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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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posted on 2018-03-12, 13:55 authored by Li Lu, Yan Jieshan, Yu Shitao, Liu Shiwei, Liu Fusheng, Xie Congxia

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.

Funding

This study was supported by the National Natural Science Foundation of China (31670594), the National Natural Science Foundation of Shandong Province (ZR2015BM007), the Program for Taishan Scholars (ts 201511033), and the China Scholarship Council (201607890001).

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