کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
11017422 | 1734140 | 2018 | 41 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application](/preview/png/11017422.png)
چکیده انگلیسی
L-Arabinose isomerase isolated from Geobacillus stearothermophilus (GSAI) was modified to improve its substrate specificity for D-galactose for the production of D-tagatose, a potential reduced-energy sweetener. Among the selected residues, mutation at residue 18 produced a mutant strain, H18T, which exhibited increased activity for D-galactose compared with the wild-type (WT) enzyme. Analysis of the substrate specificity of H18T showed a 45.4% improvement for D-galactose. Replacing histidine with threonine at residue 18 resulted in approximately 2.7-fold and 1.8-fold higher substrate binding and catalytic efficiency, respectively, for D-galactose. Further enhancement of the specific activity and catalytic efficiency of H18T for D-galactose by up to 2.7-fold and 4.3-fold, respectively, was achieved by adding borate during L-arabinose isomerase catalysis. Moreover, H18T showed thermostability and no destabilization was detected, which is promising for the industrial production of D-tagatose.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1866, Issue 11, November 2018, Pages 1084-1091
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1866, Issue 11, November 2018, Pages 1084-1091
نویسندگان
Fina Amreta Laksmi, Shigeki Arai, Hirohito Tsurumaru, Yoshitaka Nakamura, Budi Saksono, Masao Tokunaga, Matsujiro Ishibashi,