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Titolo:
Dipeptidyl peptidase IV from porcine skeletal muscle: purification and biochemical properties
Autore:
Sentandreu, MA; Toldra, F;
Indirizzi:
CSIC, Inst Agroquim & Technol Alimentos, Burjassot 46100, Valencia, Spain CSIC Burjassot Valencia Spain 46100 tos, Burjassot 46100, Valencia, Spain
Titolo Testata:
FOOD CHEMISTRY
fascicolo: 2, volume: 75, anno: 2001,
pagine: 159 - 168
SICI:
0308-8146(200111)75:2<159:DPIFPS>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEOLYTIC-ENZYME LEVELS; AMINO-ACID-SEQUENCE; HPLC PURIFICATION; SERINE PROTEASES; HUMAN-PLACENTA; AMINOPEPTIDASE; DEGRADATION; INHIBITOR; MEMBRANE; PROTEIN;
Keywords:
dipeptidyl peptidase; muscle proteolysis; peptide; enzyme purification; meat; protease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Toldra, F CSIC, Inst Agroquim & Technol Alimentos, Apartado 73, Burjassot 46100, Valencia, Spain CSIC Apartado 73 Burjassot Valencia Spain 46100 Valencia, Spain
Citazione:
M.A. Sentandreu e F. Toldra, "Dipeptidyl peptidase IV from porcine skeletal muscle: purification and biochemical properties", FOOD CHEM, 75(2), 2001, pp. 159-168

Abstract

Dipeptidyl peptidase IV (EC 3. 4. 14. 5) from porcine skeletal muscle has been purified to homogeneity by selective protein fractionation with ammonium sulfate and HPLC separations with strong anion-exchange chromatography. Pure DPP IV showed a single band with Mr about 70 kDa by SDS-PAGE and optimum activity at pH 8.0 and 45 degreesC. Substrates best hydrolyzed were those containing a proline residue in the penultimate position at the N-terminal, but it was also possible to hydrolyze (in lower amounts), X-Ala- synthetic and peptide substrates. The presence of diprotin A, puromycin, Co2+ and Fe2+ considerably inhibited DPP IV activity. A contribution of DPP IV action to the total proteolytic activity occurring in postmortem muscle during meat storage and ripening of meat products is feasible and could contribute to flavor generation in those products. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 12:37:12