Purification and characterization of an extracellular proteinase from Hendersonula toruloidea
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چکیده
منابع مشابه
Purification and Characterization of Extracellular, Polyextremophilic α-amylase Obtained from Halophilic Engyodontium album
Background: a-Amylases (EC 3.2.1.1) are covering approximately 25% of total enzyme market and are frequently used in food, pharmaceutical and detergent industries. Objectives: The first ever detailed characterization of amylase from any halophilic Engyodontium album is presented. Materials and Methods: An extracellular α-amylase was studied from halophilic E. album TISTR 3645. The enzyme was e...
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Background: Proteolytic enzymes have an important role in variety of physiological and pathological functions. They have been used in therapeutic and pharmaceutical applications. Characterizations of extracellular proteases from various strains of S. marcescens indicate that most strains produce a very similar major metalloprotease. This metalloprotease (serrapeptidase, serrapeptase) is an impo...
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An extracellular proteinase was purified from culture filtrates of Cryptococcus neoformans NHPY24 by DEAE ion-exchange chromatography and gelatin affinity column chromatography with azoalbumin as the substrate. The molecular mass of the purified enzyme was 43 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, its pH optimum was 7.0 to 8.0, and maximal activity was obtained at pH ...
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phosphorus is one of the most important nutrients for plant growth and development. chemical pi fertilizer is used to provide the phosphorus for the plants, but it is mostly fixed in the soil into insoluble form and become unavailable to the plants. phosphate-solubilizing bacteria have lots of application in agriculture as biological fertilizer. consumption of biofertilizers instead of chemical...
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A serine proteinase (Alp) from the culture supernate of a clinical isolate of Aspergillus fumigatus was purified to virtual homogeneity at a yield of 41%. The procedure involved affinity chromatography on agarose-epsilon-amino-caproyl-D-tryptophan methyl ester. Alp had an estimated mol. wt of 32 Kda and the pI was determined at pH 7.9. The enzyme was fully inhibited by phenylmethyl sulphonyl fl...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1990
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.58.9.2856-2861.1990