title: Improving lignocellulose degradation using xylanase-cellulase fusion protein with a glycine-serine linker.
abstract: The fungal hydrolytic system efficiently degrades lignocellulosics efficiently. We previously characterized two hydrolytic enzymes from Gloeophyllum trabeum, namely, endoglucanase (Cel5B) and xylanase (Xyl10g). To enhance lignocellulosic degradation, we designed a fusion protein (Xyl10g GS Cel5B) using a glycine-serine (GS) linker and expressed it in Pichia pastoris GS115, which produced a hydrolytic fusion enzyme for the degradation of lignocellulosics. Purified Xyl10g GS Cel5B protein has a molecular weight of approximately 97 kDa and shows a lower specific activity than Xyl10g or Cel5B. However, Xyl10g GS Cel5B can degrade popping-pretreated rice straw, corn stover, kenaf, and oak more efficiently than the mixture of Xyl10g and Cel5B, by about 1.41-, 1.37-, 1.32-, and 1.40-fold, respectively. Our results suggest that Xyl10g GS Cel5B is an efficient hydrolytic enzyme and a suitable candidate for degrading lignocellulosics to produce fermentable sugar.
authors.affiliation: Department of Bioenergy Science and Technology, Chonnam National University, Gwangju 500-757, Republic of Korea.
authors.forename: Ho Myeong
authors.initials: HM
authors.lastname: Kim
authors.affiliation: Department of Wood Science and Landscape Architecture, Chonnam National University, Gwangju 500-757, Republic of Korea.
authors.forename: Sera
authors.initials: S
authors.lastname: Jung
authors.affiliation: Department of Wood Science and Landscape Architecture, Chonnam National University, Gwangju 500-757, Republic of Korea; Center for Research Facilities, Chonnam National University, Gwangju 500-757, Republic of Korea.
authors.forename: Kwang Ho
authors.initials: KH
authors.lastname: Lee
authors.affiliation: Department of Bioenergy Science and Technology, Chonnam National University, Gwangju 500-757, Republic of Korea.
authors.forename: Younho
authors.initials: Y
authors.lastname: Song
authors.affiliation: Department of Bioenergy Science and Technology, Chonnam National University, Gwangju 500-757, Republic of Korea; Department of Wood Science and Landscape Architecture, Chonnam National University, Gwangju 500-757, Republic of Korea; Bio-Energy Research Center, Chonnam National University, Gwangju 500-757, Republic of Korea. Electronic address: baehj@chonnam.ac.kr.
authors.forename: Hyeun-Jong
authors.initials: HJ
authors.lastname: Bae
mesh_terms: D002480:Cellulase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002614:Chelating Agents / Q000494:pharmacology; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D005998:Glycine; D006868:Hydrolysis; D007477:Ions / Q000737:chemistry; D007700:Kinetics; D008031:Lignin / Q000737:chemistry* / Q000378:metabolism; D008670:Metals / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012694:Serine
chemical_list: D002614:Chelating Agents; D007477:Ions; D008670:Metals; D011993:Recombinant Fusion Proteins; C036909:lignocellulose; D012694:Serine; D008031:Lignin; D002480:Cellulase; D043364:Endo-1,4-beta Xylanases; D005998:Glycine
keywords: Fusion protein; GS linker; Lignocellulose