Journal
MEAT SCIENCE
Volume 88, Issue 3, Pages 462-467Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2011.01.027
Keywords
Protein oxidation; Protein aggregation; Hydrophobicity; In vitro digestibility; Cantonese sausage
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Funding
- Science and Technology Program of Guangdong Province [2008A024200007, 2009A020101002]
- National Special Funds for Scientific Research on Public Causes of Agriculture [200903012]
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The physicochemical changes of sarcoplasmic proteins, especially oxidation behaviour, were measured to determine their mechanism of action on in vitro protein digestibility during Cantonese sausage processing. The results indicated that carbonyl level increased (p<0.05) during the process. The fluorescence loss of tryptophan residues was a direct consequence of the oxidative degradation. All the parameters of protein aggregation were highly (p<0.05) correlated with carbonyl level and protein surface hydrophobicity (H(o)), indicating that protein oxidation and thermal denaturation could induce protein aggregation, leading to secondary structural changes. The analysis of in vitro digestibility showed no correlation between pepsin activity and protein oxidation, due to the biphasic response of sarcoplasmic proteins toward proteolysis. However, a highly significant (p<0.05) correlation was observed with trypsin and alpha-chymotrypsin activity, indicating that protein oxidation induced the changes in H(o), protein aggregation and secondary structure, which further influenced in vitro digestibility. (c) 2011 Elsevier Ltd. All rights reserved.
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