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Articles by Qing-Wei Yang
Total Records ( 2 ) for Qing-Wei Yang
  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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