Milk-clotting properties on bovine caseins of a novel cysteine peptidase from germinated Moringa oleifera seeds

ABSTRACT: A cysteine peptidase was previously identified from germinated Moringa oleifera seeds, but its milk-clotting properties on bovine caseins was still unclear. In this study, this novel cysteine peptidase (MoCP) showed preferential activity on κ-casein (κ-CN), with greater hydrolytic activity...

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Main Authors: Xuefeng Wang, Qiong Zhao, Li He, Yanan Shi, Jiangping Fan, Yue Chen, Aixiang Huang
Format: Article
Language:English
Published: Elsevier 2022-05-01
Series:Journal of Dairy Science
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S0022030222000960
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author Xuefeng Wang
Qiong Zhao
Li He
Yanan Shi
Jiangping Fan
Yue Chen
Aixiang Huang
author_facet Xuefeng Wang
Qiong Zhao
Li He
Yanan Shi
Jiangping Fan
Yue Chen
Aixiang Huang
author_sort Xuefeng Wang
collection DOAJ
description ABSTRACT: A cysteine peptidase was previously identified from germinated Moringa oleifera seeds, but its milk-clotting properties on bovine caseins was still unclear. In this study, this novel cysteine peptidase (MoCP) showed preferential activity on κ-casein (κ-CN), with greater hydrolytic activity compared with calf rennet, whereas weak hydrolysis of α-casein and β-casein made MoCP suitable for application in cheesemaking and may yield various functional peptides. All 3 evaluated caseins were hydrolyzed to form relatively stable peptide bands within 3 h of proteolysis with MoCP. Cleavage sites were determined by gel electrophoresis, liquid chromatography mass spectrometry/mass spectrometry, and peptide sequencing, which revealed that cleavage of κ-CN by MoCP occurred at residue Ile129-Pro130 and generated a 14,895.37-Da peptide. The flocculation reaction between MoCP and κ-CN determined by 3-dimensional microscopy with super-depth of field revealed that the initial 30 min of reaction were key for milk coagulation, which may affect curd yield. Overall, the findings presented herein suggest that the cysteine peptidase from germinated M. oleifera seeds can be considered a promising plant-derived rennet alternative for use in cheese manufacture.
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spelling doaj.art-ad79ad844b0a4e43aab5f84156064bc02022-12-22T01:21:31ZengElsevierJournal of Dairy Science0022-03022022-05-01105537703781Milk-clotting properties on bovine caseins of a novel cysteine peptidase from germinated Moringa oleifera seedsXuefeng Wang0Qiong Zhao1Li He2Yanan Shi3Jiangping Fan4Yue Chen5Aixiang Huang6College of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, Yunnan, ChinaCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, Yunnan, ChinaCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, Yunnan, ChinaCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, Yunnan, ChinaCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, Yunnan, ChinaBiotechnology and Germplasm Resources Institute, Yunnan Academy of Agricultural Sciences, Kunming 650205, Yunnan, China; Corresponding authorsCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, Yunnan, China; Corresponding authorsABSTRACT: A cysteine peptidase was previously identified from germinated Moringa oleifera seeds, but its milk-clotting properties on bovine caseins was still unclear. In this study, this novel cysteine peptidase (MoCP) showed preferential activity on κ-casein (κ-CN), with greater hydrolytic activity compared with calf rennet, whereas weak hydrolysis of α-casein and β-casein made MoCP suitable for application in cheesemaking and may yield various functional peptides. All 3 evaluated caseins were hydrolyzed to form relatively stable peptide bands within 3 h of proteolysis with MoCP. Cleavage sites were determined by gel electrophoresis, liquid chromatography mass spectrometry/mass spectrometry, and peptide sequencing, which revealed that cleavage of κ-CN by MoCP occurred at residue Ile129-Pro130 and generated a 14,895.37-Da peptide. The flocculation reaction between MoCP and κ-CN determined by 3-dimensional microscopy with super-depth of field revealed that the initial 30 min of reaction were key for milk coagulation, which may affect curd yield. Overall, the findings presented herein suggest that the cysteine peptidase from germinated M. oleifera seeds can be considered a promising plant-derived rennet alternative for use in cheese manufacture.http://www.sciencedirect.com/science/article/pii/S0022030222000960germinated Moringa oleifera seedcysteine peptidaseκ-caseincleavage siteflocculation reaction
spellingShingle Xuefeng Wang
Qiong Zhao
Li He
Yanan Shi
Jiangping Fan
Yue Chen
Aixiang Huang
Milk-clotting properties on bovine caseins of a novel cysteine peptidase from germinated Moringa oleifera seeds
Journal of Dairy Science
germinated Moringa oleifera seed
cysteine peptidase
κ-casein
cleavage site
flocculation reaction
title Milk-clotting properties on bovine caseins of a novel cysteine peptidase from germinated Moringa oleifera seeds
title_full Milk-clotting properties on bovine caseins of a novel cysteine peptidase from germinated Moringa oleifera seeds
title_fullStr Milk-clotting properties on bovine caseins of a novel cysteine peptidase from germinated Moringa oleifera seeds
title_full_unstemmed Milk-clotting properties on bovine caseins of a novel cysteine peptidase from germinated Moringa oleifera seeds
title_short Milk-clotting properties on bovine caseins of a novel cysteine peptidase from germinated Moringa oleifera seeds
title_sort milk clotting properties on bovine caseins of a novel cysteine peptidase from germinated moringa oleifera seeds
topic germinated Moringa oleifera seed
cysteine peptidase
κ-casein
cleavage site
flocculation reaction
url http://www.sciencedirect.com/science/article/pii/S0022030222000960
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