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- W2182884364 abstract "α-Amylases hydrolyze the α-1,4-glycosidic bond in starch results in maltose and oligosacharides. The enzyme has been widely used in various industries, such as starch liquefaction, textile, brewing, baking, detergent, and paper industries. To improve secretory production of S. fibuligera �-amylase in Pichia pastoris , in this research the signal peptide of S. fibuligera α-amylase was genetically engineered with modified signal peptide (MS). MS was designed to contain the pro region of the signal peptide of Saccharomyces cerevisieae α-mating factor fused to 15 residue amino acid of mouse salivary α-amylase signal peptide to replace the wild type signal peptide of α-amylase. Modification of signal peptide was done using a set of primers 5’MSP αF and 3’ALPIApa by PCR (Polymerase Chain Reaction ) method and pPICZ αA-ALPI as the template. The resulted 1,7 kb DNA fragment of MSALP1 was subcloned into pGemT plasmid and subsequently into pPICZA expression vector. Restriction and DNA sequence analysis showed that signal peptide of S. fibuligera α-amylase has been successfully modified and pPICZA-MS ALPI has been successfully constructed. Qualitative analysis of α-amylase shown that P. pastoris transformants which contain recombinant α-amylase, secreted α-amylase into growth medium indicated by clear zone on YPD medium containing 1% starch-KI/I 2." @default.
- W2182884364 created "2016-06-24" @default.
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- W2182884364 date "2008-01-01" @default.
- W2182884364 modified "2023-09-27" @default.
- W2182884364 title "Signal peptide modification of α-amylase Gene ( ALPI ) and construction of pPICZA-MS ALPI plasmid for improving secretory production of α α α α-amilase in Pichia pastoris" @default.
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