Dual-Enzyme Metal Hybrid Crystal for Direct Transformation of Whey Lactose into a High-Value Rare Sugar D-Tagatose: Synthesis, Characterization, and a Sustainable Process.

Abstract

A dual-enzyme metal-organic hybrid crystal was constructed through self-assembling of manganese phosphate embedded with β-galactosidase and L-arabinose isomerase for facile synthesis of rare sugar D-tagatose. The synthesized crystal-like hierarchical system (MnHC@β-Gal+L-AI) was extensively characterized for structural features and catalytic reactions. The results indicated that upon immobilization onto the hybrid crystal, the activity of β-galactosidase and L-arabinose iomerase was enhanced by a factor of 1.6- and 1.5-fold, respectively. The developed MnHC@β-Gal+L-AI exhibited excellent efficiency with a net equilibrium level conversion of low-cost substrate whey lactose (100%) into D-glucose (∼50%), D-galactose (∼25%), and D-tagatose (∼25%). In addition, the fabricated hybrid crystals displayed cofactor regeneration ability. Therefore, the developed hybrid system was observed to be efficiently reused more than 5 times in a batch level conversion. Hence, the developed dual-enzyme-based hybrid crystal provides a platform for direct transformation of whey lactose into rare sugar D-tagatose.