当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Protein function analysis of germinated Moringa oleifera seeds, and purification and characterization of their milk-clotting peptidase.

Protein function analysis of germinated Moringa oleifera seeds, and purification and characterization of their milk-clotting peptidase.

Abstract：

:The present study aimed to investigate the biological functions of germinated M. oleifera seed proteins and to identify the identity of milk-clotting proteases. A total of 963 proteins were identified, and those with molecular weights between 10 and 30 kDa were most abundant. The identified proteins were mainly involved in energy-associated catalytic activity and metabolic processes, and carbohydrate and protein metabolisms. The numbers of proteins associated with the hydrolytic and catalytic activities were higher than the matured dry M. oleifera seeds reported previously. Of the identified proteins, proteases were mainly involved in the milk-clotting activity. Especially, a cysteine peptidase with a molecular mass of 17.727 kDa exhibiting hydrolase and peptidase activities was purified and identified. The identified cysteine peptidase was hydrophilic, and its secondary structure consisted of 27.60% alpha helix, 9.20% beta fold, and 63.20% irregular curl; its tertiary structure was also constructed using M. oleifera seed 2S protein as the protein template. The optimal pH and temperature of the purified protease were pH 4.0 and 60 °C, respectively. The protease had high acidic stability and good thermostability, thus could potentially be applied in the dairy industry.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Wang X,He L,Zhao Q,Chen H,Shi Y,Fan J,Chen Y,Huang A

doi

10.1016/j.ijbiomac.2021.01.026

subject

Has Abstract

pub_date

2021-01-09 00:00:00

pages

539-549

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(21)00045-3

journal_volume

171

pub_type

杂志文章

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