Purification and characterization of a novel milk-clotting enzyme produced by Bacillus amyloliquefaciens GSBa-1
A novel milk-clotting enzyme (MCE) produced by Bacillus amyloliquefaciens GSBa-1 was purified and identified to belong to the peptidase M4 family, and the mature peptide with milk-clotting activity (MCA) was a neutral metalloproteinase with molecular mass of about 38 kDa. The optimal pH and temperat...
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| Veröffentlicht in: | European food research & technology 2019-11, Vol.245 (11), p.2447-2457 |
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| creator | Zhao, Xiao Cai, Miao Yang, Zhi-Jie Luo, Tian-Qi Sarwar, Abid Megrous, Sarah Aziz, Tariq Yang, Zhen-Nai |
| description | A novel milk-clotting enzyme (MCE) produced by
Bacillus amyloliquefaciens
GSBa-1 was purified and identified to belong to the peptidase M4 family, and the mature peptide with milk-clotting activity (MCA) was a neutral metalloproteinase with molecular mass of about 38 kDa. The optimal pH and temperature were determined to be at 5.5 and 57 °C for MCA, and at 7.0 and 57 °C for the proteolytic activity, respectively. The MCE exhibited slight autolysis that could be inhibited by Ca
2+
and Na
+
. Hydrolysis of caseins revealed that κ-casein exhibited higher sensitivity to the MCE action than α- and β-casein. By in-gel tryptic digestion and LC–MS/MS analysis of the major peptide (about 13 kDa) generated from hydrolysis of κ-casein by the MCE, the cleavage site was identified to be at Lys 111–Lys 112, which was different from those of other MCEs reported earlier. The MCE from
B. amyloliquefaciens
GSBa-1 could serve as a novel milk coagulant for potential application in making cheese with desired proteolysis. |
| doi_str_mv | 10.1007/s00217-019-03361-6 |
| format | Article |
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Bacillus amyloliquefaciens
GSBa-1 was purified and identified to belong to the peptidase M4 family, and the mature peptide with milk-clotting activity (MCA) was a neutral metalloproteinase with molecular mass of about 38 kDa. The optimal pH and temperature were determined to be at 5.5 and 57 °C for MCA, and at 7.0 and 57 °C for the proteolytic activity, respectively. The MCE exhibited slight autolysis that could be inhibited by Ca
2+
and Na
+
. Hydrolysis of caseins revealed that κ-casein exhibited higher sensitivity to the MCE action than α- and β-casein. By in-gel tryptic digestion and LC–MS/MS analysis of the major peptide (about 13 kDa) generated from hydrolysis of κ-casein by the MCE, the cleavage site was identified to be at Lys 111–Lys 112, which was different from those of other MCEs reported earlier. The MCE from
B. amyloliquefaciens
GSBa-1 could serve as a novel milk coagulant for potential application in making cheese with desired proteolysis.</description><identifier>ISSN: 1438-2377</identifier><identifier>EISSN: 1438-2385</identifier><identifier>DOI: 10.1007/s00217-019-03361-6</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Agriculture ; Analytical Chemistry ; Autolysis ; Bacillus amyloliquefaciens ; Bacteria ; Biotechnology ; Calcium ; Calcium ions ; Casein ; Cheese ; Chemistry ; Chemistry and Materials Science ; Clotting ; Coagulants ; Enzymes ; Food Science ; Forestry ; Hydrolysis ; Metalloproteinase ; Milk ; Original Paper ; Peptidase ; Peptides ; Proteolysis ; Purification</subject><ispartof>European food research & technology, 2019-11, Vol.245 (11), p.2447-2457</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2019</rights><rights>European Food Research and Technology