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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of the Scien...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of the Science of Food and Agriculture
Article . 2018 . Peer-reviewed
License: Wiley Online Library User Agreement
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The effect of cooking temperature on the aggregation and digestion rate of myofibrillar proteins in Jinhua ham

Authors: Chang‐Yu Zhou; Dao‐Dong Pan; Yang‐Ying Sun; Chun‐Bao Li; Xing‐Lian Xu; Jin‐Xuan Cao; Guang‐Hong Zhou;

The effect of cooking temperature on the aggregation and digestion rate of myofibrillar proteins in Jinhua ham

Abstract

AbstractBACKGROUNDIn order to evaluate the effect of cooking temperature on the nutrition quality of dry‐cured hams, 60 biceps femoris samples from 16 Jinhua hams were divided into four groups (control, 70, 100 and 120 °C) and cooked for 30 min. Carbonyl content, sulfhydryl groups, surface hydrophobicity, microstructure, protein aggregation and digestibility of myofibrillar proteins were investigated.RESULTSCooking promoted carbonylation and decreased sulfhydryl groups in a temperature‐dependent way. Scanning electron microscopy and Nile Red revealed that protein aggregation became a main phenomenon at 120 °C; it coincided with surface hydrophobicity. The increased carbonyl content and decreased sulfhydryl groups contributed to the formation of aggregates. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis profiles showed the initial difference in proteolysis rate among four groups. The in vitro digestibility of pepsin and of trypsin and α‐chymotrypsin increased from the control to 100 °C and decreased from 100 to 120 °C.CONCLUSIONThe increased digestibility could be attributed to the oxidation of proteins and exposing recognition sites of digestive enzymes, while the decreased digestibility was due to the formation of aggregates. Cooking was a main factor that affected the digestibility of Jinhua ham, and cooking at 100 °C could be an ideal way to gain the highest digestibility of Jinhua ham. © 2018 Society of Chemical Industry

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Keywords

China, Meat, Swine, Temperature, Muscle Proteins, Protein Aggregates, Myofibrils, Microscopy, Electron, Scanning, Animals, Digestion, Cooking, Sulfhydryl Compounds

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
71
Top 1%
Top 10%
Top 1%
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