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Articles by Xin-Huai Zhao
Total Records ( 4 ) for Xin-Huai Zhao
  Mei Hang and Xin-Huai Zhao
  Mao-tofu fermented for 3, 5, 7 and 9 days by a strain of Mucor sp. was extracted with five solvents including 20, 40 or 60% (v/v) ethanol solutions and pH 4.5 or 6.5 water to investigate the impacts of fermentation time and extraction solvent on the in vitro antioxidant property of the extracts. Extraction yield and degree of hydrolysis of the protein fractions in the extracts were measured. Antioxidant properties of the extracts namely scavenging activity on 2,2-diphenyl-1-picrylhydrazyl radical and 2,2’-azino-bis(3-ethyl- benzothiazoline-6-sulfonic acid), iron (III)-reducing activity and iron (II)-chelating activity were evaluated in vitro. The results showed that longer fermentation time of Mao-tofu gave the extracts a higher extraction yield, higher degree of hydrolysis of the protein fractions and higher antioxidant activity. The extract prepared with 60% ethanol solution behaved the highest antioxidant activity while that prepared with pH 4.5 water showed the lowest activity. Five extracts from Mao-tofu fermented for 9 days were analyzed by size exclusion chromatography and the molecular weights of their main protein fractions were found to be from 0.2 to 6.0 kDa. Amino acids analysis showed that total content of six hydrophobic amino acids among the five extracts showed no difference, while ethanol solution extracts had more Arg, Cys and Met but less Ala, Gly and His than that of water extract. Present result revealed that the soluble extracts of Mao-tofu had an improved in vitro antioxidant activity than soybean proteins and both fermentation time of Mucor sp. and solvent types influenced the in vitro antioxidant activity of the extracts.
  Yao Hou and Xin-Huai Zhao
  Soybean Protein Concentrates (SPC) and Soybean Protein Isolates (SPI) were hydrolyzed with trypsin or neutrase to a degree of hydrolysis of 1 and 2%, respectively, to reveal the impacts of limited hydrolysis on their functional properties. Sodium dodecylsulfate-polyacrylamide gel electrophoresis analysis showed that the hydrolysates prepared were hydrolyzed proteins but with different peptide profiles. The evaluation results indicated that the hydrolysates had an increased solubility in pH range of 3-7 over the original SPC or SPI, especially at pH of 4.5. When the hydrolysates were used to prepare heat-induced gels, limited hydrolysis of SPC or SPI led to a decreased or an enhanced hardness of the gels prepared. The SPC hydrolysates had an increased fat absorption capacity about 17-29% while the SPI hydrolysates had a decreased fat absorption capacity about 17-23%. The present study showed that limited hydrolysis of SPC and SPI by neutrase or trypsin could be applied to improve some functional properties of them intended.
  Xin-Huai Zhao , Jing-Ke Wang and Tie-Jing Li
  Plastein reaction was used in the present work to modify casein hydrolysates in the presence of extrinsic amino acids to reveal its impacts on two bioactivities. Casein was hydrolyzed by alcalase to a degree of hydrolysis of 12.4%. The prepared hydrolysates exhibited in vitro inhibition on Angiotensin-I-converting Enzyme (ACE) and scavenging activity on DPPH radical. The prepared hydrolysates were then modified by alcalase-catalyzed plastein reaction in the presence of one of three extrinsic amino acids (leucine, valine or phenylalanine). At fixed 35% (w/w) substrate concentration and 6 h reaction time, other conditions were optimized as 0.6 mol/mol amino acid addition, 3 kU g-1 peptides alcalase addition and 30°C reaction temperature. The modified hydrolysates exhibited better ACE inhibition for its IC50 value decreased from 42.2 to 21.0-25.1 mg mL-1. The scavenging activity on DPPH (hydroxyl) radical or reducing power of the modified hydrolysates was also better than that of original casein hydrolysates. The results show that alcalase-catalyzed hydrolysis of casein coupled with plastein reaction is capable of preparing casein hydrolysates with better ACE inhibition and antioxidant activity.
  Na Zhang , Qing-Qi Guo and Xin-Huai Zhao
  In the present study, the proteolysis of a semi-hard cheese induced by a strain of Mucor spp. was briefly investigated. The cheese samples were smeared with the suspension of the Mucor in the surface and kept at 4°C and a relative humidity of 85-90% for ripening. Soluble or insoluble nitrogen fractions were separated from cheese samples ripened for different times and assayed by electrophoresis and RP-HPLC analysis to show the proteolysis occurred in the cheese samples. Electrophoresis analysis of the pH 4.6-insoluble nitrogen fractions showed that some protein fractions in the cheese samples were degraded into the peptides of lower molecular weights. RP-HPLC analysis results for the water-soluble nitrogen fractions also confirmed protein degradation and the formation of some new peptides. Chemical analysis revealed that the ratio of pH 4.6-soluble nitrogen to the total nitrogen of the cheese samples had a 3-fold increase after a ripening time of 90 days. Observation results under scanning electron microscopy clearly showed textural modification in the ripened cheeses. It is thus demonstrated that the Mucor spp. might be a potential starter for semi-hard cheese to degrade protein fractions and modify cheese texture.
 
 
 
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