is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c319t-f857a0161784b3e187eca928243ed7a491ba2cd9c9714880e1f5b2559291c5063</citedby><cites>FETCH-LOGICAL-c319t-f857a0161784b3e187eca928243ed7a491ba2cd9c9714880e1f5b2559291c5063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00217-019-03361-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00217-019-03361-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Zhao, Xiao</creatorcontrib><creatorcontrib>Cai, Miao</creatorcontrib><creatorcontrib>Yang, Zhi-Jie</creatorcontrib><creatorcontrib>Luo, Tian-Qi</creatorcontrib><creatorcontrib>Sarwar, Abid</creatorcontrib><creatorcontrib>Megrous, Sarah</creatorcontrib><creatorcontrib>Aziz, Tariq</creatorcontrib><creatorcontrib>Yang, Zhen-Nai</creatorcontrib><title>Purification and characterization of a novel milk-clotting enzyme produced by Bacillus amyloliquefaciens GSBa-1</title><title>European food research & technology</title><addtitle>Eur Food Res Technol</addtitle><description>A novel milk-clotting enzyme (MCE) produced by
Bacillus amyloliquefaciens
GSBa-1 was purified and identified to belong to the peptidase M4 family, and the mature peptide with milk-clotting activity (MCA) was a neutral metalloproteinase with molecular mass of about 38 kDa. The optimal pH and temperature were determined to be at 5.5 and 57 °C for MCA, and at 7.0 and 57 °C for the proteolytic activity, respectively. The MCE exhibited slight autolysis that could be inhibited by Ca
2+
and Na
+
. Hydrolysis of caseins revealed that κ-casein exhibited higher sensitivity to the MCE action than α- and β-casein. By in-gel tryptic digestion and LC–MS/MS analysis of the major peptide (about 13 kDa) generated from hydrolysis of κ-casein by the MCE, the cleavage site was identified to be at Lys 111–Lys 112, which was different from those of other MCEs reported earlier. The MCE from
B. amyloliquefaciens
GSBa-1 could serve as a novel milk coagulant for potential application in making cheese with desired proteolysis.</description><subject>Agriculture</subject><subject>Analytical Chemistry</subject><subject>Autolysis</subject><subject>Bacillus amyloliquefaciens</subject><subject>Bacteria</subject><subject>Biotechnology</subject><subject>Calcium</subject><subject>Calcium ions</subject><subject>Casein</subject><subject>Cheese</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Clotting</subject><subject>Coagulants</subject><subject>Enzymes</subject><subject>Food Science</subject><subject>Forestry</subject><subject>Hydrolysis</subject><subject>Metalloproteinase</subject><subject>Milk</subject><subject>Original Paper</subject><subject>Peptidase</subject><subject>Peptides</subject><subject>Proteolysis</subject><subject>Purification</subject><issn>1438-2377</issn><issn>1438-2385</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kEFLxDAQhYsouK7-AU8Bz9FM0jbN0RVdhQUF9RzSNF2zts2atEL315u1ojdPMwzvffN4SXIO5BII4VeBEAocExCYMJYDzg-SGaSswJQV2eHvzvlxchLChpBM5JDOEvc0eFtbrXrrOqS6Cuk35ZXujbe76ehqpFDnPk2DWtu8Y924vrfdGpluN7YGbb2rBm0qVI5oobRtmiEg1Y6Na-zHYOp4Ml1Ay-eFwnCaHNWqCebsZ86T17vbl5t7vHpcPtxcr7BmIHpcFxlXBHLgRVoyAwU3Wgla0JSZiqtUQKmoroQWHNKiIAbqrKRZJqgAnZGczZOLiRvTxRChlxs3-C6-lJSKSKZRG1V0UmnvQvCmlltvW-VHCUTui5VTsTIWK7-LlXs0m0whiru18X_of1xf5fV7sw</recordid><startdate>20191101</startdate><enddate>20191101</enddate><creator>Zhao, Xiao</creator><creator>Cai, Miao</creator><creator>Yang, Zhi-Jie</creator><creator>Luo, Tian-Qi</creator><creator>Sarwar, Abid</creator><creator>Megrous, 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and characterization of a novel milk-clotting enzyme produced by Bacillus amyloliquefaciens GSBa-1</title><author>Zhao, Xiao ; Cai, Miao ; Yang, Zhi-Jie ; Luo, Tian-Qi ; Sarwar, Abid ; Megrous, Sarah ; Aziz, Tariq ; Yang, Zhen-Nai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c319t-f857a0161784b3e187eca928243ed7a491ba2cd9c9714880e1f5b2559291c5063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Agriculture</topic><topic>Analytical Chemistry</topic><topic>Autolysis</topic><topic>Bacillus amyloliquefaciens</topic><topic>Bacteria</topic><topic>Biotechnology</topic><topic>Calcium</topic><topic>Calcium ions</topic><topic>Casein</topic><topic>Cheese</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Clotting</topic><topic>Coagulants</topic><topic>Enzymes</topic><topic>Food Science</topic><topic>Forestry</topic><topic>Hydrolysis</topic><topic>Metalloproteinase</topic><topic>Milk</topic><topic>Original Paper</topic><topic>Peptidase</topic><topic>Peptides</topic><topic>Proteolysis</topic><topic>Purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Xiao</creatorcontrib><creatorcontrib>Cai, Miao</creatorcontrib><creatorcontrib>Yang, Zhi-Jie</creatorcontrib><creatorcontrib>Luo, Tian-Qi</creatorcontrib><creatorcontrib>Sarwar, Abid</creatorcontrib><creatorcontrib>Megrous, Sarah</creatorcontrib><creatorcontrib>Aziz, Tariq</creatorcontrib><creatorcontrib>Yang, Zhen-Nai</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Career & Technical Education Database</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology 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Zhen-Nai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of a novel milk-clotting enzyme produced by Bacillus amyloliquefaciens GSBa-1</atitle><jtitle>European food research & technology</jtitle><stitle>Eur Food Res Technol</stitle><date>2019-11-01</date><risdate>2019</risdate><volume>245</volume><issue>11</issue><spage>2447</spage><epage>2457</epage><pages>2447-2457</pages><issn>1438-2377</issn><eissn>1438-2385</eissn><abstract>A novel milk-clotting enzyme (MCE) produced by
Bacillus amyloliquefaciens
GSBa-1 was purified and identified to belong to the peptidase M4 family, and the mature peptide with milk-clotting activity (MCA) was a neutral metalloproteinase with molecular mass of about 38 kDa. The optimal pH and temperature were determined to be at 5.5 and 57 °C for MCA, and at 7.0 and 57 °C for the proteolytic activity, respectively. The MCE exhibited slight autolysis that could be inhibited by Ca
2+
and Na
+
. Hydrolysis of caseins revealed that κ-casein exhibited higher sensitivity to the MCE action than α- and β-casein. By in-gel tryptic digestion and LC–MS/MS analysis of the major peptide (about 13 kDa) generated from hydrolysis of κ-casein by the MCE, the cleavage site was identified to be at Lys 111–Lys 112, which was different from those of other MCEs reported earlier. The MCE from
B. amyloliquefaciens
GSBa-1 could serve as a novel milk coagulant for potential application in making cheese with desired proteolysis.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><doi>10.1007/s00217-019-03361-6</doi><tpages>11</tpages></addata></record> |
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| source | Springer Nature - Complete Springer Journals |
| subjects | Agriculture Analytical Chemistry Autolysis Bacillus amyloliquefaciens Bacteria Biotechnology Calcium Calcium ions Casein Cheese Chemistry Chemistry and Materials Science Clotting Coagulants Enzymes Food Science Forestry Hydrolysis Metalloproteinase Milk Original Paper Peptidase Peptides Proteolysis Purification |
| title | Purification and characterization of a novel milk-clotting enzyme produced by Bacillus amyloliquefaciens GSBa-1 |
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