Preparation and Evaluation of Peptides with Potential Antioxidant Activity by Microwave Assisted Enzymatic Hydrolysis of Collagen from Sea Cucumber Acaudina Molpadioides Obtained from Zhejiang Province in China.

Huo-Xi Jin,Qian-Wei Zhang,Yan Li,Hui Xie,Hong-Ping Xu

doi:10.3390/md17030169

Abstract

The present study was focused on the preparation and characterization of the antioxidant peptides by microwave-assisted enzymatic hydrolysis of collagen from sea cucumber Acaudina molpadioides (ASC-Am) obtained from Zhejiang Province in China. The results exhibited the effects of microwave irradiation on hydrolysis of ASC-Am with different protease. Neutrase was selected from the four common proteases (papain, pepsin, trypsin, and neutrase) based on the highest content and DPPH scavenging activity of hydrolysate Fa (Molecular weight < 1 kDa). The content and 2,2-diphenyl-1-picrylhydrazyl (DPPH) scavenging activity of Fa obtained by hydrolysis of neutrase increased by 100% and 109% respectively at a microwave power of 300 W compared with no microwave irradiation. Five subfractions were obtained after performing the gel filtration chromatography, and the Fa.2 exhibited the highest DPPH scavenging activity. The amino acid analysis showed that the contents of Glutamic acid, Alanine, Tyrosine, and Phenylalanine in fraction Fa.2 increased significantly, but an obvious decrease in the content of Glycine was observed compared to Fa. Four peptides (Fa.2-A, Fa.2-B, Fa.2-C, and Fa.2-D) were purified from Fa.2 by high performance liquid chromatography, and Fa.2-C showed the highest DPPH scavenging activity. The sequence of Fa.2-C was identified as Phenylalanine-Leucine- Alanine-Proline with a half elimination ratio (EC50) of 0.385 mg/mL. The antioxidant activity of Fa.2-C was probably attributed to the small molecular sizes and the presence of hydrophobic amino acid residues in its sequence. This report provided a promising method for the preparation of antioxidant peptides from collagen for food and medicinal purposes.

Highlights

Collagen, an important structural protein, constitutes about 30% of the total protein in the multicellular organisms [1,2]
The degree of hydrolysis of collagen is incomplete, and the molecular distribution of hydrolysate is uneven in the traditional methods
Many studies have shown that the antioxidant activity of protein hydrolysate depends on its molecular weight (Mw) and amino acid composition [15,18]

Summary

Introduction

An important structural protein, constitutes about 30% of the total protein in the multicellular organisms [1,2]. Collagen is the main component of bone, fascia, tendons, cartilage, skin, and other connective tissues [3,4]. It is widely used in the fields of food and medicine due to its unique structural and biological characteristics, such as high tensile strength, low antigenicity, good biocompatibility and biological activity [5,6,7]. In the last decade, collagen peptides have received more and more attention, and are considered as important components based on.

Methods

Results

Conclusion