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1 Rational transformation of Lactobacillus reuteri 121 reuteransucrase into a dextransucrase
article 2005    
Author: Kralj, S. · Geel-Schutten, G.H. van · Faber, E.J. · Maarel, M.J.E.C. van der · Dijkhuizen, L.
Keywords: Nutrition · Food technology · Amino acids · Bacteria · Catalysis · Mutagenesis · Synthesis (chemical) · Amino acid sequences · Glycosidic linkage · Mutation · Sugar-binding acceptors · Enzymes · 1,4 alpha glucan branching enzyme · dextransucrase · glucosyltransferase · maltose · oligosaccharide · sucrose · amino acid sequence · article · bacterial strain · catalysis · controlled study · enzyme synthesis · lactic acid bacterium · Lactobacillus reuteri · mutagenesis · nonhuman · priority journal · Amino Acid Sequence · Bacterial Proteins · Glucans · Glucose · Glucosyltransferases · Isomaltose · Kinetics · Lactobacillus · Magnetic Resonance Spectroscopy · Maltose · Molecular Sequence Data · Mutation · Protein Engineering · Sequence Alignment · Spectrum Analysis · Sucrase · Sucrose · Lactobacillus reuteri
[Abstract]

2 Aspergillus niger genome-wide analysis reveals a large number of novel alpha-glucan acting enzymes with unexpected expression profiles
article 2008    
Author: Yuan, X.-L. · Kaaij, R.M. van der · Hondel, C.A.M.J.J. van den · Punt, P.J. · Maarel, M.J.E.C. van der · Dijkhuizen, L. · Ram, A.F.J.
Keywords: Biology · Alpha-amylase · Alpha-glucan · Alpha-glucosidase · AmyR · Aspergillus niger · Cell wall · Glucoamylase · Maltose · Starch · Starch-binding domain · 1,4 alpha glucan branching enzyme · alpha glucosidase · amylase · cell enzyme · cell membrane protein · fungal protein · glucan 1,4 alpha glucosidase · glycosidase · glycosylphosphatidylinositol · maltose · protein amyr · starch · article · Aspergillus niger · carbohydrate metabolism · carbon source · controlled study · degradation · energy resource · enzymatic degradation · enzyme synthesis · gene expression profiling · gene identification · gene sequence · genetic transcription · genome analysis · microarray analysis · nonhuman · nucleotide sequence · priority journal · transcription regulation · alpha-Amylase · alpha-Glucosidases · Amino Acid Sequence · Aspergillus niger · Base Sequence · Conserved Sequence · Fungal Proteins · Gene Expression Profiling · Gene Expression Regulation, Fungal · Genome, Fungal · Genomics · Glucan 1,4-alpha-Glucosidase · Glycoside Hydrolases · Maltose · Molecular Sequence Data · Phylogeny · Trans-Activators · Transcription, Genetic · Aspergillus niger · Fungi
[Abstract]

3 Study of the glucoamylase promoter in Aspergillus niger using green fluorescent protein
article 1999    
Author: Santerre Henriksen, A.L. · Even, S. · Müller, C. · Punt, P.J. · Hondel, C.A.M.J.J. van den · Nielsen, J.
Keywords: Nutrition · Aspergillus niger · Chemostat · Glucoamylase promoter · Green fluorescent protein · Glucan 1,4 alpha glucosidase · Green fluorescent protein · Maltose · Xylose · Aspergillus niger · Continuous culture · Fungus culture · Growth rate · Mycelium · Nonhuman · Priority journal · Aspergillus niger · Genes, Reporter · Glucan 1,4-alpha-Glucosidase · Green Fluorescent Proteins · Luminescent Proteins · Promoter Regions (Genetics) · Aspergillus niger · Fungi
[Abstract]

4 Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase
article 2004    
Author: Kralj, S. · Geel-Schutten, G.H. van · Maarel, M.J.E.C. van der · Dijkhuizen, L.
Keywords: Nutrition · Food technology · Amino acid · Asparagine · Aspartic acid · Glucan · Glucoside · Glutamic acid · Glutamine · Glycosyltransferase · Oligosaccharide · Reuteransucrase · Sucrase · Sucrose · Unclassified drug · Amino terminal sequence · Bioassay · Carbohydrate synthesis · Carboxy terminal sequence · Catalysis · Controlled study · Deletion mutant · Enzyme activity · Enzyme analysis · Enzyme inactivation · Enzyme kinetics · Lactobacillus reuteri · Leuconostoc · Molecular size · Nonhuman · Priority journal · Protein binding · Sequence alignment · Streptococcus · Amino Acid Sequence · Binding Sites · Gene Deletion · Glucans · Glycosyltransferases · Kinetics · Lactobacillus · Maltose · Molecular Sequence Data · Mutagenesis, Site-Directed · Sucrose · Lactobacillus · Lactobacillus reuteri · Leuconostoc · Streptococcus
[Abstract]

5 Properties and applications of starch-converting enzymes of the alpha-amylase family
article 2002    
Author: Maarel, M.J.E.C. van der · Veen, B. van der · Uitdehaag, J.C.M. · Leemhuis, H. · Dijkhuizen, L.
Keywords: Nutrition · α-Amylase · Anti-staling of bread · Glycosylhydrolases · Starch industry · Starch-converting enzymes · Amino acids · Chemical bonds · Conformations · Crystallization · Enzymes · Hydrolysis · Mutagenesis · Substrates · X-ray crystallography · Amylopectin · Cyclodextrin · Cyclomaltodextrin glucanotransferase · Dextrin · Dipeptidyl carboxypeptidase · Fructose · Glucose · Glycosidase · Maltodextrin · Maltose · Maltotriose · Transferase · Bacterium · Crop · Enzyme active site · Enzyme conformation · Enzyme engineering · Enzyme mechanism · Enzyme specificity · Enzyme stability · Enzyme substrate complex · Enzyme synthesis · Food processing · Industrial production · Protein domain · Protein family · Site directed mutagenesis · Structure activity relation · Amino Acid Sequence · Biotechnology · Conserved Sequence · Glycoside Hydrolases · Glycosyltransferases · Models, Molecular · Molecular Sequence Data · Protein Conformation · Sequence Homology, Amino Acid · Substrate Specificity · Manihot esculenta · Solanum tuberosum · Triticum aestivum · Zea mays
[Abstract]

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