کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5132471 1492052 2018 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The effect of oxidation on the structure of G-actin and its binding ability with aroma compounds in carp grass skeletal muscle
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
The effect of oxidation on the structure of G-actin and its binding ability with aroma compounds in carp grass skeletal muscle
چکیده انگلیسی


- Raman spectroscopy and SEM were used to observe the changes of G-actin.
- Low oxidant concentration accelerated the stretch of G-actin.
- High oxidant concentration caused sharp flake aggregation of G-actin.
- 0-5 mM H2O2 enhanced the binding with alcohols by hydrogen bonds.
- 1-20 mM H2O2 increased the binding with aldehydes by surface hydrophobicity and aggregation.

To investigate the influence of oxidative modifications of G-actin on its binding ability with aroma compounds, the influence of H2O2 treatments on G-actin structure and the absorption for alcohols and aldehydes was investigated. Raman spectroscopy and scanning electron microscopy were used to evaluate structural changes of G-actin; GC-MS was used to analyze the binding with alcohols and aldehydes. Results showed that 0-5 mM H2O2 enhanced the absorption of G-actin toward alcohols involved in the formation of hydrogen bonds by increasing α-helix and carbonyl values. 0-1 mM H2O2 caused the release of aldehydes with decreased sulfhydryl sites. 1-20 mM H2O2 increased the retention of aldehydes, due to the increased hydrophobic sites by G-actin rebuilding and aggregating. The aggregated G-actin favoured the hydrophobic interactions with aroma compounds, forming the protein-aroma compound complex, thus enhancing the resultant binding ability, as evidenced by scanning electron microscopy and GC/MS analysis.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 240, 1 February 2018, Pages 346-353
نویسندگان
, , , , ,