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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2021.12
- 수록면
- 1 - 10 (10page)
- DOI
- 10.1186/s42649-021-00066-7
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Our previous study on the binding activity between Cel5H and clay minerals showed highest binding efficiency among other cellulase enzymes cloned. Here, based on previous studies, we hypothesized that the positive amino acids on the surface of Cel5H protein may play an important role in binding to clay surfaces. To examine this, protein sequences of Bacillus licheniformis Cel5H ( Bl Cel5H) and Paenibacillus polymyxa Cel5A ( Pp Cel5A) were analyzed and then selected amino acids were mutated. These mutated proteins were investigated for binding activity and force measurement via atomic force microscopy (AFM). A total of seven amino acids which are only present in Bl Cel5H but not in Pp Cel5A were selected for mutational studies and the positive residues which are present in both were omitted. Of the seven selected surface lysine residues, only three mutants K196A(M2), K54A(M3) and K157T(M4) showed 12%, 7% and 8% less clay mineral binding ability, respectively compared with wild-type. The probable reason why other mutants did not show altered binding efficiency might be due to relative location of amino acids on the protein surface. Meanwhile, measurement of adhesion forces on mica sheets showed a well-defined maximum at 69?±?19 pN for wild-type, 58?±?19 pN for M2, 53?±?19 pN for M3, and 49?±?19 pN for M4 proteins. Hence, our results demonstrated that relative location of surface amino acids of Cel5H protein especially positive charged amino acids are important in the process of clay mineral-protein binding interaction through electrostatic exchange of charges.
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참고문헌 (40)
참고문헌 신청
M. R. Barnes / 2004 / Bioinformatics for geneticists / Wiley
M.H. Baron / 1999 / Chymotrypsin Adsorption on Montmorillonite: Enzymatic Activity and Kinetic FTIR Structural Analysis / Journal of Colloid and Interface Science 214(2):319~332
Kavitha Bharatham / 2008 / Binding mode analyses and pharmacophore model development for sulfonamide chalcone derivatives, a new class of α-glucosidase inhibitors / Journal of Molecular Graphics and Modelling 26(8):1202~1212
Nagakumar Bharatham / 2007 / Pharmacophore identification and virtual screening for methionyl-tRNA synthetase inhibitors / Journal of Molecular Graphics and Modelling 25(6):813~823
R.G. Burns / Enzymes in the environment, activity, ecology, and applications
M.H. Baron / 1999 / Chymotrypsin Adsorption on Montmorillonite: Enzymatic Activity and Kinetic FTIR Structural Analysis / Journal of Colloid and Interface Science 214(2):319~332
Kavitha Bharatham / 2008 / Binding mode analyses and pharmacophore model development for sulfonamide chalcone derivatives, a new class of α-glucosidase inhibitors / Journal of Molecular Graphics and Modelling 26(8):1202~1212
Nagakumar Bharatham / 2007 / Pharmacophore identification and virtual screening for methionyl-tRNA synthetase inhibitors / Journal of Molecular Graphics and Modelling 25(6):813~823
R.G. Burns / Enzymes in the environment, activity, ecology, and applications
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