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DESSY NATALIA
Faculty of Mathematics and Science, Institut Teknologi bandung, Jalan Ganesha 10, Bandung 40132, West Java, Indonesia
Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Immunology & microbiology Medicine & Pharmacology

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Enzymatic Characterization of Recombinant Cyclodextrin Glycosyltransferase from Bacillus sp. a2-5a using Sagoo Starch as Substrate RINA IMANIAR; CATUR RIANI; DESSY NATALIA; DEBBIE SOFFIE RETNONINGRUM
Microbiology Indonesia Vol. 6 No. 3 (2012): September 2012
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (485.698 KB) | DOI: 10.5454/mi.6.3.5

Abstract

Cyclodextrin (CD) is a cyclic oligosaccharide molecule and depending on the number of glucose molecules, three types of CDs are commonly used, α-CD, β-CD, and γ-CD. CDs can be produced enzymatically using starch as substrate catalyzed by CD glycosyltransferase (CGTase). In current research, recombinant CGTase production from the synthetic gene was optimized for its production using three growth media and two induction temperatures. The highest yield was obtained in Luria Bertani medium at 25 °C. The rCGTase protein was affinity purified as a 76.39 kDa protein which showed α-cyclization and starch hydrolysis activities using zymography method. The optimum temperature, pH and incubation time was 55 °C, 6, and 24 h, respectively. The enzyme was stable at a wide pHs in the range of 5-10, retained its half activity at 56 °C for 30 min and had cyclization ratio for α-CD : β-CD : γ-CD was 4 : 81 : 15. An amount of 542 mg β-cyclodextrin was produced from 100 mL reaction of 1% (b/v) sagoo starch using 38.4 μg rCGTase in optimum condition. This work reports for the first time the character of rCGTase from Bacillus sp. A2-5a using sagoo starch as a substrate.
Combination of Genetic Manipulation Improved Saccharomycopsis fibuligera α-Amylase Secretion by Pichia pastoris Shabarni Gaffar; Dessy Natalia; Toto Subroto; Oo Suprijana; Soetijoso Soemitro
Indonesian Journal of Chemistry Vol 19, No 2 (2019)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (558.321 KB) | DOI: 10.22146/ijc.33140

Abstract

This study assessed the combinations of genetic manipulation; signal peptide modification, gene dosage increment and co-expression of folding component, to increase Saccharomycopsis fibuligera R64 α-amylase (Sfamy) secretion in Pichia pastoris. Sfamy native signal peptide was replaced with modified signal peptide which contained 15 amino acid of mouse salivary α-amylase signal peptide fused to the pro-region of the signal peptide of Saccharomyces cerevisiae α-mating factor (α-MF). Increase in gene dosage was identified by screening for P. pastoris harboring multicopies of the Sfamy gene. Whereas, co-expression of folding component was done by addition of Protein Disulfide Isomerase (PDI). Expression plasmids harboring Sfamy containing modified signal sequence (pPICZA-MS-Sfamy) was used to transform P. pastoris GS115, and gene dosage increment was screened using zeocin. Effect of PDI co-expression on secretion levels of Sfamy was assessed by constructing the pPIC3.5K-Pdi1 plasmid and introducing into P. pastoris harboring multicopies of MS-Sfamy for expression of Sfamy. Signal peptide modification consequently increased Sfamy secretion by P. pastoris by 3.3-fold compared to native signal peptide. Gene dosage increment had improved Sfamy secretion by 11-fold in P. pastoris [MS-Sfamy] resistant to 2000 μg/mL zeocin, compared to P. pastoris harboring one copy of WT-Sfamy. Hence, PDI co-expression increased the secretion of Sfamy by 2-fold as compared without PDI co-expression. In summary, the combination of genetic manipulation successfully increased Sfamy secretion by 20-fold compared to P. pastoris harboring one copy of WT-Sfamy.
Co-Authors DEBBIE SOFFIE RETNONINGRUM Oo Suprijana Riani, Catur RINA IMANIAR Shabarni Gaffar Soetijoso Soemitro Toto Subroto