Table 5.
Properties of lipase variants generated by lid and hinge region modification.
| Enzyme | Mutants | Mutants description | Mutants property | Reference |
|---|---|---|---|---|
| Proteus sp. LipK107 | E130L + K131I | The hydrophobicity of the lid domain increases | The eep (%) and E on the resolution of racemic 1-phenylethanol increased by 1.36 and 137.6%, respectively | Gao et al. (2011) |
| T138V | The eep (%) and E on the resolution of racemic 1-phenylethanol increased by 0.52 and 30.6%, respectively | |||
| Rhizopus chinensis lipase S4-3 | S4-3M | The lid of S4-3 was swapped with ferulic acid esterase from Aspergillus niger | Specific activity toward short-chain substrates increased by 7.2-fold (C3) and 38.0-fold (C2), respectively | Yu et al. (2014) |
| S4-3N | The lid of S4-3 was swapped with Rhizomucor miehei lipase | Specific activity toward substrates (C2, C6, C8, C12, and C16) increased by 1.5- to 3.3-fold and reduced 40% toward tristearin (C18) | ||
| Candida rugosa lipase (CRL) Trx-LIP4 | CRL4LID1 | The lid of CRL4 was swapped with CRL1 | Hydrolytic activity decreased by 85%, changed CLP, and reduced enantioselectivity | Akoh et al. (2004) |
| CRL LIP1 | CRL1LID3 | The lid of CRL1 was swapped with CRL3 | Specific activity toward cholesterol esters increased by 200-fold, enantioselectivity and activity reduced in organic solvent | Akoh et al. (2004) |
| Candida antarctica lipase B (CALB) | CALB-N. crassa | The lid of CALB was swapped with CALB homolog from Neurospora crassa lipase | Hydrolytic activity increased on simple esters, specifically, substrates with Ca branching on the carboxylic side, and increased enantioselectivity in hydrolysis of racemic ethyl 2-phenylpropanoate (E > 50) | Skjot et al. (2009) |
| CALB-G. zeae | The lid of CALB was swapped with CALB homologs from Gibberella zeae lipase | |||
| Penicillium expansum lipase (PEL) | T66L + D70N | The mutant residues are located at the lid (D70N) and the lid hinge region (T66L, E83K) of PEL | Specific activity toward p-nitrophenyl palmitate increased by 136.4-fold | Tang et al. (2015) |
| E83K | Specific activity toward p-nitrophenyl butyrate increased by 136.4-fold, but lack interfacial activation | |||
| A. niger lipase (ANL) | S84G | The mutant residues are located at the lid hinge region of ANL | Specific activity toward p-nitrophenyl esters decreased and displayed a pronounced interfacial activation | Shu et al. (2011) |
| D99P | Specific activity toward p-nitrophenyl palmitate increased by 2.2-fold and displayed no interfacial activation | |||
| R. chinensis lipase | F95C + F214C | A disulfide bridge was introduced into the lipase from R. chinensis in the hinge region of the lid | The half-life t1/2 value increased by 11-fold at 60°C and the Tm increase by 7°C, but the catalytic efficiency toward pNPP decreased by 1.5-fold | Yu et al. (2012) |