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A highly sensitive method has been developed for accurately measuring dextranase activity using 3-methyl-2-benzothiazolinone hydrazine. This method is based on the dextran refinement and fast-dissolving approach established in this study, as well as the assay method for enzymatic hydrolysates. The measurement parameters for the reducing sugar ends were optimized by examining the slope, intercept, R, and time stability of the standard curve of glucose solutions containing dextran. Kinetic determination was utilized to optimize enzymatic parameters and validate the method, which was subsequently utilized for the analysis of toothpaste and mouthwash. The findings suggest that the enzymatic hydrolysis follows a zero-order reaction, laying a solid foundation for the end-point assay of dextranase activity. The results demonstrated a linear correlation within the measurement range (0.7-6.5 mU/mL), exhibiting good repeatability, high sensitivity and accuracy. This method outperformed the 3,5-dinitrosalicylic acid method and circumvented potential interference from other components in toothpaste and mouthwash.
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http://dx.doi.org/10.1016/j.foodchem.2024.141292 | DOI Listing |
Biosci Biotechnol Biochem
September 2025
Department of Bioscience, Graduate School of Science and Technology, Shizuoka University, Shizuoka, Japan.
Glycoside hydrolase family 27 (GH27) consists primarily of exo-acting enzymes, including α-galactosidase, α-N-acetylgalactosaminidase, β-L-arabinopyranosidase, and isomalto-dextranase. Here, we examined the gene expression profiles and biochemical characteristics of a multi-domain protein, Fjoh_4436 (named FjGH27A), which contains a GH27 catalytic domain and is encoded upstream of the previously described branched dextran utilization locus in Flavobacterium johnsoniae. Expression of this gene increased 7.
View Article and Find Full Text PDFJ Colloid Interface Sci
December 2025
DWI-Leibniz Institute for Interactive Materials, RWTH Aachen University, Forckenbeckstraße 50, 52074 Aachen, Germany; Institute for Technical and Macromolecular Chemistry, RWTH Aachen University, Worringerweg 2, 52074 Aachen, Germany. Electronic address:
Colloidal hydrogels, also known as microgels, are promising scaffold materials in the biomedical field. Microgels exhibit high biocompatibility, porosity, and mechanical stability, crucial in supporting cell development. Bio-based polymers, such as fibrin or dextran, are desirable for controlling the properties of microgels.
View Article and Find Full Text PDFCrit Rev Microbiol
May 2025
Departamento de Microbiologia e Parasitologia, Instituto Biomédico, Universidade Federal Fluminense, Niterói, Brazil.
Biofilms are one of the most successful modes of life in the biosphere. In these assemblages, bacteria usually display higher resistance to environmental stressors, thus making their removal through the use of conventional approaches significantly more difficult. Currently, biofilms are one of the major challenges in healthcare settings, often resulting in higher mortality and morbidity rates.
View Article and Find Full Text PDFSheng 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 PDFFood 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: