Organic solvent tolerant metallo protease of novel isolate Serratia marcescens PPB-26: production and characterization
Proteases are a class of enzymes that catalyze hydrolysis of peptide bonds of proteins. In this study, 221 proteolytic bacterial isolates were obtained by enrichment culture method from soils of various regions of Himachal Pradesh, India. From these a hyper producer of protease was screened and iden...
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| Veröffentlicht in: | 3 Biotech 2016-12, Vol.6 (2), p.180-11, Article 180 |
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| creator | Thakur, Shikha Sharma, Nirmal Kant Thakur, Neerja Savitri Bhalla, Tek Chand |
| description | Proteases are a class of enzymes that catalyze hydrolysis of peptide bonds of proteins. In this study, 221 proteolytic bacterial isolates were obtained by enrichment culture method from soils of various regions of Himachal Pradesh, India. From these a hyper producer of protease was screened and identified by morphological and physiological testing and by 16S rDNA sequence as
Serratia marcescens
PPB-26. Statistical optimization of physiochemical parameters enhanced the protease production by 75 %. Protease of
S. marcescens
PPB-26 was classified as a metalloprotease. It showed optimal activity at 30 °C, pH 7.5 (0.15 M Tris–HCl buffer) and with 0.8 % substrate concentration. It had
K
m
= 0.3 %,
V
max
= 34.5 μmol min
−1
mg
−1
protein and a half life of 2 days at 30 °C. The enzyme was stable in most metal ions but showed increased activity with Fe
2+
and Cu
2+
while strong inhibition with Co
2+
and Zn
2+
. Further investigation showed that the enzyme could not only retain its activity in various organic solvents but also showed increased activity with methanol and ethanol. The reported metalloprotease is thus a potential candidate for carrying out industrial peptide synthesis. |
| doi_str_mv | 10.1007/s13205-016-0500-0 |
| format | Article |
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Serratia marcescens
PPB-26. Statistical optimization of physiochemical parameters enhanced the protease production by 75 %. Protease of
S. marcescens
PPB-26 was classified as a metalloprotease. It showed optimal activity at 30 °C, pH 7.5 (0.15 M Tris–HCl buffer) and with 0.8 % substrate concentration. It had
K
m
= 0.3 %,
V
max
= 34.5 μmol min
−1
mg
−1
protein and a half life of 2 days at 30 °C. The enzyme was stable in most metal ions but showed increased activity with Fe
2+
and Cu
2+
while strong inhibition with Co
2+
and Zn
2+
. Further investigation showed that the enzyme could not only retain its activity in various organic solvents but also showed increased activity with methanol and ethanol. The reported metalloprotease is thus a potential candidate for carrying out industrial peptide synthesis.</description><identifier>ISSN: 2190-572X</identifier><identifier>EISSN: 2190-5738</identifier><identifier>DOI: 10.1007/s13205-016-0500-0</identifier><identifier>PMID: 28330252</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Agriculture ; Bacteria ; Bioinformatics ; Biomaterials ; Biotechnology ; Cancer Research ; Catalysis ; Chemistry ; Chemistry and Materials Science ; Enzymes ; Original ; Original Article ; Peptides ; Physiology ; Proteins ; Serratia marcescens ; Solvents ; Stem Cells</subject><ispartof>3 Biotech, 2016-12, Vol.6 (2), p.180-11, Article 180</ispartof><rights>The Author(s) 2016</rights><rights>3 Biotech is a copyright of Springer, 2016.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-cc8819b91b26ad1755011990dd03e526cd29b3ad2c5e972ea4768059f8fb4b5a3</citedby><cites>FETCH-LOGICAL-c503t-cc8819b91b26ad1755011990dd03e526cd29b3ad2c5e972ea4768059f8fb4b5a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4999571/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4999571/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,41488,42557,51319,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28330252$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thakur, Shikha</creatorcontrib><creatorcontrib>Sharma, Nirmal Kant</creatorcontrib><creatorcontrib>Thakur, Neerja</creatorcontrib><creatorcontrib>Savitri</creatorcontrib><creatorcontrib>Bhalla, Tek Chand</creatorcontrib><title>Organic solvent tolerant metallo protease of novel isolate Serratia marcescens PPB-26: production and characterization</title><title>3 Biotech</title><addtitle>3 Biotech</addtitle><addtitle>3 Biotech</addtitle><description>Proteases are a class of enzymes that catalyze hydrolysis of peptide bonds of proteins. In this study, 221 proteolytic bacterial isolates were obtained by enrichment culture method from soils of various regions of Himachal Pradesh, India. From these a hyper producer of protease was screened and identified by morphological and physiological testing and by 16S rDNA sequence as
Serratia marcescens
PPB-26. Statistical optimization of physiochemical parameters enhanced the protease production by 75 %. Protease of
S. marcescens
PPB-26 was classified as a metalloprotease. It showed optimal activity at 30 °C, pH 7.5 (0.15 M Tris–HCl buffer) and with 0.8 % substrate concentration. It had
K
m
= 0.3 %,
V
max
= 34.5 μmol min
−1
mg
−1
protein and a half life of 2 days at 30 °C. The enzyme was stable in most metal ions but showed increased activity with Fe
2+
and Cu
2+
while strong inhibition with Co
2+
and Zn
2+
