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The isoelectric point (pI) of lignin-based surfactant is an important factor in the enhancement on the enzymatic hydrolysis of lignocellulose. In this work, lignin carboxylate (LC) and quaternary ammonium lignin carboxylates (LCQ-x, x%: the mass ratio of quaternizing agent to enzymatic hydrolysis lignin) with different isoelectric points were synthesized. LC or LCQ-x with pI significantly lower or higher than 4.8 reduced the non-productive adsorption of cellulase on lignin, but for the significant inhibitory effect on cellulase activity, their enhancements on the enzymatic hydrolysis of lignocellulose were not remarkable. However, LCQ-x with pI around 4.8 preserved the cellulase activity, and significantly reduced the non-productive adsorption of cellulase, therefore remarkably enhanced the enzymatic hydrolysis. 2 g/L LC, LCQ-40 (pI = 5.0) and LCQ-100 (pI = 9.2) increased the enzymatic digestibility of pretreated eucalyptus from 35.2% to 53.4%, 95.3% and 60.4% respectively. In addition, for the excellent pH-response performance, LCQ could be efficiently recovered after enzymatic saccharification., (Copyright © 2019 Elsevier Ltd. All rights reserved.)

Some zwitterionic surfactants exhibit upper critical solution temperature (UCST) in aqueous solutions. For the zwitterionic surfactant solution mixed with cellulase, when its temperature is below UCST, the cellulase can be recovered by coprecipitation with zwitterionic surfactant. In this work, 3-(Hexadecyldimethylammonio) propanesulfonate (SB3-16) was selected to enhance the enzymatic hydrolysis of lignocelluloses and recover the cellulase. After adding 2mmol/L of SB3-16, the enzymatic digestibility of eucalyptus pretreated by dilute acid (Eu-DA) and by sulfite (Eu-SPORL) increased from 27.9% and 35.1% to 72.6% and 89.7%, respectively. The results showed that SB3-16 could reduce the non-productive adsorption of cellulase on hydrophobic interface, while it did not significantly inhibit the activity of cellulase. For the solution contained 1wt% SB3-16 and 200mg protein/L CTec2 cellulase, 55.2% of protein could be recovered by cooling. The filter paper activity of the recovered cellulase was 1.93FPU/mg protein, which was 95.8% of its initial activity., (Copyright © 2017. Published by Elsevier Ltd.)

Polyvinylpyrrolidone (PVP) is an antifouling polymer to resist the adsorption of protein on solid surface. Effects of PVP on the enzymatic hydrolysis of pretreated lignocelluloses and its mechanism were studied. Adding 1g/L of PVP8000, the enzymatic digestibility of eucalyptus pretreated by dilute acid (Eu-DA) was increased from 28.9% to 73.4%, which is stronger than the classic additives, such as PEG, Tween and bovine serum albumin. Compared with PEG4600, the adsorption of PVP8000 on lignin was larger, and the adsorption layer was more stable and hydrophilic. Therefore, PVP8000 reduced 73.1% of the cellulase non-productive adsorption on lignin and enhanced the enzymatic hydrolysis of lignocelluloses greatly., (Copyright © 2016 Elsevier Ltd. All rights reserved.)