A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity.
about
Engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency.A novel bifunctional acetyl xylan esterase/arabinofuranosidase from Penicillium chrysogenum P33 enhances enzymatic hydrolysis of lignocellulose.The GH51 α-l-arabinofuranosidase from Paenibacillus sp. THS1 is multifunctional, hydrolyzing main-chain and side-chain glycosidic bonds in heteroxylans.Synergistic hydrolysis of xylan using novel xylanases, β-xylosidases, and an α-L-arabinofuranosidase from Geobacillus thermodenitrificans NG80-2.
P2860
A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年学术文章
@wuu
2015年学术文章
@zh-cn
2015年学术文章
@zh-hans
2015年学术文章
@zh-my
2015年学术文章
@zh-sg
2015年學術文章
@yue
2015年學術文章
@zh
2015年學術文章
@zh-hant
name
A novel bifunctional GH51 exo- ...... nt biomass-degrading capacity.
@ast
A novel bifunctional GH51 exo- ...... nt biomass-degrading capacity.
@en
type
label
A novel bifunctional GH51 exo- ...... nt biomass-degrading capacity.
@ast
A novel bifunctional GH51 exo- ...... nt biomass-degrading capacity.
@en
prefLabel
A novel bifunctional GH51 exo- ...... nt biomass-degrading capacity.
@ast
A novel bifunctional GH51 exo- ...... nt biomass-degrading capacity.
@en
P2093
P2860
P1476
A novel bifunctional GH51 exo- ...... nt biomass-degrading capacity.
@en
P2093
Huiying Luo
Huoqing Huang
Peilong Yang
Pengjun Shi
Wenxia Yang
Yingguo Bai
P2860
P2888
P356
10.1186/S13068-015-0366-0
P577
2015-11-30T00:00:00Z
P5875
P6179
1046893517