Thermostability improvement of Orpinomyces sp. xylanase by directed evolution
نویسندگان
چکیده
منابع مشابه
Characterization of a cold-active esterase from Serratia sp. and improvement of thermostability by directed evolution
BACKGROUND In recent years, cold-active esterases have received increased attention due to their attractive properties for some industrial applications such as high catalytic activity at low temperatures. RESULTS An esterase-encoding gene (estS, 909 bp) from Serratia sp. was identified, cloned and expressed in Escherichia coli DE3 (BL21). The estS encoded a protein (EstS) of 302 amino acids w...
متن کاملImprovement of oxidative and thermostability of N-carbamyl-d-amino Acid amidohydrolase by directed evolution.
N-Carbamyl-D-amino acid amidohydrolase (N-carbamoylase), which is currently employed in the industrial production of unnatural D-amino acid in conjunction with D-hydantoinase, has low oxidative and thermostability. We attempted the simultaneous improvement of the oxidative and thermostability of N-carbamoylase from Agrobacterium tumefaciens NRRL B11291 by directed evolution using DNA shuffling....
متن کاملDirected evolution of Aspergillus niger glucoamylase to increase thermostability
Using directed evolution and site-directed mutagenesis, we have isolated a highly thermostable variant of Aspergillus niger glucoamylase (GA), designated CR2-1. CR2-1 includes the previously described mutations Asn20Cys and Ala27Cys (forming a new disulfide bond), Ser30Pro, Thr62Ala, Ser119Pro, Gly137Ala, Thr290Ala, His391Tyr and Ser436Pro. In addition, CR2-1 includes several new putative therm...
متن کاملImproving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis.
A heat-stable raw-starch-digesting amylase (RSDA) was generated through PCR-based site-directed mutagenesis. At 65 degrees C, the half-life of this mutant RSDA, which, compared with the wild-type RSDA, lacks amino acids R178 and G179, was increased 20-fold. While the wild type was inactivated completely at pH 3.0, the mutant RSDA still retained 41% of its enzymatic activity. The enhancement of ...
متن کاملImproving the thermostability of a fungal GH11 xylanase via site-directed mutagenesis guided by sequence and structural analysis
BACKGROUND Xylanases have been widely employed in many industrial processes, and thermophilic xylanases are in great demand for meeting the high-temperature requirements of biotechnological treatments. In this work, we aim to improve the thermostability of XynCDBFV, a glycoside hydrolase (GH) family 11 xylanase from the ruminal fungus Neocallimastix patriciarum, by site-directed mutagenesis. We...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Molecular Catalysis B: Enzymatic
سال: 2012
ISSN: 1381-1177
DOI: 10.1016/j.molcatb.2012.04.021