Association of amphipathic lignin derivatives with cellobiohydrolase groups improves enzymatic saccharification of lignocellulosics

Yamamoto, Yoko; Cheng, Ningning; Koda, Keiichi; Igarashi, Kiyohiko; Tamai, Yutaka; Uraki, Yasumitsu

Association of amphipathic lignin derivatives with cellobiohydrolase groups improves enzymatic saccharification of lignocellulosics

Yamamoto, Yoko; Cheng, Ningning; Koda, Keiichi et al.

Cellulose, 2017, 24(4), 1849-1862

Permalink : https://hdl.handle.net/2115/68678

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論文情報

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アクセス権	open access
URI	https://hdl.handle.net/2115/68678
タイトル	Association of amphipathic lignin derivatives with cellobiohydrolase groups improves enzymatic saccharification of lignocellulosics
著者	Yamamoto, Yoko ; Cheng, Ningning ; Koda, Keiichi ; Igarashi, Kiyohiko ; Tamai, Yutaka ; Uraki, Yasumitsu
著者名 Yamamoto, Yoko
著者名 Cheng, Ningning
e-Rad_Researcher 80322840 著者名 Koda, Keiichi
著者名 Igarashi, Kiyohiko
e-Rad_Researcher 50281796 著者名 Tamai, Yutaka
e-Rad_Researcher 90193961 著者名 Uraki, Yasumitsu
言語	英語
キーワード	Amphipathic lignin derivative
	Aggregation
	Cellulase
	Enzymatic saccharification
	Surface plasmon resonance
発行日	2017-04
出版者	Springer
収録物名	Cellulose
巻(号)	24(4)
ページ	1849-1862
抄録	Amphipathic lignin derivatives (ALDs), prepared from hardwood acetic acid lignin and softwood soda lignin via coupling with a mono-epoxylated polyethylene glycol, have been reported to improve the enzymatic saccharification efficiency of lignocellulose while maintaining significant residual cellulase activity after saccharification. We previously demonstrated that the effect of ALDs was caused by a direct interaction between ALDs and Cel6A (or CBH II). In this study, a different ALD was prepared from softwood kraft lignin in addition to aforementioned ALDs. The interactions between all the ALDs and the enzymes other than Cel6A, such as Cel7A and Cel7B, in a cellulase cocktail were investigated using surface plasmon resonance. The kraft lignin-based ALD showed the highest residual cellulase activity among all ALDs and an improved cellulolytic enzyme efficiency similar to those of the other ALDs. All ALDs were found to directly associate with major enzymes in the cellulase cocktail, Cel6A and Cel7A (or CBH I), but not with Cel7B (or EG I). In addition, the ALDs showed a much higher affinity to amino groups than to hydroxy and carboxy groups. In contrast, polyethylene glycol (molecular mass 4000 Da), one part of the ALD and a previously reported enzymatic saccharification enhancer, did not adsorb onto any enzymes in the cellulase cocktail or the amino group. Size exclusion chromatography demonstrated that the ALDs formed self-aggregates in both water and chloroform; the formation process in the latter was especially unique. Therefore, we conclude that the high residual cellulase activity is attributed to the direct association of ALD aggregates with the CBH group.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	The final publication is available at Springer via doi:10.1007/s10570-017-1214-0
PISSN	0969-0239
EISSN	1572-882X
NCID	AA11006365
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1007/s10570-017-1214-0