16 results on '"Ni, Hui"'
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2. Ultra-high pressure assisted extraction of polysaccharide from Bangia fusco-purpurea: Structure and in vitro hypolipidemic activity
3. A disulfide bond mutant of Pseudoalteromonas porphyrae κ-carrageenase conferred improved thermostability and catalytic activity and facilitated its utilization in κ-carrageenan industrial waste residues recycling
4. Enzymatic hydrolysates of κ-carrageenan by κ-carrageenase-CLEA immobilized on amine-modified ZIF-8 confer hypolipidemic activity in HepG2 cells
5. In vitro fermentation of Bangia fusco-purpurea polysaccharide by human gut microbiota and the protective effects of the resultant products on Caco-2 cells from lipopolysaccharide-induced injury
6. Structural characterization and antioxidant activity of polysaccharides extracted from Porphyra haitanensis by different methods
7. Structural characterization and pro-angiogenic property of a polysaccharide isolated from red seaweed Bangia fusco-purpurea
8. A low-molecular-weight ascophyllan prepared from Ascophyllum nodosum: Optimization, analysis and biological activities
9. Enhancement in affinity of Aspergillus niger JMU-TS528 α-L-rhamnosidase (r-Rha1) by semiconservative site-directed mutagenesis of (α/α)6 catalytic domain
10. Improving the thermostability by introduction of arginines on the surface of α-L-rhamnosidase (r-Rha1) from Aspergillus niger
11. Improvement thermostability of Pseudoalteromonas carrageenovora arylsulfatase by rational design
12. Characterization of an arylsulfatase from a mutant library of Pseudoalteromonas carrageenovora arylsulfatase
13. Characterization and immobilization of arylsulfatase on modified magnetic nanoparticles for desulfation of agar
14. Characterization of an alkaline β-agarase from Stenotrophomonas sp. NTa and the enzymatic hydrolysates
15. Expression and biochemical characterization of recombinant α-l-rhamnosidase r-Rha1 from Aspergillus niger JMU-TS528
16. Enhancement in affinity of Aspergillus niger JMU-TS528 α-L-rhamnosidase (r-Rha1) by semiconservative site-directed mutagenesis of (α/α) 6 catalytic domain.
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