High-level production of yeast (Schwanniomyces occidentalis) phytase in transgenic rice plants by a combination of signal sequence and codon modification of the phytase gene
Summary This study was designed to produce yeast (Schwanniomyces occidentalis) phytase in rice with a view to future applications in the animal feed industry. To achieve high‐level production, chimeric genes with the secretory signal sequence of the rice chitinase‐3 gene were constructed using eithe...
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| Published in | Plant Biotechnology Journal Vol. 3; no. 1; pp. 43 - 55 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
Blackwell Science Ltd
01.01.2005
Wiley |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Summary
This study was designed to produce yeast (Schwanniomyces occidentalis) phytase in rice with a view to future applications in the animal feed industry. To achieve high‐level production, chimeric genes with the secretory signal sequence of the rice chitinase‐3 gene were constructed using either the original full‐length or N‐truncated yeast phytase gene, or a modified gene whose codon usage was changed to be more similar to that of rice, and then introduced into rice (Oryza sativa L.). When the original phytase genes were used, the phytase activity in the leaves of transgenic rice was of the same level as in wild‐type plants, whose mean value was 0.039 U/g fresh weight (g‐FW) (1 U of activity was defined as 1 µmol P released per min at 37 °C). In contrast, the enzyme activity was increased markedly when codon‐modified phytase genes were introduced: up to 4.6 U/g‐FW of leaves for full‐length codon‐modified phytase, and 10.6 U/g‐FW for truncated codon‐modified phytase. A decrease in the optimum temperature and thermal stability was observed in the truncated heterologous enzyme, suggesting that the N‐terminal region plays an important role in enzymatic properties. In contrast, the optimum temperature and pH of full‐length heterologous phytase were indistinguishable from those of the benchmark yeast phytase, although the heterologous enzyme was less glycosylated. Full‐length heterologous phytase in leaf extract showed extreme stability. These results indicate that codon modification, combined with the use of a secretory signal sequence, can be used to produce substantial amounts of yeast phytase, and possibly any phytases from various organisms, in an active and stable form. |
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| AbstractList | This study was designed to produce yeast (Schwanniomyces occidentalis) phytase in rice with a view to future applications in the animal feed industry. To achieve high-level production, chimeric genes with the secretory signal sequence of the rice chitinase-3 gene were constructed using either the original full-length or N-truncated yeast phytase gene, or a modified gene whose codon usage was changed to be more similar to that of rice, and then introduced into rice (Oryza sativa L.). When the original phytase genes were used, the phytase activity in the leaves of transgenic rice was of the same level as in wild-type plants, whose mean value was 0.039 U/g fresh weight (g-FW) (1 U of activity was defined as 1 micromol P released per min at 37 degrees C). In contrast, the enzyme activity was increased markedly when codon-modified phytase genes were introduced: up to 4.6 U/g-FW of leaves for full-length codon-modified phytase, and 10.6 U/g-FW for truncated codon-modified phytase. A decrease in the optimum temperature and thermal stability was observed in the truncated heterologous enzyme, suggesting that the N-terminal region plays an important role in enzymatic properties. In contrast, the optimum temperature and pH of full-length heterologous phytase were indistinguishable from those of the benchmark yeast phytase, although the heterologous enzyme was less glycosylated. Full-length heterologous phytase in leaf extract showed extreme stability. These results indicate that codon modification, combined with the use of a secretory signal sequence, can be used to produce substantial amounts of yeast phytase, and possibly any phytases from various organisms, in an active and stable form. This study was designed to produce yeast ( Schwanniomyces occidentalis ) phytase in rice with a view to future applications in the animal feed industry. To achieve high‐level production, chimeric genes with the secretory signal sequence of the rice chitinase‐3 gene were constructed using either the original full‐length or N‐truncated yeast phytase gene, or a modified gene whose codon usage was changed to be more similar to that of rice, and then introduced into rice ( Oryza sativa L.). When the original phytase genes were used, the phytase activity in the leaves of transgenic rice was of the same level as in wild‐type