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• W2598889053 abstract "Recombinant chimeric α-amylase (Ba-Gt-amy) has been produced extracellularly in P. pastoris under AOX promoter. Clones of P. pastoris with multiple gene copies have been generated by multiple transformations and Post-Transformational Vector Amplification (PTVA), which led to 10.7-fold enhancement in α-amylase titre as compared to a clone with a copy of the gene. The recombinant P. pastoris integrated 8 copies of Ba-Gt-amy in the genome of P. pastoris, as revealed by real time PCR data analysis. Heterologous protein expression as well as mRNA level of Ba-Gt-amy was higher in multi-copy clone than that with single copy. The pure Ba-Gt-amy expressed in P. pastoris is a glycoprotein of 75 kDa, which is optimally active at pH 4.0 and 60 °C with T1/2 of 40 min at 70 °C. The Kinetic parameters and end product analysis suggested that glycosylation has no effect on catalytic properties of Ba-Gt-amy. The enzyme saccharifies soluble as well as raw starches efficiently and generates maltose and maltooligosaccharides, thus, useful in baking and sugar syrup industries. The strategy for generating multi-copy clones is being reported for the first time, which could be useful in enhancing the production of other recombinant proteins." @default.
• W2598889053 created "2017-04-07" @default.
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• W2598889053 date "2017-03-22" @default.
• W2598889053 modified "2023-09-27" @default.
• W2598889053 title "Production of Chimeric Acidic α-Amylase by the Recombinant Pichia pastoris and Its Applications" @default.
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• W2598889053 doi "https://doi.org/10.3389/fmicb.2017.00493" @default.
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