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Titolo:
Purification and properties of two intracellular aminopeptidases produced by Brevibacterium linens SR3
Autore:
Fernandez, J; Mohedano, AF; Gaya, P; Medina, M; Nunez, M;
Indirizzi:
INIA, Dept Tecnol Alimentos, Madrid, Spain INIA Madrid SpainINIA, Dept Tecnol Alimentos, Madrid, Spain Univ Autonoma Madrid, Fac Ciencias, Area Ingn Quim, Madrid, Spain Univ Autonoma Madrid Madrid Spain encias, Area Ingn Quim, Madrid, Spain
Titolo Testata:
INTERNATIONAL DAIRY JOURNAL
fascicolo: 4, volume: 10, anno: 2000,
pagine: 241 - 248
SICI:
0958-6946(2000)10:4<241:PAPOTI>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXTRACELLULAR PROTEINASE; CHEESE; BULGARICUS; ATCC-9174; ENZYMES;
Keywords:
Brevibacterium linens; aminopeptidase; purification;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Nunez, M INIA, Dept Tecnol Alimentos, Carretera La Coruna Km 7, Madrid, Spain INIA Carretera La Coruna Km 7 Madrid Spain Km 7, Madrid, Spain
Citazione:
J. Fernandez et al., "Purification and properties of two intracellular aminopeptidases produced by Brevibacterium linens SR3", INT DAIRY J, 10(4), 2000, pp. 241-248

Abstract

Two aminopeptidases, designated as aminopeptidase I (API) and aminopeptidase II (APII), were isolated from the disrupted cells of Brevibacterium linens SR3 and purified to homogeneity by a combination of Phenyl-Sepharose, DEAE-Sepharose, Q-Sepharose and Sepharose CL-6B chromatography. Optimal temperature for enzymatic activity was 45 degrees C for API and 37 degrees C forAPII, and the pH optimum was found to be 8.5 for API and 8.0 for APII. Divalent metals ions like Co2+ and Ni2+ increased enzymatic activity while Ca2, Cu2+ and Fe2+ had an inhibitory effect. The enzymes were strongly inhibited by EDTA, 1,10-Phenantroline and cysteine, indicating that both aminopeptidases were metalloenzymes. The K-m values of API and APII for L-leucine-p-nitroanilide were 1.0 and 0.25 mM, respectively. Native molecular masses of aminopeptidases I and II were 80 and 220 kDa after gel filtration chromatography while molecular masses of 14 and 18 kDa, were seen, after SDS-polyacrylamide gel electrophoresis. (C) 2000 Elsevier Science Ltd. All rights reserved.

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Documento generato il 07/07/20 alle ore 17:36:58