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Titolo:
Characterization of the proteases involved in hydrolyzing paddlefish (Polyodon spathula) myosin
Autore:
Wang, BW; Wang, CZ; Mims, SD; Xiong, YLL;
Indirizzi:
Kentucky State Univ, Human Nutr Program, Frankfort, KY 40601 USA Kentucky State Univ Frankfort KY USA 40601 ogram, Frankfort, KY 40601 USA Kentucky State Univ, Aquaculture Res Ctr, Frankfort, KY 40601 USA KentuckyState Univ Frankfort KY USA 40601 s Ctr, Frankfort, KY 40601 USA Univ Kentucky, Dept Anim Sci, Lexington, KY 40506 USA Univ Kentucky Lexington KY USA 40506 pt Anim Sci, Lexington, KY 40506 USA
Titolo Testata:
JOURNAL OF FOOD BIOCHEMISTRY
fascicolo: 6, volume: 24, anno: 2000,
pagine: 503 - 515
SICI:
0145-8884(200012)24:6<503:COTPII>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
MACKEREL SCOMBER-AUSTRALASICUS; WHITING MERLUCCIUS-PRODUCTUS; CROAKER MICROPOGON-UNDULATUS; CATHEPSIN-L-LIKE; ALKALINE PROTEASE; ATLANTIC CROAKER; STRUCTURAL PROTEINS; SKELETAL-MUSCLE; PURIFICATION; DEGRADATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Wang, CZ Kentucky State Univ, Human Nutr Program, Frankfort, KY 40601 USA Kentucky State Univ Frankfort KY USA 40601 ankfort, KY 40601 USA
Citazione:
B.W. Wang et al., "Characterization of the proteases involved in hydrolyzing paddlefish (Polyodon spathula) myosin", J FOOD BIOC, 24(6), 2000, pp. 503-515

Abstract

An extract from paddlefish surimi possessed activities of B, L, and H-likecathepsins. The optimal pH was around 5.0 for cathepsins B and L, and was between 6.0-6.5 for the H-like cathepsin. The enzyme activities were not impaired by heating at 40C for 20 min. However, the protease extract lost about 20% of its cathepsin B, 50% B+L, and 90% H-like cathepsin activities after heating at 50C for 20 min. The activity of H-like cathepsin was not inhibited by E-64, suggesting that it did not belong to the known cysteine protease group. The protease extract was capable of hydrolyzing myosin heavy chain, producing a major fragment(s) around 140 kDa. Degradation of myosin bythe protease extract was substantially reduced by protease inhibitors including E-64, a protease inhibitor mixture, and bovine plasma powder.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 21:48:12