Overexpression of a fungal β-mannanase from Bispora sp. MEY-1 in maize seeds and enzyme characterization

Mannans and heteromannans are widespread in plants cell walls and are well-known as anti-nutritional factors in animal feed. To remove these factors, it is common practice to incorporate endo-β-mannanase into feed for efficient nutrition absorption. The objective of this study was to overexpress a β...

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Veröffentlicht in:PloS one 2013-02, Vol.8 (2), p.e56146-e56146
Hauptverfasser: Xu, Xiaolu, Zhang, Yuhong, Meng, Qingchang, Meng, Kun, Zhang, Wei, Zhou, Xiaojin, Luo, Huiying, Chen, Rumei, Yang, Peilong, Yao, Bin
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container_title PloS one
container_volume 8
creator Xu, Xiaolu
Zhang, Yuhong
Meng, Qingchang
Meng, Kun
Zhang, Wei
Zhou, Xiaojin
Luo, Huiying
Chen, Rumei
Yang, Peilong
Yao, Bin
description Mannans and heteromannans are widespread in plants cell walls and are well-known as anti-nutritional factors in animal feed. To remove these factors, it is common practice to incorporate endo-β-mannanase into feed for efficient nutrition absorption. The objective of this study was to overexpress a β-mannanase gene directly in maize, the main ingredient of animal feed, to simplify the process of feed production. The man5A gene encoding an excellent β-mannanase from acidophilic Bispora sp. MEY-1 was selected for heterologous overexpression. Expression of the modified gene (man5As) was driven by the embryo-specific promoter ZM-leg1A, and the transgene was transferred to three generations by backcrossing with commercial inbred Zheng58. Its exogenous integration into the maize embryonic genome and tissue specific expression in seeds were confirmed by PCR and Southern blot and Western blot analysis, respectively. Transgenic plants at BC3 generation showed agronomic traits statistically similar to Zheng58 except for less plant height (154.0 cm vs 158.3 cm). The expression level of MAN5AS reached up to 26,860 units per kilogram of maize seeds. Compared with its counterpart produced in Pichia pastoris, seed-derived MAN5AS had higher temperature optimum (90°C), and remained more β-mannanase activities after pelleting at 80°C, 100°C or 120°C. This study shows the genetically stable overexpression of a fungal β-mannanase in maize and offers an effective and economic approach for transgene containment in maize for direct utilization without any purification or supplementation procedures.
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MEY-1 in maize seeds and enzyme characterization</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Public Library of Science (PLoS)</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Xu, Xiaolu ; Zhang, Yuhong ; Meng, Qingchang ; Meng, Kun ; Zhang, Wei ; Zhou, Xiaojin ; Luo, Huiying ; Chen, Rumei ; Yang, Peilong ; Yao, Bin</creator><contributor>Li, Yi</contributor><creatorcontrib>Xu, Xiaolu ; Zhang, Yuhong ; Meng, Qingchang ; Meng, Kun ; Zhang, Wei ; Zhou, Xiaojin ; Luo, Huiying ; Chen, Rumei ; Yang, Peilong ; Yao, Bin ; Li, Yi</creatorcontrib><description>Mannans and heteromannans are widespread in plants cell walls and are well-known as anti-nutritional factors in animal feed. To remove these factors, it is common practice to incorporate endo-β-mannanase into feed for efficient nutrition absorption. The objective of this study was to overexpress a β-mannanase gene directly in maize, the main ingredient of animal feed, to simplify the process of feed production. The man5A gene encoding an excellent β-mannanase from acidophilic Bispora sp. MEY-1 was selected for heterologous overexpression. Expression of the modified gene (man5As) was driven by the embryo-specific promoter ZM-leg1A, and the transgene was transferred to three generations by backcrossing with commercial inbred Zheng58. Its exogenous integration into the maize embryonic genome and tissue specific expression in seeds were confirmed by PCR and Southern blot and Western blot analysis, respectively. Transgenic plants at BC3 generation showed agronomic traits statistically similar to Zheng58 except for less plant height (154.0 cm vs 158.3 cm). The expression level of MAN5AS reached up to 26,860 units per kilogram of maize seeds. Compared with its counterpart produced in Pichia pastoris, seed-derived MAN5AS had higher temperature optimum (90°C), and remained more β-mannanase activities after pelleting at 80°C, 100°C or 120°C. This study shows the genetically stable overexpression of a fungal β-mannanase in maize and offers an effective and economic approach for transgene containment in maize for direct utilization without any purification or supplementation procedures.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0056146</identifier><identifier>PMID: 23409143</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Agriculture ; Agronomy ; Animal Feed ; Ascomycota - enzymology ; Ascomycota - genetics ; beta-Mannosidase - genetics ; beta-Mannosidase - metabolism ; Biology ; Biotechnology ; Cell walls ; Containment ; Corn ; Embryos ; Enzyme Activation ; Enzyme Stability ; Enzymes ; Feed additives ; Feeds ; Food additives ; Fungi ; Gene Expression ; Genetic Vectors - genetics ; Genomes ; Genomics ; Inbreeding ; Laboratories ; Mannanases ; Nutrition ; Pelleting ; Phenotype ; Pichia - genetics ; Pichia pastoris ; Purification ; Regeneration ; Seeds ; Seeds - genetics ; Seeds - physiology ; Tobacco ; Transformation, Genetic ; Transgenic plants ; Yeast ; Zea mays ; Zea mays - genetics ; Zea mays - physiology</subject><ispartof>PloS one, 2013-02, Vol.8 (2), p.e56146-e56146</ispartof><rights>2013 Xu et al. 