6ife

Publication Abstract from PubMed

beta-Xylosidase, of the glycoside hydrolase family 43 from Bacillus sp. HJ14, was expressed in Escherichia coli. Recombinant beta-xylosidase (rHJ14GH43) exhibited maximum activity at 25 degrees C, approximately 15, 45, and 88% of maximum activity at 0, 10, and 20 degrees C, respectively, and poor stability at temperatures over 20 degrees C. rHJ14GH43 showed moderate or high activity, but poor stability, in NaCl, KCl, NaNO3, KNO3, Na2SO4, and (NH4)2SO4 at concentrations from 3.0 to 30.0% (w/v). The crystal structure of rHJ14GH43 was resolved and showed higher structural flexibility due to fewer salt bridges and hydrogen bonds compared to mesophilic and thermophilic beta-xylosidases. High structural flexibility is presumed to be a key factor for catalytic adaptations to low temperatures and high salt concentrations. Approximately one-third of the surface of rHJ14GH43 is positively charged, which may be the primary factor responsible for poor stability in high neutral salt environments.

Biochemical and structural properties of a low-temperature-active glycoside hydrolase family 43 beta-xylosidase: Activity and instability at high neutral salt concentrations.,Zhang R, Li N, Liu Y, Han X, Tu T, Shen J, Xu S, Wu Q, Zhou J, Huang Z Food Chem. 2019 Dec 15;301:125266. doi: 10.1016/j.foodchem.2019.125266. Epub 2019, Jul 27. PMID:31387037^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.