Interfacial molecular interactions of cellobiohydrolase Cel7A and its variants on cellulose [electronic resource]

• Ngôn ngữ: eng
• Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Basic Energy Sciences ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2020
• Mô tả vật lý: Size: Article No. 10 : , digital, PDF file.
• Bộ sưu tập: Metadata
• ID: 262694
• Chủ đề: 1. 09 biomass fuels

Tóm tắt

 Molecular-scale mechanisms of the enzymatic breakdown of cellulosic biomass into fermentable sugars are still poorly understood, with a need for independent measurements of enzyme kinetic parameters. We measured binding times of cellobiohydrolase Trichoderma reesei Cel7A (Cel7A) on celluloses using wild-type Cel7A (WT<
 sub>
 intact<
 /sub>
 ), the catalytically deficient mutant Cel7A E212Q (E212Q<
 sub>
 intact<
 /sub>
 ) and their proteolytically isolated catalytic domains (CD) (WT<
 sub>
 core<
 /sub>
  and E212Q<
 sub>
 core<
 /sub>
 , respectively). The binding time distributions were obtained from time-resolved, super-resolution images of fluorescently labeled enzymes on cellulose obtained with total internal reflection fluorescence microscopy.