کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8359250 | 1542289 | 2018 | 28 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of two novel thermostable esterases from Thermoanaerobacterium thermosaccharolyticum
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
This paper first describes characterization of two thermostable esterases (ThLip1 and ThLip2) from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum DSM 571. The recombinant esterase ThLip1 was active at 80â¯Â°C, pH 6.5 and maintained approx. 85% of original activity after 2â¯h incubation at 75â¯Â°C. Kinetic parameters, Km, Vmax and kcat/Km for 4-Nitrophenyl caprylate (pNPC) were 3.52â¯Â±â¯0.47â¯mM, 191.18â¯Â±â¯1.82â¯Î¼molâ¯minâ1 mgâ1 and 20.80â¯Â±â¯0.07â¯mMâ1â¯sâ1, respectively. The purified recombinant esterase ThLip2 was optimally active at pH 6.5 and 75â¯Â°C and it was stable against a pH range of 6.0-8.0 possessing 2â¯h half-life at 80â¯Â°C. Kinetic experiments at 75â¯Â°C with pNPC as a substrate gave a Km of 3.37â¯mM, Vmax of 578.14â¯Î¼molâ¯minâ1 mgâ1and kcat of 231.2 sâ1. The hydrolysis of linalyl acetate were carried out using ThLip1 and ThLip2 as catalyst, affording linalool yields over 140â¯mg/l in 10â¯h.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 152, December 2018, Pages 64-70
Journal: Protein Expression and Purification - Volume 152, December 2018, Pages 64-70
نویسندگان
Wenqian Li, Hao Shi, Huaihai Ding, Liangliang Wang, Yu Zhang, Xun Li, Fei Wang,