Isolation and some properties of a serine protease from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam

An endopeptidase (Cudrania protease) with a molecular mass of 76 kDa has been purified from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam. The enzyme was stable between pH 6 and 10 at 30 degrees C for 60 min. The enzyme activity was inhibited by diisopropyl fluorophosphate, chymostati...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2000-03, Vol.64 (3), p.623-624
Main Authors: Uchikoba, T. (Kagoshima Univ. (Japan). Faculty of Science), Arima, K, Shimada, M, Yonezawa, H, Kaneda, M
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
CUDRANIA
Cudrania cochinchinensis
Enzymes and enzyme inhibitors
FRUIT
Fruit - enzymology
fruits
FRUTO
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Hydrolases
Moraceae
Plants - enzymology
PROTEASAS
PROTEASE
PROTEASES
SERINA
SERINE
Serine Endopeptidases - isolation & purification
Serine Endopeptidases - metabolism
serine protease
Temperature
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Summary:An endopeptidase (Cudrania protease) with a molecular mass of 76 kDa has been purified from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam. The enzyme was stable between pH 6 and 10 at 30 degrees C for 60 min. The enzyme activity was inhibited by diisopropyl fluorophosphate, chymostatin, and aprotinin, but not by EDTA or pepstatin. These results indicated that the enzyme was a serine protease
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.64.623