Production of Bioactive Peptides from Soybean Meal by Solid State Fermentation with Lactic Acid Bacteria and Protease

Naifu Wang,Yonghui Shi,Yuan Zeng,Guowei Le

doi:10.19026/ajfst.6.163

Naifu Wang, Yonghui Shi + Show 2 more

Open Access

https://doi.org/10.19026/ajfst.6.163

Copy DOI

Abstract

In this study, soybean meal was first solid state fermented with different strains of Lactic Acid Bacteria (LAB). Among the strains used, Lactobacillus plantarum Lp6 was selected for further studies because of its highest Degree of Hydrolysis (DH) of protein (2.49Â±0.08%) in soybean meal after 72 h fermentation. Soybean meal fermented with L. plantarum Lp6 can also improve its DPPH radical scavenging and Angiotensin Converting Enzyme (ACE) inhibitory activities. The addition of protease into soybean meal during the fermentation resulted in lowered IC50 of DPPH radical scavenging and ACE inhibitory activities, indicating more bioactive peptides were produced during fermentation. Molecular weight distribution analysis revealed the Extracts from Fermented Soybean Meal (EFSM) was mainly composed of oligopeptides. These results indicated that soybean meal fermented with L. plantarum Lp6 and protease could be an easy and cheap method to produce functional food.

Highlights

Peptides derived from food proteins with bioactive activities, such as anti-hypertension, immunomodulation, antioxidation, antimicrobial action and antithrombosis are recognized as functional food ingredients in preventing lifestyle-related diseases (Inoue et al, 2011)
Many studies have reported that the bioactive activities of milk fermented with Lactic Acid Bacteria (LAB), such as antioxidant or Angiotensin Converting Enzyme (ACE) inhibitory activities were correlated to the Degree of Hydrolysis (DH) of protein (Virtanen et al, 2007; Ramchandran and Shah, 2008; Pan and Guo, 2010; Pihlanto et al, 2010; Gonzalez-Gonzalez et al, 2011)
The growth performance of different strains of LAB in soybean meal after 72 h of solid state fermentation was assessed by measuring pH and DH (Fig. 1)

Summary

Introduction

Peptides derived from food proteins with bioactive activities, such as anti-hypertension, immunomodulation, antioxidation, antimicrobial action and antithrombosis are recognized as functional food ingredients in preventing lifestyle-related diseases (Inoue et al, 2011). These peptides can be released from protein sequences by digestive proteases, microbial or plant enzymes or by fermentation. Among the starters used for fermentation, Lactic Acid Bacteria (LAB) are thought to be safe bacteria that have been widely used in food or drink products for many years. Proteases of LAB can hydrolyze various proteins, producing a large number of different oligopeptides (Wang et al, 2008). Compare to the proteases from fungi or plants, the proteolytic activity of LAB is low and proteins could not reach a high DH after fermentation when only LAB was used as starters

Objectives

Methods

Results

Conclusion