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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Format: | Article |
Language: | English |
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Elsevier
2022-05-01
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Series: | Journal of Dairy Science |
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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. |
first_indexed | 2024-12-11T04:05:42Z |
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id | doaj.art-ad79ad844b0a4e43aab5f84156064bc0 |
institution | Directory Open Access Journal |
issn | 0022-0302 |
language | English |
last_indexed | 2024-12-11T04:05:42Z |
publishDate | 2022-05-01 |
publisher | Elsevier |
record_format | Article |
series | Journal of Dairy Science |
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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