Recent Research on Lipase Immobilization with Multipoint Covalent Treatment by Glutaraldehyde

Immobilized lipase has played an essential role in the chemical and biological sciences as a viable alternative to standard chemical catalysts. Glutaraldehyde is a low-cost crosslinking agent at risk of being superseded by developing crosslinking compounds with biocompatible, biodegradable, and non-toxic characteristics. The multipoint covalent treatment method using glutaraldehyde has both advantages and disadvantages. Immobilization techniques can be improved to improve the overall performance of immobilized lipase. The most recent update on lipase immobilization with multipoint covalent treatment by glutaraldehyde was summarized in this review. Covalent binding lipase on pre-activated support and aggregation-crosslinking lipase into crosslinked enzyme aggregates (CLEAs) or adsorption-crosslinking lipase on support are the most common immobilization techniques. Based on the above technologies, the advancement trends in important domains, such as the advancement of supports, additives, reactors, and cross-linking agents, are summarized. In addition, the application of the improved immobilized lipase by glutaraldehyde in the production of fatty acids, glycerides, biodiesel, and drug precursors was reviewed. In view of this, we put forward further studies on multipoint covalent treatment in lipase immobilization with glutaraldehyde. Various analytical methods are required to provide additional information about the structure of glutaraldehyde and its crosslinked products for assisting the proper immobilization conditions. Applying the composite strategy can also bring new opportunities for improving the efficiency of biological catalysts