Efficient production of l-asparaginase from Bacillus licheniformis with low-glutaminase activity: Optimization, scale up and acrylamide degradation studies
► Production of l-asparaginase from Bacillus licheniformis and its statistical optimization. ► High yields of enzyme obtained i.e. 32IU/ml in 18h after statistical optimization. ► Optimized process yielded 30IU/ml of enzyme in 15h is obtained in 30L fermenter. ► l-Asparaginse produced by B. lichenif...
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Veröffentlicht in: | Bioresource technology 2012-12, Vol.125, p.11-16 |
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creator | Mahajan, Richi V. Saran, Saurabh Kameswaran, Karthikeya Kumar, Vinod Saxena, R.K. |
description | ► Production of l-asparaginase from Bacillus licheniformis and its statistical optimization. ► High yields of enzyme obtained i.e. 32IU/ml in 18h after statistical optimization. ► Optimized process yielded 30IU/ml of enzyme in 15h is obtained in 30L fermenter. ► l-Asparaginse produced by B. licheniformis is free of glutaminase activity. ► l-Asparaginase produced was efficiently able to degrade polyacrylamide.
l-Asparaginase has potential as an anti-cancer drug and for prevention of acrylamide formation in fried and baked foods. Production of the enzyme by Bacillus licheniformis (RAM-8) was optimized by process engineering using a statistical modeling approach and a maximum yield of 32.26IU/ml was achieved. The l-asparaginase exhibited glutaminase activity of only 0.8IU/ml and would therefore be less prone to cause the side effects associated with asparaginase therapy compared to enzyme preparations with higher glutaminase activities. When production was carried out in a 30-L bioreactor, enzyme production reached 29.94IU/ml in 15h. The enzyme inhibited poly-acrylamide formation in 10% acrylamide solution and reduced acrylamide formation in fried potatoes by 80%. |
doi_str_mv | 10.1016/j.biortech.2012.08.086 |
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l-Asparaginase has potential as an anti-cancer drug and for prevention of acrylamide formation in fried and baked foods. Production of the enzyme by Bacillus licheniformis (RAM-8) was optimized by process engineering using a statistical modeling approach and a maximum yield of 32.26IU/ml was achieved. The l-asparaginase exhibited glutaminase activity of only 0.8IU/ml and would therefore be less prone to cause the side effects associated with asparaginase therapy compared to enzyme preparations with higher glutaminase activities. When production was carried out in a 30-L bioreactor, enzyme production reached 29.94IU/ml in 15h. The enzyme inhibited poly-acrylamide formation in 10% acrylamide solution and reduced acrylamide formation in fried potatoes by 80%.</description><identifier>ISSN: 0960-8524</identifier><identifier>EISSN: 1873-2976</identifier><identifier>DOI: 10.1016/j.biortech.2012.08.086</identifier><identifier>PMID: 23018158</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Acrylamide ; Asparaginase - biosynthesis ; Asparaginase - chemistry ; Asparaginase - isolation & purification ; Bacillus - enzymology ; Bacillus - growth & development ; Bacillus licheniformis ; Bioreactors ; Bioreactors - microbiology ; Cell Culture Techniques - methods ; Computer Simulation ; Enzyme Activation ; Enzymes ; Fermentation ; Glutaminase ; Glutaminase - biosynthesis ; Glutaminase - chemistry ; l-Asparaginase ; l-Asparagine ; Low glutaminase ; Mathematical models ; Models, Biological ; Optimization ; Polyacrylamide-degradation ; Side effects</subject><ispartof>Bioresource technology, 2012-12, Vol.125, p.11-16</ispartof><rights>2012 Elsevier Ltd</rights><rights>Copyright © 2012 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-cd88c80b6ee65acc28f631037bc4e448b573bff8f43178561cac11272ff34cef3</citedby><cites>FETCH-LOGICAL-c434t-cd88c80b6ee65acc28f631037bc4e448b573bff8f43178561cac11272ff34cef3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0960852412012813$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23018158$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mahajan, Richi V.</creatorcontrib><creatorcontrib>Saran, Saurabh</creatorcontrib><creatorcontrib>Kameswaran, Karthikeya</creatorcontrib><creatorcontrib>Kumar, Vinod</creatorcontrib><creatorcontrib>Saxena, R.K.</creatorcontrib><title>Efficient production of l-asparaginase from Bacillus licheniformis with low-glutaminase activity: Optimization, scale up and acrylamide degradation studies</title><title>Bioresource technology</title><addtitle>Bioresour Technol</addtitle><description>► Production of l-asparaginase from Bacillus licheniformis and its statistical optimization. ► High yields of enzyme obtained i.e. 32IU/ml in 18h after statistical optimization. ► Optimized process yielded 30IU/ml of enzyme in 15h is obtained in 30L fermenter. ► l-Asparaginse produced by B. licheniformis is free of glutaminase activity. ► l-Asparaginase produced was efficiently able to degrade polyacrylamide.
