کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5792801 | 1109645 | 2011 | 6 صفحه PDF | دانلود رایگان |

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 (H0), 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 α-chymotrypsin activity, indicating that protein oxidation induced the changes in H0, protein aggregation and secondary structure, which further influenced in vitro digestibility.
Journal: Meat Science - Volume 88, Issue 3, July 2011, Pages 462-467