Effect of pepsin hydrolysis on antioxidant activity of jellyfish protein hydrolysate

Pratchaya Muangrod,Benjamaporn Wonganu,Savitri Vatanyoopaisarn,Wiriya Charoenchokpanich,Benjawan Thumthanaruk,Sittiruk Roytrakul,Vilai Rungsardthong

doi:10.1051/e3sconf/202130202010

Abstract

Edible jellyfish have been consumed as food for more than a century with offering high protein and crunchy texture. The pepsin hydrolysis of jellyfish protein yields jellyfish protein hydrolysate (ep-JPH), reported for potential bioactivities such as antioxidant activity or antihypertensive activities. Due to the substantial number of by-products generated from jellyfish processing, the by-products were then selected as a raw material of JPH production. This research aimed to evaluate the effect of the hydrolysis time of pepsin on the antioxidant activity of ep-JPH. The dried desalted jellyfish by-products powder was enzymatically hydrolysed by 5% (w/w) pepsin, and the hydrolysis time was varied from 6, 12, 18, and 24 h at 37oC. Results showed that increased hydrolysis time increased the degree of hydrolysis (DH) and inhibition of DPPH radical. The 24 h ep-JPH possessed the highest DH and the highest inhibitory effect of DPPH radical. The results demonstrated that, in this experiment, all ep-JPHs were DPPH radical scavengers, exhibiting different inhibition activities depending on DH values.

Highlights

Protein hydrolysates are products of protein degradation that yield various sizes of peptides and free amino acids [1, 2]
Results of proximate composition of jellyfish protein powder (JPP) were similar to the previous study that JPP had 7.69%, 76.41%, 1.35%, and 15.76%, respectively [27], but slightly different from the work of Emrerk et al (2021) [37], who reported that JPP had 5.27%, 68.8%, 3.18%, and 9.11%, respectively
According to the high protein content, the JPP was selected for producing jellyfish protein hydrolysate

Summary

Introduction

Protein hydrolysates are products of protein degradation that yield various sizes of peptides and free amino acids [1, 2]. There are several methods of protein hydrolysate production, including acids or alkali hydrolysis and enzymatic hydrolysis [1,2,3]. Different methods of protein hydrolysate production result in different bioactivity of protein hydrolysate due to its amino acid composition and sequence [1, 4, 5]. Enzymatic hydrolysis is one of the practical protein hydrolysate productions via protease enzymes that cleave specific peptide bonds and provide short peptides with small molecular weights [1]. Most low molecular weight enzymatic hydrolysate peptides containing approximately 2-20 amino acid residues are considered bioactive peptides [5, 6]. Different types of protease enzymes provided different bioactive peptides

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Results

Conclusion