LAUSR

How to improve the accessibility of immobilized cellulase to insoluble cellulose and recover immobilized enzyme from remaining insoluble substrate is a challenge to the efficient hydrolysis of cellulose into glucose. The objective of this work is to solve the problems mentioned above by the immobilization of cellulase onto poly(methacrylamide-co-acrylic acid) (PMAAc), developing a reversibly soluble–insoluble biocatalyst with upper critical solution temperature (UCST) of 16 °C. The as-prepared PMAAc–cellulase with a new UCST of 19 °C exhibited significantly improved pH, temperature, storage, and operation stabilities compared with that of free catalyst, and about 82.4% of its original activity was retained even after ten cycles. Cellulase systems containing endo-β-1,4-glucanase (EG), cellobiohydrolase (CBH), and β-glucosidase (β-G) are coimmobilized at an optimum ratio on PMAAc by adjusting the additive amount of β-G, which can obtain higher hydrolysis efficiency. It was found that the coimmobilization of...