期刊
FOOD CHEMISTRY
卷 214, 期 -, 页码 710-716出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2016.07.115
关键词
Trypsin; Surface hydrophobicity; Secondary structures; Absorption capacity; Volatile compounds
资金
- National Natural Science Foundation of Chinat [31471681]
- Modern Agricultural Technical System Foundation [CARS-43-17]
- National Agricultural Transformation of Scientific and Technological Achievements Projects of China [2013GB2C200191]
- Scientific and Technological program of Ningbo University [XKL14D2087, 2013C910017]
- K.C. Wong Magna Fund at Ningbo University
In order to investigate the mechanism between flavor binding and proteins degradation during meat processing, the influence of different trypsin contents on the structure of myosin and the adsorption capacity on aldehydes and ketones was determined. The 1% treatment produced subfragment 2 (S2), light meromyosin (LMM) and decreased 18 and 16 kDa light chains; 5% and 10% treatments produced 100 and 65 kDa new bands and more S2, LMM and cleaned light chains. With the rising trypsin contents, beta-sheet, beta-turn, random coil, hydrophobicity and total sulfydryl content increased; solubility, alpha-helix and free percentages of aldehydes and ketones decreased. The increase of absorbing capacity could be attributed to the increased hydrophobicity and total sulphydryl and the unfolding of secondary structures by exposing reactive amino and thiol groups and hydrophobic sites; the decreased solubility was related to the increased hydrophobicity. The trypsin-dose dependent proteolysis of myosin increased the retention of volatile compounds. (C) 2016 Elsevier Ltd. All rights reserved.
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