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Tytuł:
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Charge-oriented strategies of tunable substrate affinity based on cellulase and biomass for improving in situ saccharification: A review.
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Autorzy:
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Zhou Z; College of Chemistry and Life Science, Suzhou University of Science and Technology, Suzhou 215009, PR China.
Ju X; College of Chemistry and Life Science, Suzhou University of Science and Technology, Suzhou 215009, PR China.
Chen J; College of Chemistry and Life Science, Suzhou University of Science and Technology, Suzhou 215009, PR China.
Wang R; College of Chemistry and Life Science, Suzhou University of Science and Technology, Suzhou 215009, PR China.
Zhong Y; College of Chemistry and Life Science, Suzhou University of Science and Technology, Suzhou 215009, PR China.
Li L; College of Chemistry and Life Science, Suzhou University of Science and Technology, Suzhou 215009, PR China. Electronic address: .
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Źródło:
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Bioresource technology [Bioresour Technol] 2021 Jan; Vol. 319, pp. 124159. Date of Electronic Publication: 2020 Sep 24.
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Typ publikacji:
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Journal Article; Review
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Język:
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English
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Imprint Name(s):
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Original Publication: Barking, Essex, England : New York, N.Y. : Elsevier Applied Science ; Elsevier Science Pub. Co., 1991-
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MeSH Terms:
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Cellulase*
Biomass ; Cellulose ; Hydrolysis ; Lignin
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Contributed Indexing:
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Keywords: Cellulase; Immobilization; In situ saccharification; Lignocellulosic biomass; Surface charge
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Substance Nomenclature:
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9004-34-6 (Cellulose)
9005-53-2 (Lignin)
EC 3.2.1.4 (Cellulase)
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Entry Date(s):
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Date Created: 20201003 Date Completed: 20201125 Latest Revision: 20201125
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Update Code:
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20240105
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DOI:
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10.1016/j.biortech.2020.124159
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PMID:
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33010717
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The intrinsic recalcitrance of lignocellulosic biomass makes it resistant to enzymatic hydrolysis. The electron-rich surface of the lignin and cellulose-alike structure of hemicellulose competitively absorb the cellulase. Thus, modifying the surface charge on biomass components to alter cellulase affinity is an urgent requisite. Developing charge tunable cellulase will alter substrate affinity. Also, charge-based immobilization generates controllable substrate affinity. Within immobilized cellulase involved in situ biomass saccharification, charge effects made a crucial contribution. In addition to affecting the interaction between immobilized cellulase and biomass, charge exerts an impact on cellulase to immobilize the materials, further investigation is essential. This study aims to review the charge effects on the cellulase affinity in biomass saccharification, strategies of charge tunable cellulase, and immobilized cellulase, thereby explaining the role of electrostatic interaction. In terms of electrostatic behavior, the pathways and plans to improve in situ biomass saccharification seem to be promising.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)