4.7 Article

Potential protein hydrolysates from the white and purple flower varieties of Orthosiphon aristatus leaves

期刊

FOOD CHEMISTRY
卷 432, 期 -, 页码 -

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2023.137261

关键词

Orthosiphon aristatus; Bioactive peptides; Trypsin; Pepsin; Antibacterial property

向作者/读者索取更多资源

This study aimed to extract bioactive peptides from the white and purple flower varieties of Orthosiphon aristatus leaves. The results showed that trypsin hydrolysates had higher antioxidant and antibacterial activities. The white flower hydrolysates exhibited higher radical scavenging activity, while the purple flower hydrolysates showed higher ferric reducing power and bacterial growth inhibition.
This study was aimed to extract bioactive peptides from the white and purple flower varieties of Orthosiphon aristatus leaves. The herb is well known for its pharmacological importance, possibly attributed to its plant proteins. Phenol based extraction was used to extract plant proteins, and then hydrolysed by proteolytic enzymes such as trypsin (serine protease) and pepsin (aspartic protease). MS/MS analysis revealed that 145 and 125 proteins were detected from the white and purple flower varieties, respectively. Trypsin hydrolysates were showed to have a higher degree of hydrolysis (24-33%), resulting in higher antioxidant and antibacterial activities. The white flower of trypsin hydrolysates showed a higher radical scavenging activity which could be attributed to its higher content of stress proteins (19%). However, trypsin hydrolysates from the purple flower showed higher ferric reducing power and bacterial growth inhibition. The performance of hydrolysates was better than ampicillin in inhibiting Acinetobacter baumanni and Staphylococcus aureus.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据