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Stability and activity of cellulase modified with polyethylene glycol (PEG) at different amino groups in the ionic liquid [C2OHmim][OAc]

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ABSTRACT Polyethylene glycol (PEG), as a suitable tool to improve enzyme stability, such as monomethoxyl-polyethylene glycol aldehyde (mPEG-ALD) and monomethoxyl-polyethylene glycol succinimide (mPEG-SPA), has been appended at the ε-amino group… Click to show full abstract

ABSTRACT Polyethylene glycol (PEG), as a suitable tool to improve enzyme stability, such as monomethoxyl-polyethylene glycol aldehyde (mPEG-ALD) and monomethoxyl-polyethylene glycol succinimide (mPEG-SPA), has been appended at the ε-amino group of lysine or the N-terminal α-amino acid residue of commercial cellulase. The modified cellulases thus obtained are designated as Cell-ALD and Cell-SPA, respectively. The stabilities and activities of these modified cellulases have been studied in the ionic liquid [C2OHmim][OAc]. Cell-ALD showed excellent stability and activity in [C2OHmim][OAc], such as the activity of Cell-ALD 5k (molecular weight of ALD is 5000), which can reach above 80% of its original value after remaining in [C2OHmim][OAc] for 24 h, and outstanding performance in the hydrolysis of natural cellulose.

Keywords: stability; amino; glycol peg; polyethylene glycol; c2ohmim oac; activity

Journal Title: Chemical Engineering Communications
Year Published: 2018

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