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MEY-1 in maize seeds and enzyme characterization</title><author>Xu, Xiaolu ; Zhang, Yuhong ; Meng, Qingchang ; Meng, Kun ; Zhang, Wei ; Zhou, Xiaojin ; Luo, Huiying ; Chen, Rumei ; Yang, Peilong ; Yao, Bin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-8ad586b416395dabaea7114585acec2711bcd848e69adc61eb582031e1216c963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Agriculture</topic><topic>Agronomy</topic><topic>Animal Feed</topic><topic>Ascomycota - enzymology</topic><topic>Ascomycota - genetics</topic><topic>beta-Mannosidase - genetics</topic><topic>beta-Mannosidase - metabolism</topic><topic>Biology</topic><topic>Biotechnology</topic><topic>Cell walls</topic><topic>Containment</topic><topic>Corn</topic><topic>Embryos</topic><topic>Enzyme Activation</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Feed additives</topic><topic>Feeds</topic><topic>Food additives</topic><topic>Fungi</topic><topic>Gene Expression</topic><topic>Genetic Vectors - genetics</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Inbreeding</topic><topic>Laboratories</topic><topic>Mannanases</topic><topic>Nutrition</topic><topic>Pelleting</topic><topic>Phenotype</topic><topic>Pichia - genetics</topic><topic>Pichia pastoris</topic><topic>Purification</topic><topic>Regeneration</topic><topic>Seeds</topic><topic>Seeds - genetics</topic><topic>Seeds - physiology</topic><topic>Tobacco</topic><topic>Transformation, Genetic</topic><topic>Transgenic plants</topic><topic>Yeast</topic><topic>Zea mays</topic><topic>Zea mays - genetics</topic><topic>Zea mays - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xu, Xiaolu</creatorcontrib><creatorcontrib>Zhang, Yuhong</creatorcontrib><creatorcontrib>Meng, Qingchang</creatorcontrib><creatorcontrib>Meng, Kun</creatorcontrib><creatorcontrib>Zhang, Wei</creatorcontrib><creatorcontrib>Zhou, Xiaojin</creatorcontrib><creatorcontrib>Luo, Huiying</creatorcontrib><creatorcontrib>Chen, Rumei</creatorcontrib><creatorcontrib>Yang, Peilong</creatorcontrib><creatorcontrib>Yao, Bin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing &amp; 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MEY-1 in maize seeds and enzyme characterization</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-02-11</date><risdate>2013</risdate><volume>8</volume><issue>2</issue><spage>e56146</spage><epage>e56146</epage><pages>e56146-e56146</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Mannans and heteromannans are widespread in plants cell walls and are well-known as anti-nutritional factors in animal feed. To remove these factors, it is common practice to incorporate endo-β-mannanase into feed for efficient nutrition absorption. The objective of this study was to overexpress a β-mannanase gene directly in maize, the main ingredient of animal feed, to simplify the process of feed production. The man5A gene encoding an excellent β-mannanase from acidophilic Bispora sp. MEY-1 was selected for heterologous overexpression. Expression of the modified gene (man5As) was driven by the embryo-specific promoter ZM-leg1A, and the transgene was transferred to three generations by backcrossing with commercial inbred Zheng58. Its exogenous integration into the maize embryonic genome and tissue specific expression in seeds were confirmed by PCR and Southern blot and Western blot analysis, respectively. Transgenic plants at BC3 generation showed agronomic traits statistically similar to Zheng58 except for less plant height (154.0 cm vs 158.3 cm). The expression level of MAN5AS reached up to 26,860 units per kilogram of maize seeds. Compared with its counterpart produced in Pichia pastoris, seed-derived MAN5AS had higher temperature optimum (90°C), and remained more β-mannanase activities after pelleting at 80°C, 100°C or 120°C. This study shows the genetically stable overexpression of a fungal β-mannanase in maize and offers an effective and economic approach for transgene containment in maize for direct utilization without any purification or supplementation procedures.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23409143</pmid><doi>10.1371/journal.pone.0056146</doi><oa>free_for_read</oa></addata></record>
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subjects Agriculture
Agronomy
Animal Feed
Ascomycota - enzymology
Ascomycota - genetics
beta-Mannosidase - genetics
beta-Mannosidase - metabolism
Biology
Biotechnology
Cell walls
Containment
Corn
Embryos
Enzyme Activation
Enzyme Stability
Enzymes
Feed additives
Feeds
Food additives
Fungi
Gene Expression
Genetic Vectors - genetics
Genomes
Genomics
Inbreeding
Laboratories
Mannanases
Nutrition
Pelleting
Phenotype
Pichia - genetics
Pichia pastoris
Purification
Regeneration
Seeds
Seeds - genetics
Seeds - physiology
Tobacco
Transformation, Genetic
Transgenic plants
Yeast
Zea mays
Zea mays - genetics
Zea mays - physiology
title Overexpression of a fungal β-mannanase from Bispora sp. MEY-1 in maize seeds and enzyme characterization
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