Expression and characterisation of chymosin pH optima mutants produced in Trichoderma reesei

INIS

• additives 20%
• applications 20%
• bonding 20%
• calves 20%
• catalysis 20%
• cellulase 20%
• comparative evaluations 20%
• design 20%
• enzymes 60%
• fungi 20%
• genes 20%
• hydrogen 20%
• kinetics 20%
• modifications 20%
• mutagenesis 20%
• mutants 100%
• peptides 20%
• ph value 100%
• production 20%
• promoters 20%
• protein engineering 20%
• residues 20%
• secretion 20%
• substrates 20%
• trichoderma reesei 100%

Keyphrases

• Active Enzyme 16%
• Active Sites 16%
• Aspartate 16%
• Calves 16%
• Cellobiohydrolase 16%
• Cellulase 16%
• Cellulolytic 16%
• Chymosin 100%
• Double mutant 33%
• Enzyme Kinetics 16%
• Escherichia Coli 16%
• Filamentous Fungi 16%
• Hydrogen Bond Network 16%
• Industrial Processes 16%
• Octapeptide 16%
• Optimum pH 100%
• Peptide Substrate 16%
• Protein Engineering 16%
• Rational Design 16%
• Site-directed mutagenesis 16%
• Strong Promoter 16%
• Trichoderma Reesei 100%

Immunology and Microbiology

• Cellulase 50%
• Enzyme Kinetics 50%
• Escherichia coli 50%
• Filamentous Fungus 50%
• Hypocrea jecorina 100%
• Peptides 50%
• Promoter Region 50%
• Protein Engineering 50%
• Secretion (Process) 50%
• Site Directed Mutagenesis 50%