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To understand the superior hydrolytic activity after polymorphic conversion from cellulose I to II from the adsorption behaviors of enzymes

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Abstract

The role of the cellulose ultrastructure on the relationship between cellulase binding and activity is not clear yet. In this article, a quartz crystal microbalance with dissipation (QCM-D) was employed to monitor the interactions between a given cellulase and the cellulose substrates with varied polymorphs of pure cellulose I and II and the intermediate state (I/II). Initially, cellulose nanocrystals (CNCs) with polymorphs of cellulose I, I/II and II were prepared and spin-coated on QCM sensors. The cellulose substrates’ crystallinity degree was examined by XRD, and morphology was detected by AFM. Then, a commercial cellulase from Trichoderma reesei was used to test the adsorption and hydrolysis of cellulose substrates with polymorphs of I, I/II and II, respectively. The results revealed that in the enzyme adsorption and desorption process at a temperature of 15 °C, CNC-II had the lowest adsorption capacity with a total adsorption mass of 179 ng cm−2 but the highest reversible binding ratio of 33.7%; for comparison, the values were 235 ng cm−2 versus 25.6% and 207 ng cm−2 versus 26.9% for CNC-I and -I/II, respectively. And the conformation of adlayers on CNC-I, -I/II and -II derived from the QCM data became softer and softer in turn. On the other hand, CNC-II exhibited the best enzymatic hydrolytic ability among three substrates when enzymatic hydrolysis experiments were conducted at 45 °C. The results indicated that polymorphic conversion from I to II changes the affinity between the enzyme and cellulose surface; CNC-II has the lowest affinity to the enzyme, but the softer conformation of the adsorbed enzyme layer, and the more reversible adsorption may facilitate its hydrolytic activity. This article gives a perspective from the adsorption dynamics and conformation of the adsorbed enzyme layer, helping to understand the superior hydrolytic activity of cellulose with polymorph II. Thus, there is a potential of polymorphic conversion in the reduction of enzyme dosage and cost in the enzymatic hydrolysis process.

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Acknowledgments

This project was financially supported by the National Natural Science Foundation of China (nos. 31270613, 31470593, 31370571), Six Talent Projects (2015-JNHB-013) and Qing-Lan Projects in Jiangsu Province, and the Priority Academic Program Development of Jiangsu Higher Education Institutions.

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Correspondence to Junlong Song.

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Jin, E., Zhang, Y., Hu, F. et al. To understand the superior hydrolytic activity after polymorphic conversion from cellulose I to II from the adsorption behaviors of enzymes. Cellulose 24, 1371–1381 (2017). https://doi.org/10.1007/s10570-016-1183-8

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  • DOI: https://doi.org/10.1007/s10570-016-1183-8

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