Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153)
Phytase (myo-inositol hexaphosphate phosphohydrolase) belongs to phosphatases. It catalyzes the hydrolysis of phytate to less-phosphorylated inorganic phosphates and phytate. Phytase is used primarily for the feeding of simple hermit animals in order to increase the usability of amino acids, mineral...
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| Veröffentlicht in: | Molecular biotechnology 2018-11, Vol.60 (11), p.783-790 |
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| creator | Demir, Yeliz Dikbaş, Neslihan Beydemir, Şükrü |
| description | Phytase (myo-inositol hexaphosphate phosphohydrolase) belongs to phosphatases. It catalyzes the hydrolysis of phytate to less-phosphorylated inorganic phosphates and phytate. Phytase is used primarily for the feeding of simple hermit animals in order to increase the usability of amino acids, minerals, phosphorus and energy. In the present study, phytase isolation from the
Lactobacillus coryniformis
strain, isolated from Lor cheese sources, phytase purification and characterization were studied. The phytase was purified in simple three steps. The enzyme was obtained with 2.60% recovery and a specific activity of 202.25 (EU/mg protein). The molecular mass of the enzyme was determined to be 43.25 kDa with the sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method. The optimum temperature and pH for the enzyme were found as 60 °C and 5.0 and respectively. To defined the substrate specificity of the phytase, the hydrolysis of several phosphorylated compounds by the purified enzyme was studied and sodium phytate showed high specificity. Furthermore, the effects of Ca
2+
, Ag
+
, Mg
2+
, Cu
2+
, Co
2+
, Pb
2+
, Zn
2+
and Ni
2+
metal ions on the enzyme were studied. |
| doi_str_mv | 10.1007/s12033-018-0116-1 |
| format | Article |
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Lactobacillus coryniformis
strain, isolated from Lor cheese sources, phytase purification and characterization were studied. The phytase was purified in simple three steps. The enzyme was obtained with 2.60% recovery and a specific activity of 202.25 (EU/mg protein). The molecular mass of the enzyme was determined to be 43.25 kDa with the sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method. The optimum temperature and pH for the enzyme were found as 60 °C and 5.0 and respectively. To defined the substrate specificity of the phytase, the hydrolysis of several phosphorylated compounds by the purified enzyme was studied and sodium phytate showed high specificity. Furthermore, the effects of Ca
2+
, Ag
+
, Mg
2+
, Cu
2+
, Co
2+
, Pb
2+
, Zn
2+
and Ni
2+
metal ions on the enzyme were studied.</description><identifier>ISSN: 1073-6085</identifier><identifier>EISSN: 1559-0305</identifier><identifier>DOI: 10.1007/s12033-018-0116-1</identifier><identifier>PMID: 30171516</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Amino acids ; Biochemistry ; Biological Techniques ; Biotechnology ; Calcium ; Calcium ions ; Carbon dioxide ; Cell Biology ; Cheese ; Chemistry ; Chemistry and Materials Science ; Cobalt ; Copper ; Electrophoresis ; Enzymes ; Gel electrophoresis ; Human Genetics ; Hydrolysis ; Inositol ; Lactobacillus ; Lead ; Magnesium ; Metal ions ; Minerals ; Original Paper ; Phosphates ; Phosphohydrolase ; Phosphorus ; Phytase ; Protein Science ; Proteins ; Purification ; Silver ; Sodium ; Sodium dodecyl sulfate ; Sodium lauryl sulfate ; Sodium phytate ; Substrate specificity ; Substrates ; Zinc</subject><ispartof>Molecular biotechnology, 2018-11, Vol.60 (11), p.783-790</ispartof><rights>Springer Science+Business Media, LLC, part of Springer Nature 2018</rights><rights>Molecular Biotechnology