plants, whose mean value was 0.039 U/g fresh weight (g‐FW) (1 U of activity was defined as 1 µmol P released per min at 37 °C). In contrast, the enzyme activity was increased markedly when codon‐modified phytase genes were introduced: up to 4.6 U/g‐FW of leaves for full‐length codon‐modified phytase, and 10.6 U/g‐FW for truncated codon‐modified phytase. A decrease in the optimum temperature and thermal stability was observed in the truncated heterologous enzyme, suggesting that the N‐terminal region plays an important role in enzymatic properties. In contrast, the optimum temperature and pH of full‐length heterologous phytase were indistinguishable from those of the benchmark yeast phytase, although the heterologous enzyme was less glycosylated. Full‐length heterologous phytase in leaf extract showed extreme stability. These results indicate that codon modification, combined with the use of a secretory signal sequence, can be used to produce substantial amounts of yeast phytase, and possibly any phytases from various organisms, in an active and stable form. Summary This study was designed to produce yeast (Schwanniomyces occidentalis) phytase in rice with a view to future applications in the animal feed industry. To achieve high‐level production, chimeric genes with the secretory signal sequence of the rice chitinase‐3 gene were constructed using either the original full‐length or N‐truncated yeast phytase gene, or a modified gene whose codon usage was changed to be more similar to that of rice, and then introduced into rice (Oryza sativa L.). When the original phytase genes were used, the phytase activity in the leaves of transgenic rice was of the same level as in wild‐type plants, whose mean value was 0.039 U/g fresh weight (g‐FW) (1 U of activity was defined as 1 µmol P released per min at 37 °C). In contrast, the enzyme activity was increased markedly when codon‐modified phytase genes were introduced: up to 4.6 U/g‐FW of leaves for full‐length codon‐modified phytase, and 10.6 U/g‐FW for truncated codon‐modified phytase. A decrease in the optimum temperature and thermal stability was observed in the truncated heterologous enzyme, suggesting that the N‐terminal region plays an important role in enzymatic properties. In contrast, the optimum temperature and pH of full‐length heterologous phytase were indistinguishable from those of the benchmark yeast phytase, although the heterologous enzyme was less glycosylated. Full‐length heterologous phytase in leaf extract showed extreme stability. These results indicate that codon modification, combined with the use of a secretory signal sequence, can be used to produce substantial amounts of yeast phytase, and possibly any phytases from various organisms, in an active and stable form. This study was designed to produce yeast (Schwanniomyces occidentalis) phytase in rice with a view to future applications in the animal feed industry. To achieve high-level production, chimeric genes with the secretory signal sequence of the rice chitinase-3 gene were constructed using either the original full-length or N-truncated yeast phytase gene, or a modified gene whose codon usage was changed to be more similar to that of rice, and then introduced into rice (Oryza sativa L.). When the original phytase genes were used, the phytase activity in the leaves of transgenic rice was of the same level as in wild-type plants, whose mean value was 0.039 U/g fresh weight (g-FW) (1 U of activity was defined as 1 micromol P released per min at 37 degrees C). In contrast, the enzyme activity was increased markedly when codon-modified phytase genes were introduced: up to 4.6 U/g-FW of leaves for full-length codon-modified phytase, and 10.6 U/g-FW for truncated codon-modified phytase. A decrease in the optimum temperature and thermal stability was observed in the truncated heterologous enzyme, suggesting that the N-terminal region plays an important role in enzymatic properties. In contrast, the optimum temperature and pH of full-length heterologous phytase were indistinguishable from those of the benchmark yeast phytase, although the heterologous enzyme was less glycosylated. Full-length heterologous phytase in leaf extract showed extreme stability. These results indicate that codon modification, combined with the use of a secretory signal sequence, can be used to produce substantial amounts of yeast phytase, and possibly any phytases from various organisms, in an active and stable form.This study was designed to produce yeast (Schwanniomyces occidentalis) phytase in rice with a view to future applications in the animal feed industry. To achieve high-level production, chimeric genes with the secretory signal sequence of the rice chitinase-3 gene were constructed using either the original full-length or N-truncated yeast phytase gene, or a modified gene whose codon