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Antibacterial Activity of Protease Hydrolysates Isolated from Silybum marianum


Affiliations
1 College of Food Science, Shenyang Agricultural University, Shenyang 110866, China
2 College of Agronomy, Shenyang Agricultural University, Shenyang 110866, China
 

In this study, the antibacterial activity of protease hydrolysates from Silybum marianum protein isolates (SMPIs) was investigated. Neutral protease, papain, pepsin and alkaline protease were used as experimental enzymes, while Escherichia coli, Staphylococcus aureus, Sarcina lutea and Bacillus subtilis were the bacterial indicators. The results showed that neutral protease, papain and pepsin hydrolysates exerted inhibitory effects on the four types of bacteria tested. However, alkaline protease hydrolysates of SMPI showed stimulatory effects on replication of the four bacteria tested. The antibacterial mechanism of SMPI hydrolysates was studied using scanning electron microscopy, and the results showed effective inhibition of E. coli (Gram-negative, G-) and S. aureus (Gram-positive, G+). It is speculated that the underlying mechanism of SMPI hydrolysates may involve injury to E. coli and S. aureus cell membranes. Currently, no similar studies have been conducted on the antibacterial activity of SMPI.

Keywords

Antibacterial Activity, Antibacterial Mechanism, Proteolysis, Silybum marianum.
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  • Antibacterial Activity of Protease Hydrolysates Isolated from Silybum marianum

Abstract Views: 318  |  PDF Views: 114

Authors

Jing Yue
College of Food Science, Shenyang Agricultural University, Shenyang 110866, China
Zhicheng Zhu
College of Agronomy, Shenyang Agricultural University, Shenyang 110866, China
Xinhua Li
College of Food Science, Shenyang Agricultural University, Shenyang 110866, China

Abstract


In this study, the antibacterial activity of protease hydrolysates from Silybum marianum protein isolates (SMPIs) was investigated. Neutral protease, papain, pepsin and alkaline protease were used as experimental enzymes, while Escherichia coli, Staphylococcus aureus, Sarcina lutea and Bacillus subtilis were the bacterial indicators. The results showed that neutral protease, papain and pepsin hydrolysates exerted inhibitory effects on the four types of bacteria tested. However, alkaline protease hydrolysates of SMPI showed stimulatory effects on replication of the four bacteria tested. The antibacterial mechanism of SMPI hydrolysates was studied using scanning electron microscopy, and the results showed effective inhibition of E. coli (Gram-negative, G-) and S. aureus (Gram-positive, G+). It is speculated that the underlying mechanism of SMPI hydrolysates may involve injury to E. coli and S. aureus cell membranes. Currently, no similar studies have been conducted on the antibacterial activity of SMPI.

Keywords


Antibacterial Activity, Antibacterial Mechanism, Proteolysis, Silybum marianum.

References





DOI: https://doi.org/10.18520/cs%2Fv113%2Fi03%2F496-500