Abstract

The fight against food waste benefits from novel agents inhibiting spoilage. The present study investigated the preservative potential of the antimicrobial peptides Leg1 (RIKTVTSFDLPALRFLKL) and Leg2 (RIKTVTSFDLPALRWLKL) recently identified in chickpea legumin hydrolysates. Checkerboard assays revealed strong additive antimicrobial effects of Leg1/Leg2 with sodium benzoate against Escherichia coli and Bacillus subtilis with fractional inhibitory concentrations of 0.625 and 0.75. Additionally, Leg1/Leg2 displayed antifungal activity with minimum inhibitory concentrations of 500/250 µM against Saccharomyces cerevisiae and 250/125 µM against Zygosaccharomyces bailii. In contrast, no cytotoxic effects were observed against human Caco-2 cells at concentrations below 2000 µM (Leg1) and 1000 µM (Leg2). Particularly Leg2 showed antioxidative activity by radical scavenging and reducing mechanisms (maximally 91.5/86.3% compared to 91.2/94.7% for the control ascorbic acid). The present results demonstrate that Leg1/Leg2 have the potential to be applied as preservatives protecting food and other products against bacterial, fungal and oxidative spoilage.

Highlights

  • Peptides occur naturally in many foods or can be formed after the enzymatic or microbiological hydrolysis of food proteins

  • The present study investigated the preservative potential of the antimicrobial peptides Leg1 (RIKTVTSFDLPALRFLKL) and Leg2 (RIKTVTSFDLPALRWLKL) recently identified in chickpea legumin hydrolysates

  • Leg1/Leg2 displayed antifungal activity with minimum inhibitory concentrations of 500/250 μM against Saccharomyces cerevisiae and 250/125 μM against Zygosaccharomyces bailii

Read more

Summary

Introduction

Peptides occur naturally in many foods or can be formed after the enzymatic or microbiological hydrolysis of food proteins. Antimicrobial peptides (AMPs) from food sources could be a promising alternative to conventional preservatives. It has been postulated that AMPs interact with the bacterial cell membrane and lead to its disintegration, for example by the formation of pores [2]. AMPs are active against a wide range of bacteria and are less likely to evoke antimicrobial resistance [2,3]. The risk of toxic side effects is low so that food-derived AMPs are generally considered as safe. Enzymatically generated AMPs from food proteins are equivalent to products of gastrointestinal digestion and most probably safe. Only one peptide is utilized as food preservative, namely nisin, which is of bacterial origin [4]

Methods
Results
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call