l-Asparaginase has potential as an anti-cancer drug and for prevention of acrylamide formation in fried and baked foods. Production of the enzyme by Bacillus licheniformis (RAM-8) was optimized by process engineering using a statistical modeling approach and a maximum yield of 32.26IU/ml was achieved. The l-asparaginase exhibited glutaminase activity of only 0.8IU/ml and would therefore be less prone to cause the side effects associated with asparaginase therapy compared to enzyme preparations with higher glutaminase activities. When production was carried out in a 30-L bioreactor, enzyme production reached 29.94IU/ml in 15h. The enzyme inhibited poly-acrylamide formation in 10% acrylamide solution and reduced acrylamide formation in fried potatoes by 80%.</description><subject>Acrylamide</subject><subject>Asparaginase - biosynthesis</subject><subject>Asparaginase - chemistry</subject><subject>Asparaginase - isolation & purification</subject><subject>Bacillus - enzymology</subject><subject>Bacillus - growth & development</subject><subject>Bacillus licheniformis</subject><subject>Bioreactors</subject><subject>Bioreactors - microbiology</subject><subject>Cell Culture Techniques - methods</subject><subject>Computer Simulation</subject><subject>Enzyme Activation</subject><subject>Enzymes</subject><subject>Fermentation</subject><subject>Glutaminase</subject><subject>Glutaminase - biosynthesis</subject><subject>Glutaminase - chemistry</subject><subject>l-Asparaginase</subject><subject>l-Asparagine</subject><subject>Low glutaminase</subject><subject>Mathematical models</subject><subject>Models, Biological</subject><subject>Optimization</subject><subject>Polyacrylamide-degradation</subject><subject>Side effects</subject><issn>0960-8524</issn><issn>1873-2976</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1uEzEUhS0EoqHwCpWXLJhgjz22wwqoyo9UqRtYWx77OnHk-cH2tAqvwsvikJZtpCvdzXfO1T0HoStK1pRQ8X6_7sOUCtjduiW0XRNVRzxDK6oka9qNFM_RimwEaVTX8gv0Kuc9IYRR2b5EFy0jVNFOrdCfG--DDTAWPKfJLbaEacSTx7ExeTbJbMNoMmCfpgF_NjbEuGQcg93BGPyUhpDxQyg7HKeHZhuXYoaTwFSn-1AOH_DdXMIQfpuj8zucrYmAlxmb0VUoHWJVOMAOtsm4fxDOZXEB8mv0wpuY4c3jvkQ_v9z8uP7W3N59_X796baxnPHSWKeUVaQXAKIz1rbKC0YJk73lwLnqO8l675Xn9XvVCWqNpbSVrfeMW_DsEr09-dYEfi2Qi65fWYjRjDAtWVMhacfaDZXn0Y4QKSmnm_Mo5UxJwgmrqDihNk05J_B6TmEw6aAp0ce69V4_1a2PdWui6ogqvHq8sfQDuP-yp34r8PEEQM3vPkDS-Vi2BRcS2KLdFM7d-AtDjMLJ</recordid><startdate>201212</startdate><enddate>201212</enddate><creator>Mahajan, Richi V.</creator><creator>Saran, Saurabh</creator><creator>Kameswaran, Karthikeya</creator><creator>Kumar, Vinod</creator><creator>Saxena, R.K.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7SU</scope><scope>7TB</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>KR7</scope></search><sort><creationdate>201212</creationdate><title>Efficient production of l-asparaginase from Bacillus licheniformis with low-glutaminase activity: Optimization, scale up and acrylamide degradation studies</title><author>Mahajan, Richi V. ; Saran, Saurabh ; Kameswaran, Karthikeya ; Kumar, Vinod ; Saxena, R.K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-cd88c80b6ee65acc28f631037bc4e448b573bff8f43178561cac11272ff34cef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Acrylamide</topic><topic>Asparaginase - biosynthesis</topic><topic>Asparaginase - chemistry</topic><topic>Asparaginase - isolation & purification</topic><topic>Bacillus - enzymology</topic><topic>Bacillus - growth & development</topic><topic>Bacillus licheniformis</topic><topic>Bioreactors</topic><topic>Bioreactors - microbiology</topic><topic>Cell Culture Techniques - methods</topic><topic>Computer Simulation</topic><topic>Enzyme Activation</topic><topic>Enzymes</topic><topic>Fermentation</topic><topic>Glutaminase</topic><topic>Glutaminase - biosynthesis</topic><topic>Glutaminase - chemistry</topic><topic>l-Asparaginase</topic><topic>l-Asparagine</topic><topic>Low glutaminase</topic><topic>Mathematical models</topic><topic>Models, Biological</topic><topic>Optimization</topic><topic>Polyacrylamide-degradation</topic><topic>Side effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mahajan, Richi V.