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
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Characterization of two novel thermostable esterases from Thermoanaerobacterium thermosaccharolyticum Characterization of two novel thermostable esterases from Thermoanaerobacterium thermosaccharolyticum](/preview/png/8359250.png)
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,