• Corpus ID: 11098074

Structure-function studies of two polysaccharide-degrading enzymes: Bacillus stearothermophilus α-amylase and Trichoderma reesei cellobiohydrolase II

  title={Structure-function studies of two polysaccharide-degrading enzymes: Bacillus stearothermophilus $\alpha$-amylase and Trichoderma reesei cellobiohydrolase II},
  author={Anu Koivula},
Amylases and cellulases are important enzymes both for the global carbon cycle on earth and for biotechnical applications. They are capable of degrading polysaccharides, which are chemically simple polymers of repeating glucose units that form very complex and water-insoluble macroscopic structures. The enzymatic degradation of starch and cellulose is poorly understood at the molecular level. The cloning and DNA sequence determination of amylaseand cellulase-encoding genes from various… 


Microbial amylolytic enzymes.
Genes encoding enzymes from all the amylolytic enzyme groups dealt with here have been cloned, and the sequences have been found to contain some highly conserved regions thought to be essential for their action and/or structure.
The biological degradation of cellulose.
The study of cellulolytic enzymes at the molecular level has revealed some of the features that contribute to their activity and an increasing number of three-dimensional structures are becoming available for cellulases and xylanases belonging to different families, which will provide paradigms for molecular modeling of related enzymes.
Molecular Biology of Cellulolytic Fungi
The synthesis, modification and hydrolysis of carbohydrates by glycosidase enzymes are some of the fundamental activities in nature and some 20 enzymes involved in the degradation of lignocellulose have been described.
Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis.
The specific activities of the intact enzymes and their cores on two forms of insoluble cellulose (crystalline, amorphous) differentiate the CBH I and CBH II in terms of adsorption and catalytic properties.
celB, a gene coding for a bifunctional cellulase from the extreme thermophile "Caldocellum saccharolyticum"
A gene from this organism, designated celB, has been cloned in Escherichia coli as part of a bacteriophage lambda gene library that produces a thermostable cellulase that shows both endoglucanase and exoglucAnase activities on test substrates and is able to degrade crystalline cellulose to glucose.
Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 A resolution.
Endoglucanase V, from the cellulolytic soil hyphomycete Humicola insolens, is an endocellulase, the catalytic core of which consists of 210 amino acids and is known to hydrolyze the beta-1,4 links with inversion of configuration at the anomeric carbon.
Cellulose hydrolysis by the cellulases from Trichoderma reesei: a new model for synergistic interaction.
Results obtained using filter paper pretreated with one component, followed by inactivation and subsequent hydrolysis with the same or another cellulase component, point to a sequential enzymic attack of the cellulose and seems consistent with the mathematical model presented.