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CONSTRUCTION AND EXPRESSION
OF QUARTET RECOMBINANT PEPTIDE SURFACTANT FOR EOR APPLICATION Cut Nanda Sari; Usman Usman; Refiana Lestary; Riesa Khairunnisa W.R.; Leni Herlina; Syafrizal Syafrizal; Tati Kristianti; Sony Suhandono
Scientific Contributions Oil and Gas Vol 39 No 3 (2016)
Publisher : Testing Center for Oil and Gas LEMIGAS

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.29017/SCOG.39.3.98

Abstract

The main drawback of the SUPEL peptide surfactant product which has been developed for EOR application is it isunstable at a high temperature. This research is aimed at generating the prototype of peptide surfactant construction in recombinant by stringing up 4 SUPEL linier sequences. Quartet recombinant technology can produce the peptide surfactant characterized as reversible biosurfactant, which is active at high temperature but inactive at low temperature. Multiple SUPEL Construction (MSC) that was developed in this research is using synthetic DNA and producing SUPEL in 4 sequences that can flip at normal temperature and can open when heated. SDS PAGE analysis results show that MSC construction can be expressed by inducting IPTG and cell harvested at 90°C. This research proves that construction and expression of the SUPEL quartet has been achieved by producing the peptide at an ideal size.
IN SILICO POTENTIAL ANALYSIS OF X6D MODEL OF PEPTIDE SURFACTANT FOR ENHANCED OIL RECOVERY Cut Nanda Sari; Usman Usman; Rukman Hertadi; Tegar Nurwahyu Wijaya; Leni Herlina; Ken Sawitri Suliandari; Syafrizal Syafrizal; Onie Kristiawan
Scientific Contributions Oil and Gas Vol 39 No 2 (2016)
Publisher : Testing Center for Oil and Gas LEMIGAS

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.29017/SCOG.39.2.107

Abstract

Peptides and their derivatives can be applied in enhanced oil recovery (EOR) due to their ability to form an emulsion with hydrophobic molecules. However, peptide research for EOR application, either theoretical or computational studies, is still limited. The purpose of this research is to analyse the potency of the X6D model of surfactant peptide for EOR by molecular dynamics simulations in oil-water interface. Molecular dynamics simulation using GROMACS Software with Martini force field can assess a peptide’s ability for self-assembly and emulsification on a microscopic scale. Molecular dynamics simulations combined with coarse grained models will give information about the dynamics of peptide molecules in oil-water interface and the calculation of interfacial tension value. Four designs of X6D model: F6D, L6D, V6D, and I6D are simulated on the oil-water interface. The value of interfacial tension from simulation show the trend of F6D L6D > I6D > V6D. The results indicate that V6D has the greatest reduction in interfacial tension and has the stability until 90°C with the salinity of at least 1M NaCl.