کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
7587376 1492078 2017 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Effect of trypsin treatments on the structure and binding capacity of volatile compounds of myosin
ترجمه فارسی عنوان
اثر تیمارهای تریپسین بر ساختار و ظرفیت پیوند ترکیبات فرار از میوزین
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی
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, 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 214, 1 January 2017, Pages 710-716
نویسندگان
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