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Tracing cellulase components in hydrolyzate during the enzymatic hydrolysis of corncob residue and its analysis
- Cai, Cheng, Jin, Yu, Pang, Yuxia, Ke, Qia, Qiu, Wenhui, Qiu, Xueqing, Qin, Yanlin, Lou, Hongming
- Bioresource technology reports 2018 v.4 pp. 137-144
- adsorption, beta-glucosidase, cellulose, cellulose 1,4-beta-cellobiosidase, corn cobs, endo-1,4-beta-glucanase, enzymatic hydrolysis, hydrolysates, hydrolysis, hydrophobic bonding, hydrophobicity, lignin, polyacrylamide gel electrophoresis, xylanases
- Cellulase components in hydrolyzate were accurately traced by SDS-PAGE gel electrophoresis during the enzymatic hydrolysis of corncob residual (CCR) and delignified CCR (CCR-DL). After a quick initial adsorption on substrates, cellulase in hydrolyzate remained stable for CCR, but showed an obvious increasing trend for CCR-DL. It indicated that lignin in CCR was the main factor for the loss of cellulase in hydrolyzate. During CCR's hydrolysis, β‑glucosidase, xylanase, endoglucanase III (EGIII) and EGV were rapidly adsorbed on lignin and weren't released in subsequent, however, cellobiohydrolase I (CBHI), CBHII, EGI and EGIV were mainly adsorbed on cellulose in the early stage. With the hydrolysis of substrate, cellulase on cellulose would be released into hydrolyzate, but cellulase in hydrolyzate gradually became hydrophobic and much easier to be adsorb on lignin by the increasing hydrophobic interaction. These two factors dominated the change of cellulase concentration in hydrolyzate in the later stage of CCR's hydrolysis.