کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6494611 | 44812 | 2014 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization and engineering of 3-ketosteroid-â³1-dehydrogenase and 3-ketosteroid-9α-hydroxylase in Mycobacterium neoaurum ATCC 25795 to produce 9α-hydroxy-4-androstene-3,17-dione through the catabolism of sterols
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
3-Ketosteroid-â³1-dehydrogenase (KstD) is a key enzyme involved in the microbial catabolism of sterols. Here, three homologues of KstD were characterized from Mycobacterium neoaurum ATCC 25795, showing distinct substrate preferences and transcriptional responses to steroids. Single deletion of any MN-kstD failed to result in a stable and maximum accumulation of 9-OHAD due to residual KstD activities. To develop stable 9-OHAD producers, all of these MN-KstDs were inactivated, which led to about 6.02 g lâ1 of 9-OHAD from 15 g lâ1 of phytosterols. However, the product was mixed with 1.55 g lâ1 of AD as a major by-product. To transform AD, the oxygenase component of 3-ketosteroid-9α-hydroxylase (KSH), encoded by kshA, was overexpressed. As a result, the yield of 9-OHAD increased to 7.33 g lâ1 with less than 0.31 g lâ1 of AD and the selectivity of 9-OHAD production was improved to 95-97% among metabolites.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Metabolic Engineering - Volume 24, July 2014, Pages 181-191
Journal: Metabolic Engineering - Volume 24, July 2014, Pages 181-191
نویسندگان
Kang Yao, Li-Qin Xu, Feng-Qing Wang, Dong-Zhi Wei,