Zhi Yang

ORCID: 0000-0001-8062-5737
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About
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Research Areas
  • Proteins in Food Systems
  • Polysaccharides Composition and Applications
  • Food composition and properties
  • Microencapsulation and Drying Processes
  • Protein Hydrolysis and Bioactive Peptides
  • Meat and Animal Product Quality
  • Lignin and Wood Chemistry
  • Food Chemistry and Fat Analysis
  • Phytase and its Applications
  • Biofuel production and bioconversion
  • Pickering emulsions and particle stabilization
  • Thyroid Cancer Diagnosis and Treatment
  • Carbon Nanotubes in Composites
  • Risk and Safety Analysis
  • Advanced Cellulose Research Studies
  • Structural Health Monitoring Techniques
  • Muscle metabolism and nutrition
  • Microbial Metabolites in Food Biotechnology
  • Chronic Kidney Disease and Diabetes
  • Catalysis for Biomass Conversion
  • Thyroid and Parathyroid Surgery
  • Advanced Sensor and Energy Harvesting Materials
  • Electrospun Nanofibers in Biomedical Applications
  • Enzyme Production and Characterization
  • Catalytic Processes in Materials Science

WuXi AppTec (China)
2025

University of Hawaiʻi at Mānoa
2025

Massey University
2020-2024

Oak Ridge National Laboratory
2019-2023

Northwest University
2022

Suzhou Research Institute
2017-2022

Central South University
2020-2022

Tang Du Hospital
2022

Xiangya Hospital Central South University
2020-2022

Binzhou University
2021

We investigate the strain hardening behavior of various gelatin networks—namely physical gel, chemically cross-linked and a hybrid gel made combination former two—under large shear deformations using pre-stress, ramp, amplitude oscillations protocols. Further, internal structures gels were characterized by small angle neutron scattering (SANS) to enable their be correlated with nonlinear rheology. The Kratky plots SANS data demonstrate presence aggregates within network whereas, in gels,...

10.1021/acs.biomac.5b01538 article EN Biomacromolecules 2015-12-15

Abstract This study aimed to investigate the properties of heat-induced gels (85 °C for 30 min) quinoa protein isolate (QPI) in presence and absence various polysaccharides including guar gum (GG), locust bean (LBG), xanthan (XG) at pH 7. For this purpose, samples with three concentrations (0.05, 0.1, 0.2 wt%) a fixed QPI concentration (10 ionic strength (50 mM NaCl) were studied terms their gelation behaviour, small large deformation rheological properties, water holding capabilities,...

10.1007/s11483-022-09720-3 article EN cc-by Food Biophysics 2022-02-22

Concentrated emulsions were prepared at a fixed oil concentration (50 wt%) using faba bean protein isolates (FPI) as an emulsifier and texturizer. Effects of FPI (1, 3 5 wt%; pH7), pH (pH 3, 5, 7, 9; addition salts (200 mM NaCl 40 CaCl2; wt% 7) on the emulsion formation studied. The droplet size microstructural characteristics examined by static light scattering confocal laser scanning microscopy (CLSM), viscoelastic behaviours characterised oscillatory rheology. At all different...

10.1016/j.colsurfa.2023.131622 article EN cc-by-nc-nd Colloids and Surfaces A Physicochemical and Engineering Aspects 2023-05-10

The effect of thermosonication (TS) (90 °C, 10-30 min) on the fibrillisation faba bean protein isolate (FPI) was studied. self-assembly behaviour, microstructural characteristics and techno-functional (gelation emulsification) properties FPI fibrils obtained from TS treatment were compared with those conventional prolonged heating (CH) at 90 °C up to 8 h. Compared CH treatment, shown significantly accelerate formation prominent β-sheet structures as revealed by Thioflavin T (ThT)...

10.1016/j.foodhyd.2024.110127 article EN cc-by-nc Food Hydrocolloids 2024-04-22

Self-assembled micelles based on octenyl succinic anhydride (OSA)-modified starch were prepared to enhance the solubility of β-carotene. The critical micelle concentration (CMC) was lower for OSA-modified with a molecular weight (Mw) or higher degree substitution (DS). Above CMC, assembled into spherical an average hydrodynamic diameter <20 nm, as determined by dynamic light scattering (DLS). All radii gyration ( Rg), obtained from Guinier fitting small-angle X-ray (SAXS) data, between 3 and...

10.1021/acs.jafc.9b00355 article EN Journal of Agricultural and Food Chemistry 2019-05-22

In this study, the gel properties of myofibrillar proteins (MPs) from four meat sources (fish, beef, sheep, and pork) were compared. Oscillatory rheology measurements including temperature sweep, frequency strain sweep conducted to characterise small large deformation rheological MPs. addition, sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE) scanning electron microscopy (SEM) used evaluate differences in molecular weight distribution as well microstructures among different...

10.1016/j.lwt.2021.112458 article EN cc-by-nc-nd LWT 2021-09-12

Hydrolysis-induced coagulation of casein micelles by pepsin occurs during the digestion milk. In this study, effect pH (6.7-5.3) and concentration (0.110-2.75 U/mL) on hydrolysis κ-casein in bovine skim milk was investigated at 37°C using reverse-phase HPLC, oscillatory rheology, confocal laser scanning microscopy. The followed a combined kinetic model first-order putative denaturation. rate increased with increasing given pH, dependent, reached maximum ∼6.0. Both increase decrease resulted...

10.3168/jds.2021-21177 article EN cc-by-nc-nd Journal of Dairy Science 2022-01-05

The effect of thermosonication (TS) (90 °C, 10-30 min) on faba bean protein isolate (FPI) at pH 7 was investigated. microstructural and techno-functional properties TS-treated FPI were compared with native or treated conventional prolonged heating (CH, up to 8 h) 90 °C. TS treatment effectively converted amorphous aggregates containing predominant β-sheet secondary structures, as determined by Thioflavin T (ThT) fluorescence circular dichroism (CD). According sodium dodecyl...

10.1016/j.foodhyd.2024.110140 article EN cc-by-nc-nd Food Hydrocolloids 2024-04-30

The kinetics of pepsin-induced κ-casein hydrolysis and coagulation in cow, goat, sheep milk were investigated at 37°C, pH 6.3 6.0. At a 0.1 U/mg pepsin-to-κ-casein ratio, showed the fastest hydrolysis, followed by cow goat as assessed quantifying release para-κ-casein using RP-HPLC. Sheep coagulated most rapidly, with 64% 59% Goat required higher levels (90% 86% 6.0), before could occur. formed denser curds, whereas curd had more porous structure. Additionally, small-angle neutron scattering...

10.1016/j.idairyj.2024.105898 article EN cc-by International Dairy Journal 2024-02-08

The effects of three alcoholic solvents, including monohydric n-octanol, dihydric ethylene glycol, and trihydric glycerol, on the process biomass liquefaction were studied by thermogravimetry (TG) analysis. results showed that there stages during liquefaction, dehydration, volatilization alcoholysis. At stage alcoholysis, solvents combined with fragments from cracking, which resulted in exothermic reaction formed lowly volatile compounds. temperature TR alcoholysis increased following order:...

10.1021/ef900590b article EN Energy & Fuels 2009-08-25
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