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Articles by Guang-Rong Huang
Total Records ( 4 ) for Guang-Rong Huang
  Jing Zhou , Wen-Wei Chen , Zheng-Bao Jia , Guang-Rong Huang , Yao Hong , Jun-Jie Tao and Xiao-Bo Luo
  Lipase was one of the most important industrial enzymes and has diverse applications in food industry, detergent industry, fats and oil hydrolysis, peptide synthesis and pharmaceutical industries. The aim of this study was focused on isolation of a lipase producing strain from waste cooking oily soil and characterization of the lipase. The strain, Aspergillus oryzae CJLU-31 was isolated from the waste cooking oily soil and identified by ITS rDNA analysis. The lipase from Aspergillus oryzae CJLU-31 was purified by ammonium sulfate precipitation and two-step chromatography. The results showed that the purified lipase had a specific activity of 11552.2 U mg-1, 23.9-fold purification factor and molecular mass of 27 kDa by Sodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis (SDS-PAGE). The purified lipase showed higher activity when the waste cooking oil was used as the substrate. It also showed maximum activity and stability at pH 4.0 and 40°C. The lipase retained high activity over ranges of pH (2-5) and temperature (30-50°C). It was enhanced by low concentration metal ions, such as K+, Li+, Mg2+, Zn2+, Mn2+ and Ca2+, while inhibited by Fe2+, Fe3+ and Cu2+. It showed high stability in the presence of lower polarity organic solvents and activated in 0.1% polyvinyl alcohol-124. The Km and Vmax of the lipase acting on olive oil were 0.11 and 0.41 mM min-1, respectively. Heating and cooling refold-treatment activated the lipase. These features provided the lipase from Aspergillus oryzae CJLU-31 as a potential application for lipase-catalyzed synthesis of fatty acid methyl esters (biodiesel) using waste cooking oil.
  Wen-Ting Zhang , Jia-Yue Sun and Guang-Rong Huang
  The aim of this study was to investigate the stability of mackerel (Trachurus japonicas) processing byproducts protein hydrolysate with iron-binding capacity in vitro simulated gastrointestinal systems. The changes in molecular weight distribution and iron-binding capacity were used for evaluating the stability of the hydrolysate in simulated gastrointestinal digestion. The molecular weight of mackerel hydrolysate with iron-binding capacity was mostly less than 1300 Da and composted mainly by tripeptides to undepeptides. The hydrolysate was stable in gastric or intestinal digestion separately for 5 h, or two-stage gastrointestinal digestion. The iron-binding capacity did not change significantly during gastrointestinal digestion. The mackerel processing byproducts hydrolysate had potential in iron fortification functional ingredients of food industry.
  You-Yu Kong , Shi-Shi Chen , Jun-Qi Wei , Yan-Ping Chen , Wu-Tao Lan , Qing-Wei Yang and Guang-Rong Huang
  Marine fish processing byproducts were considered as potential good protein resource for producing bioactive peptides by enzymatic hydrolysis. In this study, preparation and partial characteristics of the antioxidative peptides from Spanish mackerel (Scomberomorus) processing byproducts fish frame by commercial proteases were investigated. The results showed that the mackerel frame hydrolysate with alcalase had the highest degree of hydrolysis and DPPH (1,1-diphenyl-2-pycryl-hydrazyl) radical scavenging activity, the values of 31.3 and 18.5%, respectively. The alcalase hydrolysate was ultrafiltrated into four fractions and the fraction with lower molecular weight had higher DPPH radical scavenging capacity. The fraction F4 with molecular weight less than 3 kDa had the highest DPPH radical scavenging capacity of 27.7%. The molecular weight distribution of fraction F4 showed that they were mainly consisted of less than 1 kDa small peptides and free amino acids. The small peptides in fraction F4 were mainly dipeptide to nonapeptide, especially tripeptide to hexapeptide.
  Qing-Wei Yang , Cheng Zhen , Song Chen , Ying Zhang , Wei Shen , Shi-Shi Chen and Guang-Rong Huang
  Marine fish processing byproducts were considered as potential good protein resource for producing bioactive peptides by enzymatic hydrolysis. In this study, hydrolysates with high ferrous binding ability were prepared by enzymatic hydrolysis from mackerel (Trachurus japonicus) processing byproducts. In order to get hydrolysates of high ferrous binding ability and degree of hydrolysis, the enzymatic hydrolysis conditions were optimized, including proteases type, hydrolysis time, temperature, pH and enzyme to substrate ratio. The results showed that the hydrolysate by alcalase had the highest ferrous binding ability and degree of hydrolysis, reaching to 9.8 and 49.0%, respectively. The best hydrolysis conditions of alcalase were optimized using response surface methodology to be: pH 9.0, temperature of 50°C, enzyme substrate ratio of 160 mg/100 mL, hydrolysis time of 100 min. The ferrous binding ability and degree of hydrolysis were reached to 48.0 and 45.4%, respectively, at these optimized hydrolysis conditions.
 
 
 
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