select ad.sno,ad.journal,ad.title,ad.author_names,ad.abstract,ad.abstractlink,j.j_name,vi.* from articles_data ad left join journals j on j.journal=ad.journal left join vol_issues vi on vi.issue_id_en=ad.issue_id where ad.sno_en='12190' and ad.lang_id='5' and j.lang_id='5' and vi.lang_id='5' Engineering of A Lipase towards Thermostability: Studies on | 12190
Progrès en génie génétique

Progrès en génie génétique
Libre accès

ISSN: 2169-0111

Abstrait

Engineering of A Lipase towards Thermostability: Studies on Additive Effect of the two Thermo-Stabilising Mutations at Protein Surface

Rakesh K, Nisha C, Ranvir S, Pushpender KS, Jagdeep K*

In this study we have showed combined effect of two single point mutations S311C (LipR2) and R214C (LipR3) on the protein stability and overall change in biochemical properties. We found that both of these mutations are near the surface and individually enhanced the thermal stability of the protein (T1/2 for S311C=4.5 h & R214C=7 h at 60°C). But, their combined effect was not additive on thermostability. T1/2 of double mutant (LipR2 + LipR3) was 4 h at 60°C. Circular dichroism (CD) and fluorescence studies also supported our findings. Homology modelling studies demonstrated that in double mutant (LipR4) side chain of Cys311 is protruding towards the bulk solvent and is easily available for oxidation of sulfahydril group. This might be the reason for its low thermostability as compared to LipR3. We also observed that, side chains of Cys 214 didn’t changed. Here, one of the Cystein (Cys311) is behaving like a hydrophilic residue while the other (Cys 214) is behaving like hydrophobic residue.

Keywords:

Lipase; Thermostability; Mutations; Enzyme; Nucleotide sequence

Introductio

Clause de non-responsabilité: Ce résumé a été traduit à l'aide d'outils d'intelligence artificielle et n'a pas encore été révisé ou vérifié.
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