کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7583785 | 1492021 | 2019 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Formation of allysine in β-lactoglobulin and myofibrillar proteins by glyoxal and methylglyoxal: Impact on water-holding capacity and in vitro digestibility
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The ability of α-dicarbonyls, glyoxal (GO) and methyl-glyoxal (MGO) (2 M), to induce the formation of allysine in β-lactoglubulin (LAC), and myofibrillar proteins (MP) (2â¯mg/mL) during incubation at 80â¯Â°C for 48â¯h, was studied. Both GO and MGO induced the formation of allysine in all tested proteins with GO being more reactive (23.8 and 8.6â¯nmoles/mg protein in LAC and MP respectively after 6â¯h) than MGO (2.6 and 3.1â¯nmoles/mg protein at the same sampling point). LAC seemed to be more susceptible to the glycation reactions than MP. The concentration of allysine decreased at 24â¯h along with a concomitant increase of advanced-glycation end-products suggesting that allysine may be involved in the formation of fluorescent adducts. The water-holding capacity and trypsin-chymotrypsin digestibility of the proteins decreased during the incubation assay. The mechanisms by which α-dicarbonyls-mediated carbonylation likely influenced the impairment of such protein properties are thoroughly discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 271, 15 January 2019, Pages 87-93
Journal: Food Chemistry - Volume 271, 15 January 2019, Pages 87-93
نویسندگان
Carolina Luna, Mario Estévez,