Expression and characterization of a thermostable l-aminoacylase in transgenic rice
The gene encoding a thermostable l -aminoacylase (LAA) from Deinococcus radiodurans BCRC12827 was isolated and expressed in transgenic rice under the control of a rice actin gene promoter or a seed-specific promoter, Ose705 . The recombinant LAA in the transgenic line Ose705:LAA was specifically det...
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| Veröffentlicht in: | Journal of plant biochemistry and biotechnology 2020-06, Vol.29 (2), p.336-347 |
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| creator | Kanjanaphachoat, Parawee Wang, I-Wen Hsieh, Kun-Ting Tseng, Ching-Shan Chen, Liang-Jwu |
| description | The gene encoding a thermostable
l
-aminoacylase (LAA) from
Deinococcus radiodurans
BCRC12827 was isolated and expressed in transgenic rice under the control of a rice actin gene promoter or a seed-specific promoter,
Ose705
. The recombinant LAA in the transgenic line
Ose705:LAA
was specifically detected in rice grains, but not in leaves, and its identity was confirmed by a LC/MS/MS assay. Furthermore, was efficiently purified via affinity chromatography using a nickel column. Enzymatic activity of this rice-produced LAA was determined by HPLC and a maximum activity at pH 8.0 and 45 °C in a phosphate buffer supplemented with the divalent metal ion Co
2+
using NAc-
l
-HPA as a substrate was obtained, similar to its host counterpart. This rice-produced LAA maintained approximately 50% enzyme activity after 48 h of incubation under 45 °C and maintained approximately 90% activity compared to a freshly prepared sample after being stored in rice seeds for 4 years. The present study indicated that seed-specific protein production in transgenic rice is a good and safe source for mass production of LAA, and this system can be useful for the production of other biomedical proteins as well. |
| doi_str_mv | 10.1007/s13562-019-00539-7 |
| format | Article |
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l
-aminoacylase (LAA) from
Deinococcus radiodurans
BCRC12827 was isolated and expressed in transgenic rice under the control of a rice actin gene promoter or a seed-specific promoter,
Ose705
. The recombinant LAA in the transgenic line
Ose705:LAA
was specifically detected in rice grains, but not in leaves, and its identity was confirmed by a LC/MS/MS assay. Furthermore, was efficiently purified via affinity chromatography using a nickel column. Enzymatic activity of this rice-produced LAA was determined by HPLC and a maximum activity at pH 8.0 and 45 °C in a phosphate buffer supplemented with the divalent metal ion Co
2+
using NAc-
l
-HPA as a substrate was obtained, similar to its host counterpart. This rice-produced LAA maintained approximately 50% enzyme activity after 48 h of incubation under 45 °C and maintained approximately 90% activity compared to a freshly prepared sample after being stored in rice seeds for 4 years. The present study indicated that seed-specific protein production in transgenic rice is a good and safe source for mass production of LAA, and this system can be useful for the production of other biomedical proteins as well.</description><identifier>ISSN: 0971-7811</identifier><identifier>EISSN: 0974-1275</identifier><identifier>DOI: 10.1007/s13562-019-00539-7</identifier><language>eng</language><publisher>New Delhi: Springer India</publisher><subject>Actin ; Affinity chromatography ; Agricultural production ; Aminoacylase ; Biomedical and Life Sciences ; Carbon dioxide ; Cell Biology ; Cobalt ; Column chromatography ; Enzymatic activity ; Enzyme activity ; High performance liquid chromatography ; Life Sciences ; Liquid chromatography ; Mass production ; Metal ions ; Nickel ; Original Article ; Plant Biochemistry ; Protein Science ; Proteins ; Receptors ; Rice ; Seeds ; Substrates</subject><ispartof>Journal of plant biochemistry and biotechnology, 2020-06, Vol.29 (2), p.336-347</ispartof><rights>Society for Plant Biochemistry and Biotechnology 2019</rights><rights>Society for Plant Biochemistry and Biotechnology 2019.