The preservative potential of Octopus scraps peptides−Zinc chelate against Staphylococcus aureus: Its fabrication, antibacterial activity and action mode
Introduction
Marine octopus is a rich marine resource in Asia, and is listed as popular seafood for its high nutritional value (Viciano et al., 2011). With the increasing demand for octopus at home and abroad, more octopus meat, offal, eyes, by-products and other wastes have been produced during rough processing, which caused serious environmental problems (Nurdiani et al., 2015). However, octopus peptides, which can be obtained by the enzymatic hydrolysis of octopus waste proteins, have much better bioactivity and higher nutritional and medicinal value compared with that of their parent proteins. Bioactive peptides play physiological regulatory roles in human body and have the functions of chelating, immunomodulating, antitumor, antioxidation, antivirus, antibacterial, cholesterol-lowering and antihypertensive activities (Lee & Sun, 2017; Ma et al., 2017; L.; Wang et al., 2016; Wang et al., 2014a,b).
Peptide-zinc complexes were zinc ion-modified biologically active peptide complexes with a variety of bio-functional activities. According to previous reports, most of the peptide chelated zinc are based on the body's zinc supplement preparations. The incorporation of zinc ions into the body as an organic chelate, avoids the formation of insoluble complexes with the intake of phytic acid and dietary fiber in the gastrointestinal tract, thereby increasing the bioavailability of zinc (Wang, Li, & Ao, 2012). Liao et al. (2016) found that the combination of walnut peptide and zinc ion generated walnut peptide-zinc complexes with strong anti-proliferative ability as well as reduced toxicity. Zinc complex of l-carnosine (L-CAZ) can specifically adhere to the gastric ulcer lesions and release zinc to cure ulcers, due to the inhibitory effect of L-CAZ on Helicobacter pylori (Matsukura & Tanaka, 2000).
Despite the extensive research on peptide-zinc complexes, few studies focus on their antimicrobial activity and action mechanism. In addition, limited information is available about the peptide-zinc complexes structure. Therefore, our study aimed to prepare octopus scraps protein hydrolysate (OSPH)Zn chelate, characterize its antibacterial property and investigate the action mechanism to provide fundamental understanding on the mode of antibacterial action.
Section snippets
Materials
Octopus scraps were kindly provided by Boguangtianxing Company of Fujian, China. Flavourzyme (EC. 3.4.11.1, 6.25 × 104 U/g) was purchased from Novozymes, Denmark. All other chemicals and reagents were of analytical grade and commercially available.
Microbial strains and culture
S. aureus ATCC25923 used throughout the study was obtained from the Institute of Food and Marine Bioresources, Fuzhou University (Fuzhou, PR China). The bacteria were reactivated sub-cultured 2–3 times in lysogeny broth (LB) medium at 37 °C for
Preparation of OSPH
As we expected, the zinc-chelating ability and DH of OSPH increased dramatically with the persistent period of Flavourzyme hydrolysis (Fig. 1A), which obtained a typical curve. In the first 6 h, the zinc-chelating ability approached 29.56% and the DH gradually increased to 16.54%. Subsequently, the zinc-chelating ability tended to be mild, and accompanied by a slightly lower of the DH. Since the substrate provided a limited cleavage site during the hydrolysis process, two indicators did not
Conclusions
Based on the present research, the combination of OSPH and Zn ions was mainly achieved through ZnN and ZnO bonds. Results showed that OSPH-Zn could remarkably inhibit the proliferation of S. aureus. The mechanism of action may be described as changing the permeability of cell membrane, which was associated with the integrality of membrane-disrupting effects, leading to the leakage of electrolytes as well as losses of proteins, nucleic acid and AKP. Moreover, we found that oxidative stress from
Acknowledgements
This work was supported by Natural Science Foundation of China (No.31771922).
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