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Titolo:
Purification and characterization of the alkaline serine protease producedby Bacillus sp. N4 strain from fish skin mucus
Autore:
Asakawa, M; Sadakata, Y; Araki, T; Sumi, T; Nakagawa, H;
Indirizzi:
Kumamoto Univ, Fac Educ, Food Sci Lab, Kumamoto 8608555, Japan Kumamoto Univ Kumamoto Japan 8608555 od Sci Lab, Kumamoto 8608555, Japan Mie Univ, Fac Bioresources, Tsu, Mie 5148507, Japan Mie Univ Tsu Mie Japan 5148507 Fac Bioresources, Tsu, Mie 5148507, Japan Saga Univ, Fac Agr, Dept Appl Biol Sci, Saga 8408502, Japan Saga Univ Saga Japan 8408502 gr, Dept Appl Biol Sci, Saga 8408502, Japan
Titolo Testata:
FISHERIES SCIENCE
fascicolo: 5, volume: 64, anno: 1998,
pagine: 793 - 797
SICI:
0919-9268(199810)64:5<793:PACOTA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Keywords:
Bacillus sp. N4 strain; alkaline serine protease; fish skin mucus; horse mackerel; Flavobacterium sp.;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
11
Recensione:
Indirizzi per estratti:
Indirizzo: Asakawa, M Kumamoto Univ, Fac Educ, Food Sci Lab, Kumamoto 8608555, Japan Kumamoto Univ Kumamoto Japan 8608555 Kumamoto 8608555, Japan
Citazione:
M. Asakawa et al., "Purification and characterization of the alkaline serine protease producedby Bacillus sp. N4 strain from fish skin mucus", FISHERIES S, 64(5), 1998, pp. 793-797

Abstract

Bacillus sp. N4 strain was isolated from the skin mucus of horse mackerel Trachurus japonicus. A protease was purified to homogeneity from the culture fluid by application of ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. The enzyme (N4-protease) had a single polypeptide chain with apparent molecular weight of 28,000 estimated by SDS-PAGE, and an isoelectric point around 9.5. The enzyme was most active toward azocasein and Suc-Leu-Leu-Val-Tyr-MCA at pH 10 and toward casein at pH 11, and was stable between pH 6 and pH 11. The optimum temperature of the enzyme was 50 degrees C and its activity was stable below 50 degrees C. Calcium ion was effective to activate and stabilize the enzyme especially at high temperature. Since the activity was completely inhibited by PMSF and DFP but not by sulfhydryl and metal chelating agents, it was concluded that NLE-protease is an alkaline serine protease belonging to a member of the subtilisinfamily.

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Documento generato il 22/01/20 alle ore 09:25:42