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Food Chem. 2017 Jan 1;214:710-716. doi: 10.1016/j.foodchem.2016.07.115. Epub 2016 Jul 20.

Effect of trypsin treatments on the structure and binding capacity of volatile compounds of myosin.

Author information

1
Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China.
2
Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China. Electronic address: caojinxuan@nbu.edu.cn.
3
Department of Food Science, Nanjing University of Finance & Economics, Nanjing 210023, China.
4
College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China.

Abstract

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 16kDa light chains; 5% and 10% treatments produced 100 and 65kDa new bands and more S2, LMM and cleaned light chains. With the rising trypsin contents, β-sheet, β-turn, random coil, hydrophobicity and total sulfydryl content increased; solubility, α-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.

KEYWORDS:

Absorption capacity; Secondary structures; Surface hydrophobicity; Trypsin; Volatile compounds

PMID:
27507529
DOI:
10.1016/j.foodchem.2016.07.115
[Indexed for MEDLINE]

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