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Changes in conformation and in sulfhydryl groups of actomyosin of tilapia ( Orechromis niloticus) on hydrostatic pressure treatment
Ist Teil von
Food chemistry, 2007, Vol.103 (2), p.560-564
Ort / Verlag
Oxford: Elsevier Ltd
Erscheinungsjahr
2007
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
Actomyosin extracted from tilapia muscle was subjected to hydrostatic pressure treatment (50–300
MPa, 10–60
min, 4
°C) to investigate the changes in sulfhydryl groups and on conformation. Transmission electron microscopy showed that the structure of actomyosin was aggregated and disrupted above 100
MPa, and more regular network aggregates were observed as pressure increased. Moreover, pressurisation at 50
MPa for 10
min did not change actomyosin structures. Using SDS–PAGE analysis, molecules larger than the myosin heavy chain were observed when actomyosin was treated at and above 200
MPa. Below 200
MPa actomyosin formed aggregates, mainly with hydrogen bonds. Surface sulfhydryl group content of actomyosin increased with increased pressure, up to 250
MPa. However, total sulfhydryl group content of actomyosin decreased with increased pressure and time. According to this study, 200
MPa would be the critical pressure that induced actomyosin to form regular network structures.