2012
DOI: 10.1007/s00253-012-4001-8
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Codon-optimized glucoamylase sGAI of Aspergillus awamori improves starch utilization in an industrial yeast

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Cited by 40 publications
(39 citation statements)
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“…18,19 This approach has been recently assessed for the first time by integrating a glucoamylase gene into an industrial S. cerevisiae yeast, resulting in a promising and improvable CBP amylolytic yeast, capable of efficiently converting raw starch into ethanol. 20 To achieve this purpose, several fungal strains of Aspergillus oryzae and A. awamori, screened for their efficient raw and soluble starch hydrolyzing activities, showed high amylolytic activities in liquid assays (data not shown). A. awamori CBS 115.52 was found to be a promising raw starch degrader and the cDNA copy of the glucoamylase gene GAI was amplified by PCR for expression in the laboratory strain S. cerevisiae Y294.…”
Section: Onsolidated Bioprocessing (Cbp)mentioning
confidence: 99%
“…18,19 This approach has been recently assessed for the first time by integrating a glucoamylase gene into an industrial S. cerevisiae yeast, resulting in a promising and improvable CBP amylolytic yeast, capable of efficiently converting raw starch into ethanol. 20 To achieve this purpose, several fungal strains of Aspergillus oryzae and A. awamori, screened for their efficient raw and soluble starch hydrolyzing activities, showed high amylolytic activities in liquid assays (data not shown). A. awamori CBS 115.52 was found to be a promising raw starch degrader and the cDNA copy of the glucoamylase gene GAI was amplified by PCR for expression in the laboratory strain S. cerevisiae Y294.…”
Section: Onsolidated Bioprocessing (Cbp)mentioning
confidence: 99%
“…In order to implement the large scale ethanol production from raw starch, the development of an industrial yeast http that converts starch to ethanol in one step (called consolidated bioprocessing -CBP) is needed [8][9][10][11].…”
Section: Introductionmentioning
confidence: 99%
“…In the previous studies, it has been reported that codon optimization could significantly improve the enzyme expression level and enhance the corresponding enzyme activity (Huang et al 2007;Favaro et al 2012). The KSDD enzyme activity expressed in B. subtilis was at a low level (≤1Á75 U mg À1 ) in the previous studies (Li et al 2007;Zhang et al 2013), which was possibly due to the codon preference of B. subtilis which was different from that of actinobacteria.…”
Section: Discussionmentioning
confidence: 92%
“…; Favaro et al . ). The KSDD enzyme activity expressed in B. subtilis was at a low level (≤1·75 U mg −1 ) in the previous studies (Li et al .…”
Section: Discussionmentioning
confidence: 97%