Optimization Preparation Of Collagen Peptides From Scale Of Tilapiaand And Study On Their Biological Activity
Keywords
Tilapia Scale Collagen Peptides Antioxidant Activity Cryoprotective Activity Amino Acid
Abstract
Tilapia scales were used as raw materials, and alkaline protease and trypsin were used for compound hydrolysis. On the basis of single factor experiments, the response surface method was used to optimize the enzymatic hydrolysis process to prepare fish scale collagen peptides. The antioxidant activity and bacterial low temperature of collagen peptides were measured. Protective activity, amino acid composition and relative molecular mass distribution. The results show that the optimal enzymatic hydrolysis conditions are: substrate mass concentration 30.6 mg¡¤mL-1, and the amount of trypsin and basic protein added are 1.44 and 0.70 mg¡¤mL respectively. -1. Enzymatic hydrolysis temperature is 50¡æ, pH value is 8.5, and enzymatic hydrolysis time is 6.35h. The half-mass scavenging mass concentrations (IC50) of enzymatically hydrolyzed collagen peptides for DPPH free radicals and hydroxyl free radicals are 2.89 and 3.54 mg¡¤mL-1 respectively. After a bacterial low-temperature protection test, when the mass concentration of collagen peptide is 1 mg¡¤mL-1, the survival rate of Streptococcus thermophilus reaches 75.6%. The relative molecular mass distribution of fish scale collagen peptide shows that the relative molecular mass of 78% of the polypeptide fragments is distributed in 180 Between ~2000u. Amino acid composition analysis shows that fish scale peptides are rich in glycine, alanine, proline, hydroxyproline and aspartic acid. These specific amino acids are related to the antioxidant activity and bacterial low-temperature protection activity of collagen peptides. Related. The scale of Tilapia was used in the experiment as the raw material, which was hydrolyzed by alkaline and trypsin protease. The response surface method according to single factor analysis was optimized to prepare fish scale collagen peptides. Antioxidant effects, hypothermia protection activity on bacteria, amino acid composition and molecular weight distribution of collagen peptides were analyzed. The results indicated that the optimum conditions for enzymatic hydrolysis were determined as follows: substrate concentration of 30.6mg¡¤mL-1, enzyme dosage of trypsin and alkaline protease were 1.44 and 0.70mg¡¤mL-1, hydrolysis temperature of 50¡æ, pH 8.5 and hydrolysis time of 6.35h, respectively. The IC50 of enzymatic collagen peptides on scavenging DPPH¡¤and¡¤OH were 2.89 and 3.54mg¡¤mL-1, respectively. hypothermia protection assay showed that the survival rate of Streptococcus thermophiles was 75.6% when the concentration of peptides was 1mg¡¤mL-1. Molecular weight distribution showed that 78% of collagen peptides mostly distributed between 180 to 2000u, and it was rich in Gly, Ala, Pro, Hyp and Asp, which were special amino acids relative to the antioxidant activity and cryoprotective activity
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Original research was done by Li Ling, Xu Liangzong, Wang Shaoyun
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