Boosting Hydrolysis of Cellulose at High Temperature by β‐Glucosidase Induced Metal–Organic Framework In‐Situ Co‐Precipitation Encapsulation. Issue 21 (26th September 2022)

• Record Type: Journal Article
• Authors: Jiao, Rui; Pang, Yuxia; Yang, Dongjie; Li, Zhixian; Lou, Hongming
• Is Part Of: ChemSusChem. Volume 15:Issue 21(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-09-26
• Subjects: β-Glucosidase -- Enzymatic hydrolysis -- High temperature catalysis -- Ionic liquid -- Metal–organic framework; Green chemistry -- Periodicals; Sustainable engineering -- Periodicals; Chemistry -- Periodicals; Chemical engineering -- Periodicals; 660
• DOI: 10.1002/cssc.202201354
• Languages: English
• ISSNs: 1864-5631

Abstract

Abstract: Due to the poor enzyme thermal stability, the efficient conversion of high crystallinity cellulose into glucose in aqueous phase over 50 °C is challenging. Herein, an enzyme‐induced MOFs encapsulation of β‐glucosidase (β‐G) strategy was proposed for the first time. By using various methods, including SEM, XRD, XPS, NMR, FTIR and BET, the successful preparation of a porous channel‐type flower‐like enzyme complex (β‐G@MOFs) was confirmed. The prepared enzyme complex (β‐G@MOFs) materials showed improved thermal stability (from 50 °C to 100 °C in the aqueous phase) and excellent resistance to ionic liquids (the reaction temperature was as high as 110 °C) compared to the free enzyme (β‐G). Not only the catalytic hydrolysis of cellulose by single enzyme (β‐G) in ionic liquid was realized, but also the high‐temperature continuous reaction performance of the enzyme was significantly improved. Benefiting from the significantly improved heat resistance, the β‐G@MOFs exhibited 32.1 times and 34.2 times higher enzymatic hydrolysis rate compared to β‐G for cellobiose and cellulose substrates, respectively. Besides, the catalytic activity of β‐G@MOFs was retained up to 86 % after five cycles at 110 °C. This was remarkable because the fixation of the enzyme by the MOFs ensured that the folded structure of the enzyme would not expand at high temperatures, allowing the native conformation of the encapsulated protein well‐maintained. Furthermore, we believe that this structural stability was caused by the confinement of flower‐like porous MOFs. Abstract : Enzyme‐MOF bouquet : A novel strategy was reported to construct an enzyme complex with flower‐like porous channels by enzyme‐induced encapsulation method. The encapsulation of MOF and its unique morphology endowed β‐G@MOF(PABA) with remarkably enhanced synergistic catalysis ability (exhibited 32.1 times and 34.2 times higher enzymatic hydrolysis rate compared to free enzyme, respectively) and good cycling stability.