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c270t-5aa982a8dd315b92cde60370d68eeb0388f418e0ae0593d2be8802ce604e285b3</cites><orcidid>0000-0001-7623-2738</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/s13562-019-00539-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s13562-019-00539-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Kanjanaphachoat, Parawee</creatorcontrib><creatorcontrib>Wang, I-Wen</creatorcontrib><creatorcontrib>Hsieh, Kun-Ting</creatorcontrib><creatorcontrib>Tseng, Ching-Shan</creatorcontrib><creatorcontrib>Chen, Liang-Jwu</creatorcontrib><title>Expression and characterization of a thermostable l-aminoacylase in transgenic rice</title><title>Journal of plant biochemistry and biotechnology</title><addtitle>J. Plant Biochem. Biotechnol</addtitle><description>The gene encoding a thermostable
l
-aminoacylase (LAA) from
Deinococcus radiodurans
BCRC12827 was isolated and expressed in transgenic rice under the control of a rice actin gene promoter or a seed-specific promoter,
Ose705
. The recombinant LAA in the transgenic line
Ose705:LAA
was specifically detected in rice grains, but not in leaves, and its identity was confirmed by a LC/MS/MS assay. Furthermore, was efficiently purified via affinity chromatography using a nickel column. Enzymatic activity of this rice-produced LAA was determined by HPLC and a maximum activity at pH 8.0 and 45 °C in a phosphate buffer supplemented with the divalent metal ion Co
2+
using NAc-
l
-HPA as a substrate was obtained, similar to its host counterpart. This rice-produced LAA maintained approximately 50% enzyme activity after 48 h of incubation under 45 °C and maintained approximately 90% activity compared to a freshly prepared sample after being stored in rice seeds for 4 years. The present study indicated that seed-specific protein production in transgenic rice is a good and safe source for mass production of LAA, and this system can be useful for the production of other biomedical proteins as well.</description><subject>Actin</subject><subject>Affinity chromatography</subject><subject>Agricultural production</subject><subject>Aminoacylase</subject><subject>Biomedical and Life Sciences</subject><subject>Carbon dioxide</subject><subject>Cell Biology</subject><subject>Cobalt</subject><subject>Column chromatography</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>High performance liquid chromatography</subject><subject>Life Sciences</subject><subject>Liquid chromatography</subject><subject>Mass production</subject><subject>Metal ions</subject><subject>Nickel</subject><subject>Original Article</subject><subject>Plant Biochemistry</subject><subject>Protein Science</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Rice</subject><subject>Seeds</subject><subject>Substrates</subject><issn>0971-7811</issn><issn>0974-1275</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kE1LAzEQhoMoWKt_wFPAc3SS7G6yRyn1Awoe1HOYzc62W9psTbZg_fWuXcGbpxmG530HHsauJdxKAHOXpM4LJUCWAiDXpTAnbAKlyYRUJj897lIYK-U5u0hpDZDlBrIJe51_7iKl1HaBY6i5X2FE31Nsv7D_OXYNR96vKG671GO1Ib4RuG1Dh_6wwUS8DbyPGNKSQut5bD1dsrMGN4mufueUvT_M32ZPYvHy-Dy7XwivDPQiRyytQlvXWuZVqXxNBWgDdWGJKtDWNpm0BEiQl7pWFVkLyg9QRsrmlZ6ym7F3F7uPPaXerbt9DMNLpzIwA5cVeqDUSPnYpRSpcbvYbjEenAT3I8-N8twgzx3lOTOE9BhKAxyWFP-q_0l9A2MWcqU</recordid><startdate>20200601</startdate><enddate>20200601</enddate><creator>Kanjanaphachoat, Parawee</creator><creator>Wang, I-Wen</creator><creator>Hsieh, Kun-Ting</creator><creator>Tseng, Ching-Shan</creator><creator>Chen, Liang-Jwu</creator><general>Springer India</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0001-7623-2738</orcidid></search><sort><creationdate>20200601</creationdate><title>Expression and characterization of a thermostable l-aminoacylase in transgenic