usage was changed to be more similar to that of rice, and then introduced into rice (Oryza sativa L.). When the original phytase genes were used, the phytase activity in the leaves of transgenic rice was of the same level as in wild-type plants, whose mean value was 0.039 U/g fresh weight (g-FW) (1 U of activity was defined as 1 micromol P released per min at 37 degrees C). In contrast, the enzyme activity was increased markedly when codon-modified phytase genes were introduced: up to 4.6 U/g-FW of leaves for full-length codon-modified phytase, and 10.6 U/g-FW for truncated codon-modified phytase. A decrease in the optimum temperature and thermal stability was observed in the truncated heterologous enzyme, suggesting that the N-terminal region plays an important role in enzymatic properties. In contrast, the optimum temperature and pH of full-length heterologous phytase were indistinguishable from those of the benchmark yeast phytase, although the heterologous enzyme was less glycosylated. Full-length heterologous phytase in leaf extract showed extreme stability. These results indicate that codon modification, combined with the use of a secretory signal sequence, can be used to produce substantial amounts of yeast phytase, and possibly any phytases from various organisms, in an active and stable form. |
| Author | Ohnishi, Naoto Harada, Michiko Nikumaru, Seiya Honda, Hideo Yamaguchi, Ken-ichi Hamada, Akira |
| Author_xml | – sequence: 1 givenname: Akira surname: Hamada fullname: Hamada, Akira organization: Functional Chemicals Laboratory, Mitsui Chemicals, Inc., Togo 1144, Mobara 297-0017 Japan – sequence: 2 givenname: Ken-ichi surname: Yamaguchi fullname: Yamaguchi, Ken-ichi organization: Functional Chemicals Laboratory, Mitsui Chemicals, Inc., Togo 1144, Mobara 297-0017 Japan – sequence: 3 givenname: Naoto surname: Ohnishi fullname: Ohnishi, Naoto organization: Functional Chemicals Laboratory, Mitsui Chemicals, Inc., Togo 1144, Mobara 297-0017 Japan – sequence: 4 givenname: Michiko surname: Harada fullname: Harada, Michiko organization: Functional Chemicals Laboratory, Mitsui Chemicals, Inc., Togo 1144, Mobara 297-0017 Japan – sequence: 5 givenname: Seiya surname: Nikumaru fullname: Nikumaru, Seiya organization: Functional Chemicals Laboratory, Mitsui Chemicals, Inc., Togo 1144, Mobara 297-0017 Japan – sequence: 6 givenname: Hideo surname: Honda fullname: Honda, Hideo email: hideo.honda@mitsui-chem.co.jp organization: Functional Chemicals Laboratory, Mitsui Chemicals, Inc., Togo 1144, Mobara 297-0017 Japan |
| BackLink | https://cir.nii.ac.jp/crid/1870302168149256320$$DView record in CiNii https://www.ncbi.nlm.nih.gov/pubmed/17168898$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.5938/youton.25.166 10.1080/713609297 10.1016/0271-5317(95)00040-P 10.1002/j.1460-2075.1991.tb07705.x 10.1104/pp.114.3.1103 10.1093/oxfordjournals.pcp.a078092 10.1038/81132 10.1046/j.1365-313X.1994.6020271.x 10.1038/nbt1093-1151 10.1007/BF02524753 10.1006/bbrc.1999.1501 10.1016/S0065-2164(00)47004-8 10.1007/s001220051659 10.1007/BF00280194 10.1016/S1360-1385(01)02222-1 10.1016/0003-2697(81)90168-8 10.5511/plantbiotechnology1984.2.74 10.1006/bbrc.2002.6361 10.1006/abbi.1999.1115 10.1093/jxb/49.326.1463 10.1023/A:1006012005654 10.1046/j.1365-313x.2001.00998.x 10.1016/S0014-5793(00)02106-2 10.1104/pp.109.4.1199 10.1023/A:1009690730620 10.1111/j.1399-3054.1989.tb06187.x 10.1038/nbt0793-811 10.1016/S0014-5793(01)02488-7 10.1007/s002530100795 10.1007/s004250000282 10.1111/j.1432-1033.1991.tb16166.x 10.1016/S0006-291X(03)01002-7 10.1111/j.1462-5822.2007.00901.x |
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| Notes | ArticleID:PBI098 istex:7C00731AD5102A0BFAD9B0C892947C98CDF15E43 ark:/67375/WNG-202NSGL5-G Laboratory for Sustainable Horticulture, Minami Kyushu University, Hibarigaoka, Takanabe‐cho, Miyazaki 884‐0003, Japan Present address ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
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This study was designed to produce yeast (Schwanniomyces occidentalis) phytase in rice with a view to future applications in the animal feed industry.... This study was designed to produce yeast ( Schwanniomyces occidentalis ) phytase in rice with a view to future applications in the animal feed industry. To... This study was designed to produce yeast (Schwanniomyces occidentalis) phytase in rice with a view to future applications in the animal feed industry. To... |
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| SubjectTerms | codon modification heterologous expression phytase phytate transgenic rice yeast |
| Title | High-level production of yeast (Schwanniomyces occidentalis) phytase in transgenic rice plants by a combination of signal sequence and codon modification of the phytase gene |
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