Yuxiang Bai

ORCID: 0000-0002-4485-4732
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About
Contact & Profiles
Research Areas
  • Enzyme Production and Characterization
  • Microbial Metabolites in Food Biotechnology
  • Food composition and properties
  • Polysaccharides Composition and Applications
  • Phytase and its Applications
  • Enzyme Catalysis and Immobilization
  • Biofuel production and bioconversion
  • Polysaccharides and Plant Cell Walls
  • Proteins in Food Systems
  • Drug Solubulity and Delivery Systems
  • Probiotics and Fermented Foods
  • Protein purification and stability
  • Protein Interaction Studies and Fluorescence Analysis
  • Carbohydrate Chemistry and Synthesis
  • Supramolecular Self-Assembly in Materials
  • Nanocomposite Films for Food Packaging
  • Food Chemistry and Fat Analysis
  • Microencapsulation and Drying Processes
  • Nanomaterials for catalytic reactions
  • Protein Hydrolysis and Bioactive Peptides
  • Ginkgo biloba and Cashew Applications
  • Helicobacter pylori-related gastroenterology studies
  • Pancreatitis Pathology and Treatment
  • Chemotherapy-induced organ toxicity mitigation
  • Dye analysis and toxicity

Jiangnan University
2016-2025

State Key Laboratory of Food Science and Technology
2016-2025

University of Groningen
2013-2017

National Natural Science Foundation of China
2004

Air Force Medical University
2004

Xijing Hospital
2004

Ministry of Education of the People's Republic of China
2004

Diabetes is considered one of the biggest health crises in 21st century. Controlling carbohydrate digestibility by inhibiting starch digestive enzyme (α-amylase and α-glucosidase) activities an efficient strategy to control postprandial hyperglycemia. Over last decade, synthetic inhibitors are most effective pharmaceutical approach for management type 2 diabetes mellitus (T2DM). With increasing global prevalence diabetes, identification alternative with potentially less negative side effects...

10.1016/j.lwt.2021.112455 article EN cc-by-nc-nd LWT 2021-09-11

α-Glucanotransferases of the CAZy family GH70 convert starch-derived donors to industrially important α-glucans. Here, we describe characteristics a novel GtfB-type 4,6-α-glucanotransferase high enzyme activity (60.8 U mg

10.1021/acs.jafc.4c00104 article EN Journal of Agricultural and Food Chemistry 2024-03-01

Starch-converting α-glucanotransferases of glycoside hydrolase family 70 (GH70) are promising enzymatic tools for the production diverse α-glucans with (potential) commercial applications in food and health as biomaterials. In this study, a novel GtfB enzyme from Weissella confusa MBF8-1 was screened National Center Biotechnology Information (NCBI) nonredundant protein database. The (named WcMBF8-1 GtfB) displayed high conservation motifs I–IV other enzymes but possessed unique variations...

10.1021/acs.jafc.3c08425 article EN Journal of Agricultural and Food Chemistry 2024-01-17

4,6-α-Glucanotransferase (4,6-α-GTase) enzymes, such as GTFB and GTFW of Lactobacillus reuteri strains, constitute a new reaction specificity in glycoside hydrolase family 70 (GH70) are novel enzymes that convert starch or hydrolysates into isomalto/maltopolysaccharides (IMMPs). These IMMPs still have linear chains with some α1→4 linkages but mostly (relatively long) α1→6 soluble dietary fibers. 4,6-α-GTase their products significant potential for industrial applications. Here we report an...

10.1128/aem.01860-15 article EN Applied and Environmental Microbiology 2015-08-08

Exopolysaccharides (EPS) of lactic acid bacteria (LAB) are interest for food applications. LAB well-known to produce α-glucan from sucrose by extracellular glucansucrases. Various Lactobacillus reuteri strains also possess 4,6-α-glucanotransferase (4,6-α-GTase) enzymes. Purified 4,6-α-GTases (e.g., GtfB) were shown act on starches (hydrolysates), cleaving α1→4 linkages and synthesizing α1→6 linkages, yielding isomalto-/maltopolysaccharides (IMMP). Here we report that L. cells with these...

10.1021/acs.jafc.6b00714 article EN Journal of Agricultural and Food Chemistry 2016-03-21
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