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Titolo:
EVIDENCE OF PROTEOLYTIC ACTIVITY AND ITS EFFECT ON GELATION OF MYOFIBRILLAR PROTEIN-CONCENTRATE FROM BOVINE CARDIAC-MUSCLE
Autore:
WANG BW; XIONG YL;
Indirizzi:
UNIV KENTUCKY,DEPT ANIM SCI,FOOD SCI SECT LEXINGTON KY 40546 UNIV KENTUCKY,DEPT ANIM SCI,FOOD SCI SECT LEXINGTON KY 40546
Titolo Testata:
Journal of agricultural and food chemistry
fascicolo: 8, volume: 46, anno: 1998,
pagine: 3054 - 3059
SICI:
0021-8561(1998)46:8<3054:EOPAAI>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURIMI; CHICKEN; INHIBITORS; FISH; BEEF; GEL; TEMPERATURE; ACTOMYOSIN; MYOSIN; PORK;
Keywords:
BEEF HEART; MYOFIBRILLAR PROTEIN; PROTEOLYSIS; PROTEASE INHIBITOR; GELATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
B.W. Wang e Y.L. Xiong, "EVIDENCE OF PROTEOLYTIC ACTIVITY AND ITS EFFECT ON GELATION OF MYOFIBRILLAR PROTEIN-CONCENTRATE FROM BOVINE CARDIAC-MUSCLE", Journal of agricultural and food chemistry, 46(8), 1998, pp. 3054-3059

Abstract

To explore the impact of endogenous proteases on the gelation properties of beef heart surimi, the surimi samples were incubated at different temperatures. Maximum (4.8 N) and minimum (3.3 N) gel strengths were produced by surimi sols preincubated at 60 and 50 degrees C, respectively. Preincubation at 60 degrees C as well as slow linear heating also produced gels with the highest storage modulus and water-holding capacity. Proteolytic activity with an optimum pH of 5.0 and temperatureclose to 50 degrees C was discovered. Addition of protease inhibitors, particularly bovine plasma powder, reduced the extent of gel weakening caused by the proteases and, concomitantly, enhanced the water-holding capacity of the surimi gel. SDS-PAGE showed that in the absence ofprotease inhibitors, myosin was partially hydrolyzed and a 130 kDa polypeptide formed during preincubation at 50 degrees C. Bovine plasma powder and egg white inhibited the formation of the new poly-peptide.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 15:14:12