Ardeshir Hesampour, Omid Ranaei, M. Malboobi, J. Harati, N. Mohandesi
{"title":"重组植酸酶在毕赤酵母和多形羊草有利甲基化营养平台上表达的生化特性比较","authors":"Ardeshir Hesampour, Omid Ranaei, M. Malboobi, J. Harati, N. Mohandesi","doi":"10.22059/PBS.2014.50309","DOIUrl":null,"url":null,"abstract":"Phytic acid is the dominant form of phosphorous in plant seeds. However, phytic acid cannot beutilized by animals and causes them serious phosphate deficiency. Utilization of phytase as ananimal feed additive can affect liberation of phosphor and its mineral availability. In this study,heterologous expression of the A. niger phyA gene was investigated in the methylotrophic yeastsP. pastoris and H.polymorpha and its expressed active recombinant phytase biochemical andbiophysical properties were studies and compared to native A.niger phytase. The phyA genesequence of A.niger was designed and expression of synthetic genes was highly successfully inactive form in both yeast hosts. Size of the secreted recombinant phytases, due to heavyglycosylation, varied from 50 to 65 KDa. Expressed extracellular recombinant phytase sampleswere purified and biochemical tests on properties demonstrated that both recombinant phytasesamples had similar pH profiles with pH optima determinations of pH 2.5, pH.5.5 as acidphosphatase and optimum temperature of 60 and 50 °C respectively in P. pastoris and H.polymorpha. This study concludes that recombinant P. pastoris and H. polymorpha phytases could fulfil aseries of predefined industrial quality criteria for application as animal feed supplement.","PeriodicalId":20726,"journal":{"name":"Progress in Biological Sciences","volume":"19 1","pages":"97-111"},"PeriodicalIF":0.0000,"publicationDate":"2014-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"9","resultStr":"{\"title\":\"COMPARISON OF BIOCHEMICAL PROPERTIES OF RECOMBINANT PHYTASE EXPRESSION IN THE FAVORABLE METHYLOTROPHIC PLATFORMS OF PICHIA PASTORIS AND HANSENULA POLYMORPHA\",\"authors\":\"Ardeshir Hesampour, Omid Ranaei, M. Malboobi, J. Harati, N. Mohandesi\",\"doi\":\"10.22059/PBS.2014.50309\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Phytic acid is the dominant form of phosphorous in plant seeds. However, phytic acid cannot beutilized by animals and causes them serious phosphate deficiency. Utilization of phytase as ananimal feed additive can affect liberation of phosphor and its mineral availability. In this study,heterologous expression of the A. niger phyA gene was investigated in the methylotrophic yeastsP. pastoris and H.polymorpha and its expressed active recombinant phytase biochemical andbiophysical properties were studies and compared to native A.niger phytase. The phyA genesequence of A.niger was designed and expression of synthetic genes was highly successfully inactive form in both yeast hosts. Size of the secreted recombinant phytases, due to heavyglycosylation, varied from 50 to 65 KDa. Expressed extracellular recombinant phytase sampleswere purified and biochemical tests on properties demonstrated that both recombinant phytasesamples had similar pH profiles with pH optima determinations of pH 2.5, pH.5.5 as acidphosphatase and optimum temperature of 60 and 50 °C respectively in P. pastoris and H.polymorpha. This study concludes that recombinant P. pastoris and H. polymorpha phytases could fulfil aseries of predefined industrial quality criteria for application as animal feed supplement.\",\"PeriodicalId\":20726,\"journal\":{\"name\":\"Progress in Biological Sciences\",\"volume\":\"19 1\",\"pages\":\"97-111\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2014-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Progress in Biological Sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.22059/PBS.2014.50309\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Progress in Biological Sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.22059/PBS.2014.50309","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
COMPARISON OF BIOCHEMICAL PROPERTIES OF RECOMBINANT PHYTASE EXPRESSION IN THE FAVORABLE METHYLOTROPHIC PLATFORMS OF PICHIA PASTORIS AND HANSENULA POLYMORPHA
Phytic acid is the dominant form of phosphorous in plant seeds. However, phytic acid cannot beutilized by animals and causes them serious phosphate deficiency. Utilization of phytase as ananimal feed additive can affect liberation of phosphor and its mineral availability. In this study,heterologous expression of the A. niger phyA gene was investigated in the methylotrophic yeastsP. pastoris and H.polymorpha and its expressed active recombinant phytase biochemical andbiophysical properties were studies and compared to native A.niger phytase. The phyA genesequence of A.niger was designed and expression of synthetic genes was highly successfully inactive form in both yeast hosts. Size of the secreted recombinant phytases, due to heavyglycosylation, varied from 50 to 65 KDa. Expressed extracellular recombinant phytase sampleswere purified and biochemical tests on properties demonstrated that both recombinant phytasesamples had similar pH profiles with pH optima determinations of pH 2.5, pH.5.5 as acidphosphatase and optimum temperature of 60 and 50 °C respectively in P. pastoris and H.polymorpha. This study concludes that recombinant P. pastoris and H. polymorpha phytases could fulfil aseries of predefined industrial quality criteria for application as animal feed supplement.