Scanning Calorimetric Behavior of Tilapia Myosin and Actin due to Processing of Muscle and Protein Purification

Jae W. Park, TYRE C. LANIER

Research output: Contribution to journalArticle

75 Citations (Scopus)

Abstract

The thermal behavior of tilapia muscle proteins was investigated by differential scanning calorimetry at various stages in the processing of surimi and during purification of myosin and actin. A shift in the thermal transition of actin to lower temperature was observed and the enthalpies of denaturation for both actin and myosin decreased with further processing. Salt addition also induced shifts in denaturation transitions to lower temperatures and decreased enthalpies of denaturation.

Original languageEnglish
Pages (from-to)49-51
Number of pages3
JournalJournal of Food Science
Volume54
Issue number1
DOIs
Publication statusPublished - 1989
Externally publishedYes

Fingerprint

Tilapia
Muscle Proteins
Myosins
myosin
denaturation
actin
Actins
enthalpy
muscles
Hot Temperature
heat
processing stages
surimi
Temperature
proteins
Differential Scanning Calorimetry
muscle protein
differential scanning calorimetry
temperature
Salts

ASJC Scopus subject areas

  • Food Science

Cite this

Scanning Calorimetric Behavior of Tilapia Myosin and Actin due to Processing of Muscle and Protein Purification. / Park, Jae W.; LANIER, TYRE C.

In: Journal of Food Science, Vol. 54, No. 1, 1989, p. 49-51.

Research output: Contribution to journalArticle

@article{71b13973aac04240a95f585aa55a264a,
title = "Scanning Calorimetric Behavior of Tilapia Myosin and Actin due to Processing of Muscle and Protein Purification",
abstract = "The thermal behavior of tilapia muscle proteins was investigated by differential scanning calorimetry at various stages in the processing of surimi and during purification of myosin and actin. A shift in the thermal transition of actin to lower temperature was observed and the enthalpies of denaturation for both actin and myosin decreased with further processing. Salt addition also induced shifts in denaturation transitions to lower temperatures and decreased enthalpies of denaturation.",
author = "Park, {Jae W.} and LANIER, {TYRE C.}",
year = "1989",
doi = "10.1111/j.1365-2621.1989.tb08564.x",
language = "English",
volume = "54",
pages = "49--51",
journal = "Journal of Food Science",
issn = "0022-1147",
publisher = "Wiley-Blackwell",
number = "1",

}

TY - JOUR

T1 - Scanning Calorimetric Behavior of Tilapia Myosin and Actin due to Processing of Muscle and Protein Purification

AU - Park, Jae W.

AU - LANIER, TYRE C.

PY - 1989

Y1 - 1989

N2 - The thermal behavior of tilapia muscle proteins was investigated by differential scanning calorimetry at various stages in the processing of surimi and during purification of myosin and actin. A shift in the thermal transition of actin to lower temperature was observed and the enthalpies of denaturation for both actin and myosin decreased with further processing. Salt addition also induced shifts in denaturation transitions to lower temperatures and decreased enthalpies of denaturation.

AB - The thermal behavior of tilapia muscle proteins was investigated by differential scanning calorimetry at various stages in the processing of surimi and during purification of myosin and actin. A shift in the thermal transition of actin to lower temperature was observed and the enthalpies of denaturation for both actin and myosin decreased with further processing. Salt addition also induced shifts in denaturation transitions to lower temperatures and decreased enthalpies of denaturation.

UR - http://www.scopus.com/inward/record.url?scp=84985222628&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84985222628&partnerID=8YFLogxK

U2 - 10.1111/j.1365-2621.1989.tb08564.x

DO - 10.1111/j.1365-2621.1989.tb08564.x

M3 - Article

AN - SCOPUS:84985222628

VL - 54

SP - 49

EP - 51

JO - Journal of Food Science

JF - Journal of Food Science

SN - 0022-1147

IS - 1

ER -