is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-42dfefba55add90e08fce95685f0176512fa47472509b86bc6751d65fb553c8f3</citedby><cites>FETCH-LOGICAL-c372t-42dfefba55add90e08fce95685f0176512fa47472509b86bc6751d65fb553c8f3</cites><orcidid>0000-0003-3216-1098</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12033-018-0116-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12033-018-0116-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30171516$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Demir, Yeliz</creatorcontrib><creatorcontrib>Dikbaş, Neslihan</creatorcontrib><creatorcontrib>Beydemir, Şükrü</creatorcontrib><title>Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153)</title><title>Molecular biotechnology</title><addtitle>Mol Biotechnol</addtitle><addtitle>Mol Biotechnol</addtitle><description>Phytase (myo-inositol hexaphosphate phosphohydrolase) belongs to phosphatases. It catalyzes the hydrolysis of phytate to less-phosphorylated inorganic phosphates and phytate. Phytase is used primarily for the feeding of simple hermit animals in order to increase the usability of amino acids, minerals, phosphorus and energy. In the present study, phytase isolation from the
Lactobacillus coryniformis
strain, isolated from Lor cheese sources, phytase purification and characterization were studied. The phytase was purified in simple three steps. The enzyme was obtained with 2.60% recovery and a specific activity of 202.25 (EU/mg protein). The molecular mass of the enzyme was determined to be 43.25 kDa with the sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method. The optimum temperature and pH for the enzyme were found as 60 °C and 5.0 and respectively. To defined the substrate specificity of the phytase, the hydrolysis of several phosphorylated compounds by the purified enzyme was studied and sodium phytate showed high specificity. Furthermore, the effects of Ca
2+
, Ag
+
, Mg
2+
, Cu
2+
, Co
2+
, Pb
2+
, Zn
2+
and Ni
2+
metal ions on the enzyme were studied.</description><subject>Amino acids</subject><subject>Biochemistry</subject><subject>Biological Techniques</subject><subject>Biotechnology</subject><subject>Calcium</subject><subject>Calcium ions</subject><subject>Carbon dioxide</subject><subject>Cell Biology</subject><subject>Cheese</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Cobalt</subject><subject>Copper</subject><subject>Electrophoresis</subject><subject>Enzymes</subject><subject>Gel electrophoresis</subject><subject>Human Genetics</subject><subject>Hydrolysis</subject><subject>Inositol</subject><subject>Lactobacillus</subject><subject>Lead</subject><subject>Magnesium</subject><subject>Metal ions</subject><subject>Minerals</subject><subject>Original Paper</subject><subject>Phosphates</subject><subject>Phosphohydrolase</subject><subject>Phosphorus</subject><subject>Phytase</subject><subject>Protein Science</subject><subject>Proteins</subject><subject>Purification</subject><subject>Silver</subject><subject>Sodium</subject><subject>Sodium dodecyl sulfate</subject><subject>Sodium lauryl sulfate</subject><subject>Sodium phytate</subject><subject>Substrate specificity</subject><subject>Substrates</subject><subject>Zinc</subject><issn>1073-6085</issn><issn>1559-0305</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</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>eNp1kU9v1DAQxS0Eon_gA3BBlriUQ8BjZ2LnCKvSVtqqPcDZchyb9SqJi50ctp8er1JAQurBGsvzmzdPfoS8A_YJGJOfM3AmRMVAlQNNBS_IKSC2FRMMX5Y7k6JqmMITcpbznjEOWIvX5EQwkIDQnJL9_ZKCD9bMIU7UTD39GqLdubE8DXSzM8nY2aXwuALR0_vdYTbZ0cvp8TA66lMc6bZAsTM2DMOSqY3pMAUf0xgyvbi9Bg6A4uMb8sqbIbu3T_Wc_Ph2-X1zXW3vrm42X7aVFZLPVc1773xnEE3ft8wx5a1rsVHoi-sGgXtTy1pyZG2nms42EqFv0HeIwiovzsnFqvuQ4q_F5VkXH9YNg5lcXLLmrFVSQqtYQT_8h-7jkqbi7khJVaOQqlCwUjbFnJPz-iGF0aSDBqaPQeg1CF2C0McgNJSZ90_KSze6_u_En58vAF-BXFrTT5f-rX5e9TeIqJIh</recordid><startdate>20181101</startdate><enddate>20181101</enddate><creator>Demir, 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and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153)</title><author>Demir, Yeliz ; Dikbaş, Neslihan ; Beydemir, Şükrü</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c372t-42dfefba55add90e08fce95685f0176512fa47472509b86bc6751d65fb553c8f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Amino acids</topic><topic>Biochemistry</topic><topic>Biological