Abstract
Although several serine collagenolytic proteases from bacteria were reported, none has been used to prepare bioactive collagen peptides. MCP-01 is the most abundant extracellular protease of deep-sea Pseudoalteromonas sp. SM9913 and is a serine collagenolytic protease with high efficiency on fish collagen hydrolysis. Here, we set up a pilot scale process to ferment SM9913 for extracellular protease production. With SM9913 extracellular protease as a tool, a process to prepare collagen oligopeptide-rich hydrolysate from codfish skin was set up, which was further scaled up to pilot (100 L) and plant (2000 L) levels with yields >66%. The hydrolysates from laboratory-, pilot- and plant-scales had quite similar quality, containing ~95% peptides with molecular weights lower than 3000 Da and approximately 60% lower than 1000 Da, in which collagen oilgopeptides account for approximately 95%. Bioactivity analyses showed that the hydrolysate had moisture-retention ability, antioxidant activity, and promoting effect on cell viability of human dermal fibroblasts. Safety evaluation showed that the hydrolysate was nontoxic and nonirritating to skin. Therefore, SM9913 extracellular protease is a good enzyme to prepare bioactive oligopeptides from fish skin. The results also suggest that the collagen oligopeptides-rich hydrolysate may have potentials in biomedical, functional food, pharmaceutical and cosmetic industries.
Highlights
Bioactive oligopeptides, which contain only 2–10 amino acid residues with molecular weights of less than 1,500 Da, have received much attention due to their numerous potential physiological functions, including angiotensin-I-converting enzyme (ACE) inhibitory activity[1], antimicrobial activity[2], antioxidative[3] and immunomodulatory[4] properties etc
Fish processing industry produces a considerable number of by-products accounting for ~70–85% of the total weight of catch, 30% of which is in the form of bones and skins. Because it is rich in collagen, fish skin is a good material for preparing bioactive collagen oligopeptides to improve its additional value
These studies suggest that proteins in fish skin contain various bioactive sequences that can be released by enzyme hydrolysis
Summary
Bioactive oligopeptides, which contain only 2–10 amino acid residues with molecular weights of less than 1,500 Da, have received much attention due to their numerous potential physiological functions, including angiotensin-I-converting enzyme (ACE) inhibitory activity[1], antimicrobial activity[2], antioxidative[3] and immunomodulatory[4] properties etc. Fish processing industry produces a considerable number of by-products accounting for ~70–85% of the total weight of catch, 30% of which is in the form of bones and skins Because it is rich in collagen, fish skin is a good material for preparing bioactive collagen oligopeptides to improve its additional value. It has been showed that hydrolysates from fish skin usually contain multitudinous bioactive peptides, such as antimicrobial peptides[2], immunomodulatory peptides[4], antioxidative peptides[3], and ACE inhibitory peptides[1] These studies suggest that proteins in fish skin contain various bioactive sequences that can be released by enzyme hydrolysis. We aimed to prepare bioactive and collagen oligopeptides-rich hydrolysate from fish skin with the extracellular protease from SM9913. A process to prepare collagen oligopeptide-rich hydrolysate from fish skin with the extracellular protease from SM9913 was set up and was scaled up to pilot and plant scales. The bioactivities of the plant-scale hydrolysate, including moisture-absorption and retention abilities, antioxidant activity and its promotion effect on human cell proliferation, as well as its security evaluation, were investigated to assess its potentials in biotechnology and industry
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