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Titolo:
Purification of balansain I, an endopeptidase from unripe fruits of Bromelia balansae Mez (Bromeliaceae)
Autore:
Pardo, MF; Lopez, LMI; Canals, F; Aviles, FX; Natalucci, CL; Caffini, NO;
Indirizzi:
Natl Univ La Plata, Fac Ciencias Exactas, LIPROVE, Dept Ciencias Biol, RA-1900 La Plata, Argentina Natl Univ La Plata La Plata Argentina RA-1900 A-1900 La Plata, Argentina Univ Autonoma Barcelona, Inst Biol Fonamental, E-08193 Barcelona, Spain Univ Autonoma Barcelona Barcelona Spain E-08193 E-08193 Barcelona, Spain
Titolo Testata:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
fascicolo: 9, volume: 48, anno: 2000,
pagine: 3795 - 3800
SICI:
0021-8561(200009)48:9<3795:POBIAE>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; STEM BROMELAIN; PROTEINASES; BINDING; ANANAIN;
Keywords:
plant endopeptidase; Bromelia balansae; Bromeliaceae; purification;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Natalucci, CL Natl Univ La Plata, Fac Ciencias Exactas, LIPROVE, Dept Ciencias Biol, CC 711, RA-1900 La Plata, Argentina Natl Univ La Plata CC 711 LaPlata Argentina RA-1900 entina
Citazione:
M.F. Pardo et al., "Purification of balansain I, an endopeptidase from unripe fruits of Bromelia balansae Mez (Bromeliaceae)", J AGR FOOD, 48(9), 2000, pp. 3795-3800

Abstract

A new plant endopeptidase was obtained from unripe fruits of Bromelia balansae Met (Bromeliaceae). Crude extracts were partially purified by ethanol fractionation. This preparation (redissolved ethanol precipitate, REP) showed maximum activity at pH 8.8-9.2, was very stable even at high ionic strength values (no appreciable decrease in proteolytic activity could be detected after 24 h in 1 M sodium chloride solution at 37 degrees C), and exhibited high thermal stability (inactivation required heating for 60 min at 75 degrees C). Anion exchange chromatography allowed the isolation of a fraction purified to mass spectroscopy, SDS-PAGE, and IEF homogeneity, named balansain I, with pi 5.45 and molecular mass 23192 (mass spectrometry). The purification factor is low (2.9-fold), but the yield is high (48.3%), a common occurrence in plant organs with high proteolytic activity, where proteases represent the bulk of protein content of crude extracts. Balansain I exhibits a similar but narrower pH profile than that obtained for REP, with a maximum pH value similar to 9.0 and was inhibited by E-64 and other cysteine peptidases inhibitors but not affected by inhibitors of the other catalytic types of peptidases. The alanine and glutamine derivatives of N-alpha-carbobenzoxy-L-amino acid p-nitrophenyl esters was strongly preferred by the enzyme. The N-terminal sequence of balansain I showed a very high homology (85-90%) with other known Bromeliaceae endopeptidases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 11:49:01