Results 271 to 280 of about 66,613 (293)
Some of the next articles are maybe not open access.
Protein engineering of chymosin and expression in Trichoderma reesei
Biochemical Society Transactions, 1991Chymosin (EC 3.4.23.4) is an aspartic proteinase containing three disulphide bridges, which occurs naturally in the fourth stomach of the unweaned calf The mature enzyme initiates milk clotting by the specific cleavage of Ic-casein between the Phe105-Met106 bond [l-41. This high specificity forms the basis for its extensive use in the process of cheese
Pitts, Jim E. +4 more
openaire +5 more sources
Induction of Cellulases in Trichoderma reesei
1983Various synthetic derivatives of glucose and several different disaccharides were shaken with washed mycelia of Trichoderma reesei QM 9414 to test for CM-cellulase and for β-glucosidase activity. The extent of induction always increased with increases in the concentration of the inducers. Lactose and sophorose were good inducers, the latter being about
Hans-Peter Hohn, Hermann Sahm
openaire +2 more sources
Two major xylanases of Trichoderma reesei
Enzyme and Microbial Technology, 1992The two main xylanases produced by Trichoderma reesei were purified to electrophoretic homogeneity by ion-exchange and gel chromatography. The enzymes had isoelectric points of 9.0 and 5.5 and their molecular masses were 20 and 19 kDa, respectively.
Maija Tenkanen +2 more
openaire +2 more sources
Domain function in Trichoderma reesei cellobiohydrolases
Journal of Biotechnology, 1992The filamentous fungus, Trichoderma reesei produces all of the enzymatic activities required for efficient hydrolysis of highly ordered crystalline cellulose. All the principal enzymes involved in cellulose hydrolysis possess two functional domains, one directly involved in catalysis and the other in substrate recognition and binding.
Tapani Reinikainen +4 more
openaire +3 more sources
The α-glucuronidase-encoding gene of Trichoderma reesei
Gene, 1996The Trichoderma reesei cDNA coding for alpha-glucuronidase (GLRI), which releases glucuronic acid attached to xylose units of xylan, was cloned and sequenced. The deduced N-terminal amino acid (aa) sequence of the protein was verified by sequencing of the purified GLRI.
Merja Penttilä +3 more
openaire +3 more sources
Promoters and Synthetic Promoters in Trichoderma reesei
Trichoderma reesei holds immense promise for large-scale protein production, rendering it an excellent subject for deeper exploration using genetic engineering methods to achieve a comprehensive grasp of its cellular physiology. Understanding the genetic factors governing its intrinsic regulatory network is crucial, as lacking this knowledge could ...Muhammad, Adnan, Gang, Liu
openaire +2 more sources
Open the Pores: Electroporation for the Transformation of Trichoderma reesei
2020During the electroporation of T. reesei, linearized exogenous DNA is absorbed into swollen conidia by an electrical impulse. The advantage of this method is that it is less time-consuming, less expensive, and easier to perform than the classical protoplast transformation while at the same time having a comparable efficiency.
openaire +3 more sources