Techniques</topic><topic>Biotechnology</topic><topic>Calcium</topic><topic>Calcium ions</topic><topic>Carbon dioxide</topic><topic>Cell Biology</topic><topic>Cheese</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Cobalt</topic><topic>Copper</topic><topic>Electrophoresis</topic><topic>Enzymes</topic><topic>Gel electrophoresis</topic><topic>Human Genetics</topic><topic>Hydrolysis</topic><topic>Inositol</topic><topic>Lactobacillus</topic><topic>Lead</topic><topic>Magnesium</topic><topic>Metal ions</topic><topic>Minerals</topic><topic>Original Paper</topic><topic>Phosphates</topic><topic>Phosphohydrolase</topic><topic>Phosphorus</topic><topic>Phytase</topic><topic>Protein Science</topic><topic>Proteins</topic><topic>Purification</topic><topic>Silver</topic><topic>Sodium</topic><topic>Sodium dodecyl sulfate</topic><topic>Sodium lauryl sulfate</topic><topic>Sodium phytate</topic><topic>Substrate specificity</topic><topic>Substrates</topic><topic>Zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Demir, Yeliz</creatorcontrib><creatorcontrib>Dikbaş, Neslihan</creatorcontrib><creatorcontrib>Beydemir, Şükrü</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology 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Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Demir, Yeliz</au><au>Dikbaş, Neslihan</au><au>Beydemir, Şükrü</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153)</atitle><jtitle>Molecular biotechnology</jtitle><stitle>Mol Biotechnol</stitle><addtitle>Mol Biotechnol</addtitle><date>2018-11-01</date><risdate>2018</risdate><volume>60</volume><issue>11</issue><spage>783</spage><epage>790</epage><pages>783-790</pages><issn>1073-6085</issn><eissn>1559-0305</eissn><abstract>Phytase (myo-inositol hexaphosphate phosphohydrolase) belongs to phosphatases. It catalyzes the hydrolysis of phytate to less-phosphorylated inorganic phosphates and phytate. Phytase is used primarily for the feeding of simple hermit animals in order to increase the usability of amino acids, minerals, phosphorus and energy. In the present study, phytase isolation from the
Lactobacillus coryniformis
strain, isolated from Lor cheese sources, phytase purification and characterization were studied. The phytase was purified in simple three steps. The enzyme was obtained with 2.60% recovery and a specific activity of 202.25 (EU/mg protein). The molecular mass of the enzyme was determined to be 43.25 kDa with the sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method. The optimum temperature and pH for the enzyme were found as 60 °C and 5.0 and respectively. To defined the substrate specificity of the phytase, the hydrolysis of several phosphorylated compounds by the purified enzyme was studied and sodium phytate showed high specificity. Furthermore, the effects of Ca
2+
, Ag
+
, Mg
2+
, Cu
2+
, Co
2+
, Pb
2+
, Zn
2+
and Ni
2+
metal ions on the enzyme were studied.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>30171516</pmid><doi>10.1007/s12033-018-0116-1</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0003-3216-1098</orcidid></addata></record> |
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| ispartof | Molecular biotechnology, 2018-11, Vol.60 (11), p.783-790 |
| issn | 1073-6085 1559-0305 |
| language | eng |
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| source | SpringerNature Journals |
| subjects | Amino acids Biochemistry Biological Techniques Biotechnology Calcium Calcium ions Carbon dioxide Cell Biology Cheese Chemistry Chemistry and Materials Science Cobalt Copper Electrophoresis Enzymes Gel electrophoresis Human Genetics Hydrolysis Inositol Lactobacillus Lead Magnesium Metal ions Minerals Original Paper Phosphates Phosphohydrolase Phosphorus Phytase Protein Science Proteins Purification Silver Sodium Sodium dodecyl sulfate Sodium lauryl sulfate Sodium phytate Substrate specificity Substrates Zinc |
| title | Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153) |
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