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Titolo:
Properties of a milk clotting protease isolated from fruits of Bromelia balansae Mez
Autore:
Pardo, MF; Lopez, LMI; Caffini, NO; Natalucci, CL;
Indirizzi:
Natl Univ La Plata, Fac Ciencias Exactas, Dept Ciencias Biol, LIPROVE, RA-1900 La Plata, Argentina Natl Univ La Plata La Plata Argentina RA-1900 A-1900 La Plata, Argentina
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 5, volume: 382, anno: 2001,
pagine: 871 - 874
SICI:
1431-6730(200105)382:5<871:POAMCP>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; CYSTEINE-PROTEINASES; ARABIDOPSIS-THALIANA; GERMINATING-SEEDS; STEM BROMELAIN; UNRIPE FRUITS; EXPRESSION; CDNA; PURIFICATION; CLONING;
Keywords:
Bromeliaceae; cysteine peptidase; food protein hydrolysis; N-terminal sequence homology; plant endopeptidase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Caffini, NO Natl Univ La Plata, Fac Ciencias Exactas, Dept Ciencias Biol, LIPROVE, CC 711, RA-1900 La Plata, Argentina Natl Univ La Plata CC 711 La Plata Argentina RA-1900 rgentina
Citazione:
M.F. Pardo et al., "Properties of a milk clotting protease isolated from fruits of Bromelia balansae Mez", BIOL CHEM, 382(5), 2001, pp. 871-874

Abstract

Unripe fruit extracts of Bromelia balansae Met (Bromeliaceae), whose principal endopeptidase is balansain I (isolated for anion exchange chromatography: pl = 5.45, molecular weight = 23 192), exhibit a pH profile with a maximum activity around pH 9.0 and are inhibited only by cysteine peptidases inhibitors. The alanine and glutamine derivatives of N-alpha -carbobenzoxy-L-amino acid p-nitrophenyl esters were strongly preferred by the enzyme. Enzymatic hydrolysis of milk and soy proteins yield characteristic patterns at pH 9.0. The N-terminal sequence showed a very high homology (85-90%) with other known Bromeliaceae endopeptidases.

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Documento generato il 11/07/20 alle ore 13:16:27