کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10603427 | 982479 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and characterization of d-Gal-6-sulfurylase from Eucheuma striatum
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
d-Gal-6-sulfurylase catalyzing the conversion of μ-carrageenan into κ-carrageenan was extracted from Eucheuma striatum and purified by ammonium sulfate precipitation, hydrophobic interaction chromatography and ion exchange chromatography. The purified enzyme was a monomeric protein with a molecular mass of about 65 kDa as shown in SDS-PAGE. The maximum activity of the enzyme was observed at pH 7.0 and temperature 40 °C. Km value for μ-carrageenan was 4.31 mM, and the corresponding Vmax was 0.17 mM minâ1. The carrageenan treated with 10 U of the purified enzyme exhibited 7.1-fold increase in gel strength with a removal of 30% sulfate groups. 1H NMR spectral analysis of the control and enzyme treated carrageenan confirmed the conversion of μ- into κ-carrageenan and highlighted the specificity of Gal-6-sulfurylase for μ-carrageenan. This Gal-6-sulfurylase provides an eco-friendly and alternative for alkali treatment method to produce high gel strength κ-carrageenan.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Carbohydrate Polymers - Volume 96, Issue 1, 1 July 2013, Pages 9-14
Journal: Carbohydrate Polymers - Volume 96, Issue 1, 1 July 2013, Pages 9-14
نویسندگان
Xiaojuan Qin, Chaoyang Ma, Zaixiang Lou, Aimei Wang, Hongxin Wang,