Adsorption Kinetics of Lipase from Gibberellazeae (GZEL) and Its C-terminal Truncated Mutant to Phospholipid Monolayers [脂肪酶GZEL及其C-端截断突变体对磷脂单分子膜的吸附动力学研究]

作者：Wang F.-H.; Chen W.-C.; Wei R.-X.; Zhang H.; Yang B.; Wang Y.-H.

来源：Modern Food Science and Technology, 2019, 35(3): 26-32.

DOI：10.13982/j.mfst.1673-9078.2019.3.005

• Gibberellazeae
• Interfacial binding kinetics
• Lipase
• Monolayer technology

The adsorption kinetics of Gibberellazeae lipase (GZEL) onto different phospholipid monolayers was investigated based on monolayer technology. Meanwhile, was constructed to analyze the effect of deletion of C-terminal peptide (269-319 amino acids) on the adsorption kinetic parameters of GZEL onto various phospholipid monolayers was analyzed by the truncated mutation method. Results revealed that the adsorption kinetic parameters (adsorption constant ka, dissociation constant kd, adsorption equilibrium constant KAds) of GZEL onto different phospholipid monolayers were closely related to the type of phospholipid monolayer and initial surface pressure. Nonetheless, compared to the wild-type GZEL, a significant decrease of the adsorption constant ka and a significant increase of the dissociation constant kd towards different phospholipid monolayers were found after 269-319 peptide was deleted from GZEL. Both changes in adsorption and dissociation constants caused a significant reduction in the adsorption affinity (KAds) of the enzyme for various phospholipid monolayers. The order of preference for the wild-type GZEL for different phospholipid monolayers was: Phosphatidylserine > phosphatidylcholine > phosphatidylethanolamine. However, after the deletion of the 269-319 peptide, no significant difference was found in the affinity of the enzyme protein for the three phospholipid monolayers. The above results indicated that the 269-319 peptide played an important role in both the interfacial adsorption and selectivity of lipase GZEL to phospholipid monolayers.

• 单位
  华南理工大学