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Dian Andriani
Research Center for Biotechnology, Indonesian Institute of Sciences (LIPI)

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Screening for Natural Producers Capable of Producing 1,3-Propanediol from Glycerol Dian Andriani; Wien Kusharyoto; Bambang Prasetya; Thomas Willke; Klaus Dieter Vorlop
Annales Bogorienses Vol. 14 No. 1 (2010): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2010.v14.n1.19-24

Abstract

Glycerol is a renewable resource found as the main by-product in the transesterification of triglycerides and fat saponification. Due to the increased production of plant oils, especially palm oil in developing countries, and their larger use by the oleochemical industry, glycerol surpluses are on the world market and this may result in a decrease in glycerol price. As a consequence, biotechnological processes have been developed to convert this substrate into value-added products, such as 1,3-propanediol (1,3-PD). The microbial production of 1,3-PD could be competitive to chemical routes assuming that it is based on cheap raw material and an optimised process. In the screening for 1,3 PD–producing bacteria, raw glycerol as by-product from rapeseed oil processing unit was used as a carbon source compared with commercial glycerol. By using increasing concentration of both glycerols from 50 to 150 g/l, two potential bacteria were obtained from soil samples. BMP-1 was obtained from an enrichment culture using 50 g/l commercial glycerol, while BMR-1 was obtained from an enrichment culture using 100 g/l raw glycerol. The highest conversion yield obtained using the isolate BMP-1 was around 0.62 g 1,3-PD formed per mol glycerol consumed, and 0.73 mol 1,3-PD formed per mol glycerol using the isolate BMR-1. No bacteria were obtained from cultures using 150 g/l commercial and raw glycerol, respectively, which indicated that higher concentration of glycerol has inhibition effect. 
Expression of an Anti-Transferrin Receptor Antibody scFV Fragment in Escherichia coli Using A L-Rhamnose-Based Tightly Regulated Promoter System Dian Andriani; Ira Handayani; Wien Kusharyoto
Annales Bogorienses Vol. 16 No. 2 (2012): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2012.v16.n2.1-6

Abstract

Transferrin receptor (TfR) levels are elevated in various types of cancer cells and correlate with the aggressive or proliferative ability of tumor cells. Therefore, TfR levels are considered useful as a prognostic tumor marker, and TfR is a potential target for drug delivery in therapy of malignant cells. In such kind of targeted delivery system, antibody fragments are frequently used as targeting moiety. Here, we report the generation of an anti-TfR single-chain antibody variable (scFv). The cDNA encoding the variable heavy and light chain domains of the scFv antibody fragment was derived from the anti-TfR monoclonal antibody LUCA31. The gene encoding the anti-TfR scFv fragment was codon optimized for expression in Escherichia coli, subsequently synthesized, and cloned into the pJExpress-804 Rhamex vector. The expression vector utilizes the E. coli rhaB promoter and corresponding regulatory genes, and is tightly regulated by the presence of L-L-rhamnose, it is also tightly regulated in the absence of L-L-rhamnose by the addition of D-glucose The His6-tagged anti-TfR scFv fragment was expressed in E. coli NiCo21 and purified by means of immobilized metal chelate affinity chromatography on TALON™ matrix. In SDS-PAGE, a single band corresponding to a molecular mass of approximately 30 kDa was observed which corresponded to the predicted molecular mass based on the amino acid sequence.
Generation of mCherryBody: an Anti-Transferrin Receptor Antibody Variable Fragment Linked by The Fluorescent Protein mCherry Wien Kusharyoto; Dian Andriani; Ira Handayani
Annales Bogorienses Vol. 20 No. 2 (2016): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2016.v20.n2.55-62

Abstract

A facile generation of a recombinant antibody fragment with intrinsic fluorescent properties of the monomeric mCherry fluorescent protein is described. The so-called mCherryBody was designed based on the structure model of the variable fragment of anti-transferrin receptor antibody LUCA31 and the X-ray crystallographic structure of the mCherry protein. mCherryBody was constructed to retain optimal spatial geometry between the C- and N-termini of the antibody light-chain (VL) and heavy-chain (VH) by mimicking the domains interface pairing in antibody Fab fragments and incorporation of the mCherry fluorescent protein as a bridging scaffold. The gene encoding the chimeric protein was cloned into the pJExpress414 expression vector, expressed and secreted into the periplasm of Escherichia coli NiCo21(DE3) for assembly and disulphide bond formation. Based on its amino acid sequence, mCherryBody was predicted to have a molecular weight of 51.46 kDa. The modular assembly used in the generation of mCherryBody may permit the interchange of binding sites and of fluorescent proteins to create robust panels of coloured antibody fragments. Thus, the mCherryBody platform facilitates rapid generation of colored single-chain variable fragment (scFv) chimeras that could be used for screening of antibodies against cell surface markers or receptors.
Co-Authors Bambang Prasetya Ira Handayani Klaus Dieter Vorlop Thomas Willke Wien Kusharyoto