rice</title><author>Kanjanaphachoat, Parawee ; Wang, I-Wen ; Hsieh, Kun-Ting ; Tseng, Ching-Shan ; Chen, Liang-Jwu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c270t-5aa982a8dd315b92cde60370d68eeb0388f418e0ae0593d2be8802ce604e285b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Actin</topic><topic>Affinity chromatography</topic><topic>Agricultural production</topic><topic>Aminoacylase</topic><topic>Biomedical and Life Sciences</topic><topic>Carbon dioxide</topic><topic>Cell Biology</topic><topic>Cobalt</topic><topic>Column chromatography</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>High performance liquid chromatography</topic><topic>Life Sciences</topic><topic>Liquid chromatography</topic><topic>Mass production</topic><topic>Metal ions</topic><topic>Nickel</topic><topic>Original Article</topic><topic>Plant Biochemistry</topic><topic>Protein Science</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Rice</topic><topic>Seeds</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kanjanaphachoat, Parawee</creatorcontrib><creatorcontrib>Wang, I-Wen</creatorcontrib><creatorcontrib>Hsieh, Kun-Ting</creatorcontrib><creatorcontrib>Tseng, Ching-Shan</creatorcontrib><creatorcontrib>Chen, Liang-Jwu</creatorcontrib><collection>CrossRef</collection><jtitle>Journal of plant biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kanjanaphachoat, Parawee</au><au>Wang, I-Wen</au><au>Hsieh, Kun-Ting</au><au>Tseng, Ching-Shan</au><au>Chen, Liang-Jwu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and characterization of a thermostable l-aminoacylase in transgenic rice</atitle><jtitle>Journal of plant biochemistry and biotechnology</jtitle><stitle>J. Plant Biochem. Biotechnol</stitle><date>2020-06-01</date><risdate>2020</risdate><volume>29</volume><issue>2</issue><spage>336</spage><epage>347</epage><pages>336-347</pages><issn>0971-7811</issn><eissn>0974-1275</eissn><abstract>The gene encoding a thermostable
l
-aminoacylase (LAA) from
Deinococcus radiodurans
BCRC12827 was isolated and expressed in transgenic rice under the control of a rice actin gene promoter or a seed-specific promoter,
Ose705
. The recombinant LAA in the transgenic line
Ose705:LAA
was specifically detected in rice grains, but not in leaves, and its identity was confirmed by a LC/MS/MS assay. Furthermore, was efficiently purified via affinity chromatography using a nickel column. Enzymatic activity of this rice-produced LAA was determined by HPLC and a maximum activity at pH 8.0 and 45 °C in a phosphate buffer supplemented with the divalent metal ion Co
2+
using NAc-
l
-HPA as a substrate was obtained, similar to its host counterpart. This rice-produced LAA maintained approximately 50% enzyme activity after 48 h of incubation under 45 °C and maintained approximately 90% activity compared to a freshly prepared sample after being stored in rice seeds for 4 years. The present study indicated that seed-specific protein production in transgenic rice is a good and safe source for mass production of LAA, and this system can be useful for the production of other biomedical proteins as well.</abstract><cop>New Delhi</cop><pub>Springer India</pub><doi>10.1007/s13562-019-00539-7</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0001-7623-2738</orcidid></addata></record> |
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| source | Springer Nature - Complete Springer Journals |
| subjects | Actin Affinity chromatography Agricultural production Aminoacylase Biomedical and Life Sciences Carbon dioxide Cell Biology Cobalt Column chromatography Enzymatic activity Enzyme activity High performance liquid chromatography Life Sciences Liquid chromatography Mass production Metal ions Nickel Original Article Plant Biochemistry Protein Science Proteins Receptors Rice Seeds Substrates |
| title | Expression and characterization of a thermostable l-aminoacylase in transgenic rice |
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