Chitin biopolymer mediates self-sufficient biocatalyst of pyridoxal 5′-phosphate and L-lysine decarboxylase

Abstract

Enzyme cofactors are essential in biocatalysis for many enzymes. However, their high commercial cost limits the industrial application of cofactor-dependent enzymes. We overcame this challenge by constructing a self-sufficient biocatalyst that co-immobilised pyridoxal 5′-phosphate (PLP) and L-lysine decarboxylase (LDC) using natural polymer chitin as the functional material. First, degree of deacetylation (DDA) of chitin was regulated to enhance PLP adsorption and immobilisation. Then, the enzyme was immobilised via fusion of a chitin-binding domain. Chitin with 36% DDA efficiently co-immobilised LDC and PLP. Laser scanning confocal microscope and scanning electron microscope proved that the LDC and PLP were immobilised on the chitin. The self-sufficient biocatalyst retained over 55% of its original activity after five cycles. The proposed strategy provides a new way to achieve co-immobilisation of PLP-dependent enzymes.