Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana
Abstract Extracellular amylase production by the moderate halophile Halomonas meridiana was optimized and the enzyme was characterized biochemically. The highest amylase production was achieved by growing H. meridiana cultures in media with 5% salts and starch, in the absence of glucose until the en...
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Veröffentlicht in: | FEMS microbiology letters 2000-02, Vol.183 (1), p.67-71 |
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creator | Coronado, María-José Vargas, Carmen Hofemeister, Jürgen Ventosa, Antonio Nieto, Joaquín J. |
description | Abstract
Extracellular amylase production by the moderate halophile Halomonas meridiana was optimized and the enzyme was characterized biochemically. The highest amylase production was achieved by growing H. meridiana cultures in media with 5% salts and starch, in the absence of glucose until the end of the exponential phase. The amylase exhibited maximal activity at pH 7.0, being relatively stable in alkaline conditions. Optimal temperature and salinity for activity were 37°C and 10% NaCl, respectively. Moreover, activity at salinity as high as 30% salts was detected. Maltose and maltotriose were the main end products of starch hydrolysis, indicating an α-amylase activity. |
doi_str_mv | 10.1111/j.1574-6968.2000.tb08935.x |
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Extracellular amylase production by the moderate halophile Halomonas meridiana was optimized and the enzyme was characterized biochemically. The highest amylase production was achieved by growing H. meridiana cultures in media with 5% salts and starch, in the absence of glucose until the end of the exponential phase. The amylase exhibited maximal activity at pH 7.0, being relatively stable in alkaline conditions. Optimal temperature and salinity for activity were 37°C and 10% NaCl, respectively. Moreover, activity at salinity as high as 30% salts was detected. Maltose and maltotriose were the main end products of starch hydrolysis, indicating an α-amylase activity.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2000.tb08935.x</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amylase production ; Amylases ; Halomonas meridiana ; Maltose ; Maltotriose ; Microbiology ; Moderate halophile ; Salinity ; Salinity effects ; Salts ; Sodium chloride ; Starch ; α-Amylase</subject><ispartof>FEMS microbiology letters, 2000-02, Vol.183 (1), p.67-71</ispartof><rights>2000 Federation of European Microbiological Societies 2000</rights><rights>2000 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2000.tb08935.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2000.tb08935.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids></links><search><creatorcontrib>Coronado, María-José</creatorcontrib><creatorcontrib>Vargas, Carmen</creatorcontrib><creatorcontrib>Hofemeister, Jürgen</creatorcontrib><creatorcontrib>Ventosa, Antonio</creatorcontrib><creatorcontrib>Nieto, Joaquín J.</creatorcontrib><title>Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana</title><title>FEMS microbiology letters</title><description>Abstract
Extracellular amylase production by the moderate halophile Halomonas meridiana was optimized and the enzyme was characterized biochemically. The highest amylase production was achieved by growing H. meridiana cultures in media with 5% salts and starch, in the absence of glucose until the end of the exponential phase. The amylase exhibited maximal activity at pH 7.0, being relatively stable in alkaline conditions. Optimal temperature and salinity for activity were 37°C and 10% NaCl, respectively. Moreover, activity at salinity as high as 30% salts was detected. Maltose and maltotriose were the main end products of starch hydrolysis, indicating an α-amylase activity.</description><subject>Amylase production</subject><subject>Amylases</subject><subject>Halomonas meridiana</subject><subject>Maltose</subject><subject>Maltotriose</subject><subject>Microbiology</subject><subject>Moderate halophile</subject><subject>Salinity</subject><subject>Salinity effects</subject><subject>Salts</subject><subject>Sodium chloride</subject><subject>Starch</subject><subject>α-Amylase</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kE1OwzAQRi0EEqVwBwvWCf5J7GTBAlWUIhXBAtbWJHaUREkcnFS03IqLcCYcWrECb8bSvG9m9BC6pCSk_l3XIY1lFIhUJCEjhIRjRpKUx-H2CM1-W8doRrhMAkpSeYrOhqH2aMSImKHm2Vm9ycfKdhg6jbPK5qVpqxwanJfgIB-Nqz7gB7CFZ_DXZwDtroHB4MLZFo-lwa3VxsFocAmN7cuqMXjlf63tYMCtn6Ar6OAcnRTQDObiUOfodXn3slgF66f7h8XtOrCUJTLQlBSpprEAaYqYcCpzQgVEhaTAM6kjJkXOjO_KxOSS8SgDyWKdpXEsRUr5HF3t5_bOvm3MMKrablznVyrGKSUiEVHiqZs99e7P3aneVS24naJETWpVrSZ_avKnJrXqoFZt1fJxLaTPx_u83fT_pIM_0vwbq2uBbQ</recordid><startdate>20000201</startdate><enddate>20000201</enddate><creator>Coronado, María-José</creator><creator>Vargas, Carmen</creator><creator>Hofemeister, Jürgen</creator><creator>Ventosa, Antonio</creator><creator>Nieto, Joaquín J.</creator><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>20000201</creationdate><title>Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana</title><author>Coronado, María-José ; Vargas, Carmen ; Hofemeister, Jürgen ; Ventosa, Antonio ; Nieto, Joaquín J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-o1287-d10f9d156a7ef50317c016a4f71a3b7d4276c2ea7e78ec7234ba725db95576913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amylase production</topic><topic>Amylases</topic><topic>Halomonas meridiana</topic><topic>Maltose</topic><topic>Maltotriose</topic><topic>Microbiology</topic><topic>Moderate halophile</topic><topic>Salinity</topic><topic>Salinity effects</topic><topic>Salts</topic><topic>Sodium chloride</topic><topic>Starch</topic><topic>α-Amylase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Coronado, María-José</creatorcontrib><creatorcontrib>Vargas, Carmen</creatorcontrib><creatorcontrib>Hofemeister, Jürgen</creatorcontrib><creatorcontrib>Ventosa, Antonio</creatorcontrib><creatorcontrib>Nieto, Joaquín J.</creatorcontrib><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Coronado, María-José</au><au>Vargas, Carmen</au><au>Hofemeister, Jürgen</au><au>Ventosa, Antonio</au><au>Nieto, Joaquín J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana</atitle><jtitle>FEMS microbiology letters</jtitle><date>2000-02-01</date><risdate>2000</risdate><volume>183</volume><issue>1</issue><spage>67</spage><epage>71</epage><pages>67-71</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><abstract>Abstract
Extracellular amylase production by the moderate halophile Halomonas meridiana was optimized and the enzyme was characterized biochemically. The highest amylase production was achieved by growing H. meridiana cultures in media with 5% salts and starch, in the absence of glucose until the end of the exponential phase. The amylase exhibited maximal activity at pH 7.0, being relatively stable in alkaline conditions. Optimal temperature and salinity for activity were 37°C and 10% NaCl, respectively. Moreover, activity at salinity as high as 30% salts was detected. Maltose and maltotriose were the main end products of starch hydrolysis, indicating an α-amylase activity.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1574-6968.2000.tb08935.x</doi><tpages>5</tpages></addata></record> |
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source | Oxford University Press Journals All Titles (1996-Current); Wiley Online Library All Journals; Alma/SFX Local Collection |
subjects | Amylase production Amylases Halomonas meridiana Maltose Maltotriose Microbiology Moderate halophile Salinity Salinity effects Salts Sodium chloride Starch α-Amylase |
title | Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana |
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