 3, respectively) and two minor bands of protease activity with apparent molecular weights of approximately 15 500 an...
متن کاملProperties of two homologous alkaline proteases from Streptomyces rectus.
Some physicochemical properties of two thermostable proteases from Streptomyces rectus are described. The enzymes were judged to be identical with respect to molecular weight, inactivation with serine protease inhibitors, and in primary structure by peptide analysis. Amino acid analysis indicated the enzymes had identical compositions except for their amide content. The molecular weights of the...
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ژورنال
عنوان ژورنال: Microbiology
سال: 1987
ISSN: 1350-0872,1465-2080
DOI: 10.1099/00221287-133-6-1461