Structural analysis by circular dichroism of some enzymes involved in plant cell wall degradation

FEBS Letters

Gilbert, H.J.²  Clark, D.C.⁵  Hazlewood, G.P.⁴  Durrant, A.J.²  Waksman, G.¹  Goodenough, P.W.³ 

[1] Department of Agricultural Sciences, University of Bristol, UK;Department of Agriculture Biochemistry and Nutrition, University of Newcastle upon Tyne, UK;Department of Protein Engineering (Reading Laboratory), University of Newcastle upon Tyne, UK;Department of Biochemistry (Cambridge Research Station): Institute of Animal Physiology and Genetics Research, University of Bristol, UK;Food Structure Biopolymer Technology (Norwich Laboratory), AFRC Institute of Food Research, University of Newcastle upon Tyne, UK

关键词: Cellulase;    Polygalacturonase;    Xylanase;   

DOI  :  10.1016/0014-5793(91)80512-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three enzymes which degrade different polysaccharide components of plant cell walls have been characterized by circular dichroism (CD). A bacterial endoglucanase, which in the native state forms part of a multiprotein cellulase complex, showed a tendency to form aggregates as measured by CD. Depending on its degree of aggregation, this enzyme displayed between 50% and 100% helical structure, whereas a bacterial xylanase and a fungal polygalacturonase exhibited more β-sheet structure. The polygalacturonase was apparently devoid of helical structure.

【 授权许可】

Unknown