N-terminal PEGylated cellulase: a high stability enzyme in 1-butyl-3-methylimidazolium chloride

Literature Information

Publication Date 2013-03-22
DOI 10.1039/C3GC40104A
Impact Factor 10.182
Authors

Lu Li, Juan Xie, Shitao Yu, Zhongliang Su, Shiwei Liu, Fusheng Liu, Congxia Xie, Baoquan Zhang, Chenggang Zhang


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Abstract

A new approach to improve cellulase stability in 1-butyl-3-methylimidazolium chloride ([Bmim][Cl]), based on covalently binding the N-terminal α-amino acid residue of commercial cellulase to mPEG-ALD (monomethoxyl-polyethylene glycol aldehyde), is proposed. N-terminal PEGylated cellulase (Cell-ALD) was obtained by using mPEG-ALD as a modifier and by controlling the reaction pH in the range of 4–5. The stability of Cell-ALD was first studied in different concentrations of [Bmim][Cl] at 50 °C and 80 °C. The thermal stability of Cell-ALD was obviously enhanced, and was affected by the molecular weight of mPEG-ALD and the degree of modification (DM). mPEG-ALD 5k (an average molecular weight of 5000 Daltons) increased the stability of the enzyme at 50 °C by more than 30 times compared with the unmodified cellulase in 25% [Bmim][Cl] which behaves as a powerful enzyme deactivating agent. Thus, a stabilized Cell-ALD has been successfully used for the saccharification of dissolved cellulose in [Bmim][Cl] (i.e. up to 95% hydrolysis in 24 h) at 50 °C.

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