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[Site-directed mutagenesis enhances the activity of dextranase from KQ11].
Sheng Wu Gong Cheng Xue Bao
September 2024
School of Food and Biological Engineering, Hefei University of Technology, Hefei 230009, Anhui, China.
Dextranase is an enzyme that specifically hydrolyzes the α-1, 6 glucoside bond. In order to improve the activity of dextranase from KQ11, site-directed mutagenesis was used to modify the amino acids involved in the "tunnel-like binding site". A saturating mutation at position 507 was carried out on this basis.
View Article and Find Full Text PDFDetermination of dextranase activity using 3-methyl-2-benzothiazolinone hydrazone method: Substrate refinement and fast-dissolution, method development and validation.
Food Chem
January 2025
State Key Laboratory Base of Eco-chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, No.53 Zhengzhou Road, Qingdao 266042, China.. Electronic address:
Article Synopsis
- A new sensitive method has been developed to measure dextranase activity using a compound called 3-methyl-2-benzothiazolinone hydrazine, improving upon existing techniques.
- The method focuses on optimizing measurement parameters and validating dynamic enzymatic conditions by analyzing glucose solutions that involve dextran.
- Results reveal that dextranase hydrolysis behaves like a zero-order reaction, leading to a reliable, high-sensitivity assay suitable for testing products like toothpaste and mouthwash, while outperforming previous methods.
Temperature-regulated cascade reaction for homogeneous oligo-dextran synthesis using a fusion enzyme.
Int J Biol Macromol
October 2024
College of Food and Biological Engineering, Hefei University of Technology, Hefei, China. Electronic address:
Based on the principle of cascade reaction, a fusion enzyme of dextransucrase and dextranase was designed without linker to catalyze the production of oligo-dextran with homogeneous molecular weight from sucrose in one catalytic step. Due to the different effects of temperature on the two components of the fusion enzyme, temperature served as the "toggle switch" for the catalytic efficiency of the two-level fusion enzyme, regulating the catalytic products of the fusion enzyme. Under optimal conditions, the fusion enzyme efficiently utilized 100 % of the sucrose, and the yield of oligo-dextran with a homogeneous molecular weight reached 70 %.
View Article and Find Full Text PDFBiochemical properties of a Flavobacterium johnsoniae dextranase and its biotechnological potential for Streptococcus mutans biofilm degradation.
World J Microbiol Biotechnol
May 2024
São Carlos Institute of Physics, University of São Paulo, Avenida Trabalhador São-carlense, 400, Parque Arnold Schimidt, São Carlos, SP, 13566-590, Brazil.
Cariogenic biofilms have a matrix rich in exopolysaccharides (EPS), mutans and dextrans, that contribute to caries development. Although several physical and chemical treatments can be employed to remove oral biofilms, those are only partly efficient and use of biofilm-degrading enzymes represents an exciting opportunity to improve the performance of oral hygiene products. In the present study, a member of a glycosyl hydrolase family 66 from Flavobacterium johnsoniae (FjGH66) was heterologously expressed and biochemically characterized.
View Article and Find Full Text PDFStructural insights into α-(1→6)-linkage preference of GH97 glucodextranase from Flavobacterium johnsoniae.
FEBS J
July 2024
Department of Bioscience, Graduate School of Science and Technology, Shizuoka University, Japan.
Glycoside hydrolase family 97 (GH97) comprises enzymes like anomer-inverting α-glucoside hydrolases (i.e., glucoamylase) and anomer-retaining α-galactosidases.
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