| The fisheries industry has been fast in recent years base on application of modern science and technology. Anglerfish, as one of important fish-catches in world, usually taken its meat for processing entirely for anglerfish fillet. But anglerfish skin with a variety of collagen, a non-edible by-product produced in large majority during aquatic processing industry, often in a way of directly discarding as wast material or processing low value feedstuff, will not only result into waste of underutilized resource but also lead to environmental contamination. Collagen or collagen peptides, extracted effectively from the skins of anglerfish fishes if a better measurement is carried out based on current scientific enzymic or acid method. Hence, optimized utilization of these by-products is a promising road to protect the environment and increase the extra revenue of aquatic processing. In order to provide basic data for processing and application of anglerfish collagen peptides, in my experimental study, extracted subsequently collagen peptides from abandoned anglerfish skins with pepsin and2709alkaline protease, further investigated its characterization and the antioxidant and antibacterial activity.Pepsin-soluble collagen (PSC) with a yield of9.23±0.54%was effectively isolated from anglerfish (Lophius Litulon) skins, contained glycinecine (Gly)(344residues/1000residues) as the major amino acid and had imino acids of193residues/1000residues. PSC could be as a high-quality drug carrier based on the micrographs which had a uniform and regular network ultrastructure. Amino acid composition, Sodium dodecyl sulphate polyacylamide gel electrophoresis (SDS-PAGE), ultraviolet (UV) and fourier transform infrared (FTIR) suggested that PSC chiefly consisted of type I collagen with small polypeptide chains. It was found the denaturation temperature (Td) of PSC was18.78℃, manifested that its stability was less than those of mammalian and tropical fish species, but higher than those of cod skins. PSC had a better solubility at acid pH and the NaCI concentrations were low2%(w/v).Through orthogonal test, the optimum preparation process of anglerfish skin collagen peptides with molecular weight of less than50kDa isolated with2709alkaline protease was A3B3C2D1, namely, the addition of2709alkaline protease was1%, solid-liquid ratio was1:20, processing temperature and time of5℃and6h respectively. It was dissolved to a greater extent in acidic pH4but declined at pH7, namely pH had the minimum influence on the foaming capability (FC). pH had the maximum influence on foaming stability (FS) at acid pH, the foaming stabilities of anglerfish skin collagen peptides had the minimum influence at pH value of more than7. The emulsifying ability (EAI) and emulsifying stability (ESI) of anglerfish skin collagen peptides exhibited a increase as pH approached to alkaline. Comparing with acid pH, collagen peptides in alkaline pH showed much higher.The properties of ATSC with10mg/mL in vitro against hydroxyl radical and superoxide anion was better. Then after ultrafiltration, the molecular weight of less than2000D group had the highest activity. This collagen peptides could enhance activities of superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) and catalase (CAT), increase hydroxyproline (Hyp) content and decrease malonaldehyde (MAD) level in vivo, and the effect of100mg·kg-1·d-1dosage against D-galactose induced skin aging was better. Therefore, anglerfish skin collagen peptides could can be used as a positive substance against aging. Anglerfish skin collagen peptides could enhance the inhibition of antibiotics of Escherichiacoliand Staphylococcusaureus. Thus, anglerfish skin collagen peptides could improve efficacy of antibiotics, and almost no effect on Candida albicans. |
PDF Full Text Request