</creatorcontrib><creatorcontrib>Saran, Saurabh</creatorcontrib><creatorcontrib>Kameswaran, Karthikeya</creatorcontrib><creatorcontrib>Kumar, Vinod</creatorcontrib><creatorcontrib>Saxena, R.K.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Environmental Engineering Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Civil Engineering Abstracts</collection><jtitle>Bioresource technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mahajan, Richi V.</au><au>Saran, Saurabh</au><au>Kameswaran, Karthikeya</au><au>Kumar, Vinod</au><au>Saxena, R.K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Efficient production of l-asparaginase from Bacillus licheniformis with low-glutaminase activity: Optimization, scale up and acrylamide degradation studies</atitle><jtitle>Bioresource technology</jtitle><addtitle>Bioresour Technol</addtitle><date>2012-12</date><risdate>2012</risdate><volume>125</volume><spage>11</spage><epage>16</epage><pages>11-16</pages><issn>0960-8524</issn><eissn>1873-2976</eissn><abstract>► Production of l-asparaginase from Bacillus licheniformis and its statistical optimization. ► High yields of enzyme obtained i.e. 32IU/ml in 18h after statistical optimization. ► Optimized process yielded 30IU/ml of enzyme in 15h is obtained in 30L fermenter. ► l-Asparaginse produced by B. licheniformis is free of glutaminase activity. ► l-Asparaginase produced was efficiently able to degrade polyacrylamide.
l-Asparaginase has potential as an anti-cancer drug and for prevention of acrylamide formation in fried and baked foods. Production of the enzyme by Bacillus licheniformis (RAM-8) was optimized by process engineering using a statistical modeling approach and a maximum yield of 32.26IU/ml was achieved. The l-asparaginase exhibited glutaminase activity of only 0.8IU/ml and would therefore be less prone to cause the side effects associated with asparaginase therapy compared to enzyme preparations with higher glutaminase activities. When production was carried out in a 30-L bioreactor, enzyme production reached 29.94IU/ml in 15h. The enzyme inhibited poly-acrylamide formation in 10% acrylamide solution and reduced acrylamide formation in fried potatoes by 80%.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>23018158</pmid><doi>10.1016/j.biortech.2012.08.086</doi><tpages>6</tpages></addata></record> |
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subjects | Acrylamide Asparaginase - biosynthesis Asparaginase - chemistry Asparaginase - isolation & purification Bacillus - enzymology Bacillus - growth & development Bacillus licheniformis Bioreactors Bioreactors - microbiology Cell Culture Techniques - methods Computer Simulation Enzyme Activation Enzymes Fermentation Glutaminase Glutaminase - biosynthesis Glutaminase - chemistry l-Asparaginase l-Asparagine Low glutaminase Mathematical models Models, Biological Optimization Polyacrylamide-degradation Side effects |
title | Efficient production of l-asparaginase from Bacillus licheniformis with low-glutaminase activity: Optimization, scale up and acrylamide degradation studies |
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