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.… Click to show full abstract
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...
               
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