. Further investigation showed that the enzyme could not only retain its activity in various organic solvents but also showed increased activity with methanol and ethanol. The reported metalloprotease is thus a potential candidate for carrying out industrial peptide synthesis.</description><subject>Agriculture</subject><subject>Bacteria</subject><subject>Bioinformatics</subject><subject>Biomaterials</subject><subject>Biotechnology</subject><subject>Cancer Research</subject><subject>Catalysis</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Enzymes</subject><subject>Original</subject><subject>Original Article</subject><subject>Peptides</subject><subject>Physiology</subject><subject>Proteins</subject><subject>Serratia marcescens</subject><subject>Solvents</subject><subject>Stem Cells</subject><issn>2190-572X</issn><issn>2190-5738</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNklFrFDEQxxdRbKn9AL5IwBdfVifJZbPxQbDFqlBoQQXfwmx29rplLzmT7IF--ma5elRBMC8ZMr_5Zyb5V9VzDq85gH6TuBSgauBNDQqghkfVseAGaqVl-_gQi-9H1WlKt1CW4spweFodiVZKEEocV7uruEY_OpbCtCOfWQ4TRSzBhjJOU2DbGDJhIhYG5sOOJjYWFjOxLxQj5hHZBqOj5Mgndn19Vovm7VLVzy6PwTP0PXM3GNFliuMvXA6fVU8GnBKd3u8n1beLD1_PP9WXVx8_n7-_rJ0CmWvn2pabzvBONNhzrRRwbgz0PUhSonG9MJ3EXjhFRgvClW5aUGZoh27VKZQn1bu97nbuNtSXFnPEyW7jWHr-aQOO9s-MH2_sOuzsyhijNC8Cr-4FYvgxU8p2M5ZJpwk9hTlZ3rawarRq9H-gQhsJUqqCvvwLvQ1z9OUlCtUoIRvTQqH4nnIxpBRpOPTNwS4esHsP2OIBu3jALjUvHg58qPj94wUQeyCVlF9TfHD1P1XvAMvavWk</recordid><startdate>20161201</startdate><enddate>20161201</enddate><creator>Thakur, Shikha</creator><creator>Sharma, Nirmal Kant</creator><creator>Thakur, Neerja</creator><creator>Savitri</creator><creator>Bhalla, Tek Chand</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><scope>C6C</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8AO</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>ABJCF</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>L6V</scope><scope>LK8</scope><scope>M7P</scope><scope>M7S</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20161201</creationdate><title>Organic solvent tolerant metallo protease of novel isolate Serratia marcescens PPB-26: production and characterization</title><author>Thakur, Shikha ; Sharma, Nirmal Kant ; Thakur, Neerja ; Savitri ; Bhalla, Tek Chand</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-cc8819b91b26ad1755011990dd03e526cd29b3ad2c5e972ea4768059f8fb4b5a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Agriculture</topic><topic>Bacteria</topic><topic>Bioinformatics</topic><topic>Biomaterials</topic><topic>Biotechnology</topic><topic>Cancer Research</topic><topic>Catalysis</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Enzymes</topic><topic>Original</topic><topic>Original Article</topic><topic>Peptides</topic><topic>Physiology</topic><topic>Proteins</topic><topic>Serratia marcescens</topic><topic>Solvents</topic><topic>Stem Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thakur, Shikha</creatorcontrib><creatorcontrib>Sharma, Nirmal Kant</creatorcontrib><creatorcontrib>Thakur, Neerja</creatorcontrib><creatorcontrib>Savitri</creatorcontrib><creatorcontrib>Bhalla, Tek Chand</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>3 Biotech</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Thakur, Shikha</au><au>Sharma, Nirmal Kant</au><au>Thakur, Neerja</au><au>Savitri</au><au>Bhalla, Tek Chand</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Organic solvent tolerant metallo protease of novel isolate Serratia marcescens PPB-26: production and characterization</atitle><jtitle>3 Biotech</jtitle><stitle>3 Biotech</stitle><addtitle>3 Biotech</addtitle><date>2016-12-01</date><risdate>2016</risdate><volume>6</volume><issue>2</issue><spage>180</spage><epage>11</epage><pages>180-11</pages><artnum>180</artnum><issn>2190-572X</issn><eissn>2190-5738</eissn><abstract>Proteases are a class of enzymes that catalyze hydrolysis of peptide bonds of proteins. In this study, 221 proteolytic bacterial isolates were obtained by enrichment culture method from soils of various regions of Himachal Pradesh, India. From these a hyper producer of protease was screened and identified by morphological and physiological testing and by 16S rDNA sequence as
Serratia marcescens
PPB-26. Statistical optimization of physiochemical parameters enhanced the protease production by 75 %. Protease of
S. marcescens
PPB-26 was classified as a metalloprotease. It showed optimal activity at 30 °C, pH 7.5 (0.15 M Tris–HCl buffer) and with 0.8 % substrate concentration. It had
K
m
= 0.3 %,
V
max
= 34.5 μmol min
−1
mg
−1
protein and a half life of 2 days at 30 °C. The enzyme was stable in most metal ions but showed increased activity with Fe
2+
and Cu
2+
while strong inhibition with Co
2+
and Zn
2+
. Further investigation showed that the enzyme could not only retain its activity in various organic solvents but also showed increased activity with methanol and ethanol. The reported metalloprotease is thus a potential candidate for carrying out industrial peptide synthesis.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>28330252</pmid><doi>10.1007/s13205-016-0500-0</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | 3 Biotech, 2016-12, Vol.6 (2), p.180-11, Article 180 |
| issn | 2190-572X 2190-5738 |
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| source | SpringerNature Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Agriculture Bacteria Bioinformatics Biomaterials Biotechnology Cancer Research Catalysis Chemistry Chemistry and Materials Science Enzymes Original Original Article Peptides Physiology Proteins Serratia marcescens Solvents Stem Cells |
| title | Organic solvent tolerant metallo protease of novel isolate Serratia marcescens PPB-26: production and characterization |
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