Immobilization and catalytic properties of candida lipolytic lipase on surface of organic intercalated and modified MgAl-LDHs

• Organic part in LDHs improves immobilization efficiency and activity of lipase.
• Positive charge in LDHs is found to be beneficial to enzyme immobilization.
• The immobilized enzyme has a wider pH range and a better thermostability in reaction.

In this study, MgAl-LDHs (layered double hydroxides) intercalated with sodium dodecyl sulfate and outside surface modified with (3-aminopropyl)triethoxysilane (KH550) were prepared. The existence of organic part in LDHs improved immobilization efficiency and activity recovery of candida lipolytic lipase loaded. Also the positive charge in framework of LDHs was found to be beneficial to the enzyme immobilization. An immobilization efficiency of 56.4% and an activity recovery over 69.2% of the enzyme were obtained after it was loaded on the intercalated and modified LDHs, and catalytic activity of the immobilization can be kept at least five times. Moreover, the immobilized enzyme was found to have higher temperature resistance, wider pH value and better thermostability in reactive activity.

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