Elsevier

Food Control

Volume 98, April 2019, Pages 24-33
Food Control

The preservative potential of Octopus scraps peptides−Zinc chelate against Staphylococcus aureus: Its fabrication, antibacterial activity and action mode

https://doi.org/10.1016/j.foodcont.2018.11.015Get rights and content

Highlights

  • OSPH-Zn chelate with high Zn-chelating rate was fabricated through Znsingle bondN and Znsingle bondO covalent bonds.

  • OSPH-Zn exhibited remarkably antimicrobial ability against foodborne spoilage bacteria S. aureus.

  • The antibacterial mechanism of OSPH-Zn was studied in mechanical damage and oxidative damage of cell.

  • The results suggest the potential in making marine peptide-zinc chelate as a new type of antimicrobial food ingredients.

Abstract

A new type of zinc-chelating peptide was fabricated from Octopus scraps protein hydrolysate and its antibacterial activity against Staphylococcus aureus was characterized. Results of Fluorescence spectra and Fourier Transform Infrared Spectrometer (FT-IR) demonstrated that the amino nitrogen atoms and the oxygen atoms belonging to the carboxylate groups were the primary chelating sites for zinc ions. The zinc-peptide chelate exerted remarkably antimicrobial ability towards S. aureus, whose minimum inhibitory concentration (MIC) was 1.56 mg/mL. To investigate the antibacterial mechanism, changes of bacterial morphology, cell constituents, membrane potential, intracellular reactive oxygen species (ROS) level and intracellular enzyme activity were measured. Results revealed that Zn-peptide exerted its bactericidal activity by damaging bacterial cell membranes and cell walls, increasing the cell permeability which resulted in structural lesions and release of cell components. Besides, Zn-peptide induced S. aureus cell death via ROS triggered pathway. These findings further promote the development of Zn-peptide complexes, suggesting that Zn-peptide chelate has potential as natural bacteriostatic agent in food processing industry.

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)single bondZn 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 Znsingle bondN and Znsingle bondO 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).

References (37)

  • C. Wang et al.

    Zn(II) chelating with peptides found in sesame protein hydrolysates: Identification of the binding sites of complexes

    Food Chemistry

    (2014)
  • X. Wang et al.

    Zinc-binding capacity of yak casein hydrolysate and the zinc-releasing characteristics of casein hydrolysate-zinc complexes

    Journal of Dairy Science

    (2011)
  • J. Wei et al.

    Serum immune response of pearl oyster Pinctada fucata to xenografts and allografts

    Fish & Shellfish Immunology

    (2017)
  • X. Yan et al.

    Blasting extrusion processing: The increase of soluble dietary fiber content and extraction of soluble-fiber polysaccharides from wheat bran

    Food Chemistry

    (2015)
  • Y. Zhang et al.

    Antibacterial activity and mechanism of cinnamon essential oil against Escherichia coli and Staphylococcus aureus

    Food Control

    (2016)
  • J. Zhou et al.

    Preparation and characterization of β-lactoglobulin hydrolysate-iron complexes

    Journal of Dairy Science

    (2012)
  • H.A.G. And et al.

    A Fluorescent zinc probe based on metal-induced peptide folding

    Journal of the American Chemical Society

    (1996)
  • S.J. Dixon et al.

    The role of iron and reactive oxygen species in cell death

    Nature Chemical Biology

    (2014)
  • Cited by (54)

    • Antimicrobial and drug delivery aspect of environment-friendly polymer nanocomposites

      2023, Nanocomposites-Advanced Materials for Energy and Environmental Aspects
    • Antimicrobial mechanism of linalool against Brochothrix thermosphacta and its application on chilled beef

      2022, Food Research International
      Citation Excerpt :

      Compared with the control group, the MP was found to exhibit a rapid depolarization trend in B. thermosphacta under linalool stress and linalool in MIC and 2MIC groups altered MP to a comparable extent, which was thought to be the membrane damage caused by less negative intracellular charge (Liu et al., 2020). As a component of proton dynamics, MP is closely related to the production of ATP (Fang et al., 2019). Previous studies concluded that extracellular Na+ inward diffusion was an important cause of cell membrane depolarization (Plasek et al., 2013).

    View all citing articles on Scopus
    View full text