Purification and characterization of two extracellular proteinases from Arthrobacter nicotianae 9458

Abstract Two extracellular serine proteinases with molecular masses of about 53–55 and 70–72 kDa, were purified from Arthrobacter nicotianae 9458 and characterized. The enzymes differed with respect to temperature optimum, 55–60 and 37°C, respectively, tolerance to low values of pH and temperature,...

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Bibliographic Details
Published in:FEMS microbiology letters 1999-01, Vol.170 (2), p.327-333
Main Authors: Smacchi, Emanuele, Fox, Patrick F., Gobbetti, Marco
Format: Article
Language:English
Subjects:
Arthrobacter
Arthrobacter - enzymology
Bacterial Proteins - chemistry
Bacterial Proteins - drug effects
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Casein
Caseins - metabolism
Cheese - microbiology
Edetic Acid - pharmacology
Enzyme Inhibitors - pharmacology
Ethylenediaminetetraacetic acids
Food industries
Fundamental and applied biological sciences. Psychology
Hot Temperature
Hydrogen-Ion Concentration
Hydrophobicity
Metabolism. Enzymes
Microbiology
Milk and cheese industries. Ice creams
Optimization
pH effects
Protein purification
Proteinases
Ripening
Serine
Serine Endopeptidases - chemistry
Serine Endopeptidases - drug effects
Serine Endopeptidases - isolation & purification
Serine Endopeptidases - metabolism
Smear surface‐ripened cheese
Sodium chloride
Sodium Chloride - pharmacology
Temperature
Temperature tolerance
β‐Casein
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Summary:Abstract Two extracellular serine proteinases with molecular masses of about 53–55 and 70–72 kDa, were purified from Arthrobacter nicotianae 9458 and characterized. The enzymes differed with respect to temperature optimum, 55–60 and 37°C, respectively, tolerance to low values of pH and temperature, heat stability, sensitivity to EDTA and sulfhydryl blocking agents, and hydrophobicity. Both proteinases were optimally active in the pH range of 9.0 and 9.5, had considerable activity at pH 6.0 on αs1- and β-caseins, and tolerated NaCl over 5%. Specificity on casein fractions was generally similar and β-casein was more susceptible to hydrolysis than αs1-casein. The proteinases of Arthrobacter spp. may play a significant role in ripening of the smear surface-ripened cheeses.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1999.tb13391.x