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Titolo:
THERMAL-BEHAVIOR OF BASIC-AMINO-ACID RESIDUES OF MUSCLE PROTEIN DURING THE INCUBATION OF FISH AND POULTRY MINCES
Autore:
HOSSAIN SMZ; ITO T; KANOH S; NIWA E;
Indirizzi:
MIE UNIV,FAC BIORESOURCES TSU MIE 5178507 JAPAN
Titolo Testata:
Fisheries science
fascicolo: 1, volume: 64, anno: 1998,
pagine: 121 - 124
SICI:
0919-9268(1998)64:1<121:TOBROM>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Keywords:
THERMAL DENATURATION; BASIC AMINO ACID RESIDUES; ACIDIC DYE-BINDING ABILITY; ALKALIMETRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
6
Recensione:
Indirizzi per estratti:
Citazione:
S.M.Z. Hossain et al., "THERMAL-BEHAVIOR OF BASIC-AMINO-ACID RESIDUES OF MUSCLE PROTEIN DURING THE INCUBATION OF FISH AND POULTRY MINCES", Fisheries science, 64(1), 1998, pp. 121-124

Abstract

The thermal behavior of basic amino acid residues of muscle proteins during incubating fish and poultry minces was investigated. For the transglutaminase-free muscle minces from Alaska pollack, Pacific mackerel, and horse mackerel, their acidic dye-binding ability was increased upon their incubation at 30 degrees C for 5 h and simultaneously, the rise of pH was suppressed in their titration with 0.1 N NaOH. The increment of the dye-binding ability and the suppression of pH rise, however, were not observed for the minces from beef, chicken, and pork. Based on the above results, it was presumed that the basic amino acid residues are easy-to-expose on the molecular surface of fish proteins during the incubation but hard-to-expose in the case of poultry proteins.

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Documento generato il 26/11/20 alle ore 14:27:50