Oxidoreductases TRIZ Cases

A recombinant host cell converts glucose to xylitol using NAD+-specific D-arabitol 4-oxidoreductase and NADPH-specific xylitol dehydrogenase.

Specific AlkB mutations at positions V129 and T136 reduce over-oxidation to dicarboxylic acids, increasing HLAME yield while maintaining green biocatalysis.

Engineered yeast cells replace expensive chemical catalysts to produce very long chain fatty acids via modular biological pathways.

Enzymatic oxidation using specific cytochrome P450 monooxygenases replaces costly classical isolation steps from natural oils.

Cupriavidus necator expresses cis-aconitate decarboxylase to boost itaconic acid titers while avoiding protein aggregation from heterologous enzymes.

A recombinant polypeptide catalyzes substrate prenylation to produce cannabinoids in a cell-free environment.

Coexpressing Campanula flavonoid 3′,5′-hydroxylase and Clitoria anthocyanin glucosyltransferase bypasses polyacylation to achieve true blue hues.

Endpoint TaqMan PCR assays eliminate denaturing steps to resolve DNA quality sensitivity bottlenecks in large-scale zygosity analysis.

Short interfering nucleic acids silence dopamine-beta-hydroxylase to lower intraocular pressure and slow optic neuropathy progression.

The 24DT21 gene enables safe 2,4-D application by metabolizing the herbicide via hydroxylation and conjugation, preventing dicot crop damage.

Alpha-glucosidase and glucose oxidase create firm centers and elastic surfaces, resolving texture uniformity trade-offs.

Wild-type bacterial enzymes replace transition metal complexes in reductive amination, eliminating waste while maintaining high enantiomeric excess.

Engineered oleaginous yeast produces desaturated fatty alcohols through heterologous enzyme expression, lowering production costs and environmental impact.

Enhanced fructose 6-phosphate epimerase and phosphatase convert substrates to tagatose, resolving costly separation and low yield bottlenecks.

Sorbitol dehydrogenase gene modulation alters maize seed size, number, and sugar profiles through targeted genetic expression changes.

Deleting the tyrB gene eliminates byproduct pathways, resolving the trade-off between high purity and low production cost.

Next-generation sequencing identifies the uncultivable symbiont's gene cluster, allowing ET-743 synthesis in host cells without natural source yields.

Phosphoketolase converts D-fructose to acetyl phosphate without ATP expenditure, increasing acetyl-CoA precursor yield.

Threonine residue substitution at position 149 stabilizes laccase protein structure, preventing aggregation and boosting recombinant yield in bacterial hosts.

Site-directed mutagenesis at positions 95, 108, 172, and 303 boosts enzyme activity 33-fold, reducing reaction time from 20 hours to 120 minutes.

Fermentation coupled with solvent extraction isolates methacrylate esters for subsequent transesterification into methyl methacrylate.

Deleting competing dehydrogenase genes reduces fructose by-product accumulation, raising the L-sorbose transformation rate to 96.12%.

Directed evolution of the POX gene modifies metabolic pathways to suppress short-chain dibasic acid formation during fermentation.

Introducing sulfhydryl oxidase into E. coli cytoplasm resolves the contradiction between low production costs and reliable disulfide bond formation.

Mutating residues A166, V376, and T196 in L-glutamate dehydrogenase enables high substrate concentration biocatalysis, resolving low efficiency bottlenecks.

Cell-free systems perform enzymatic hydroxylation and glycosylation to replicate natural collagen structures while maintaining industrial scalability.

Site-directed mutations in the substrate binding site of NMAADH improve catalytic activity and specificity for synthesizing N-alkyl amino acids.

Engineered alcohol dehydrogenase mutants catalyze asymmetric reduction of prochiral ketones to produce optically pure chiral diaryl alcohols.

Mutated HPPD polypeptides alter enzyme binding to resist herbicide inhibition, maintaining catalytic activity while conferring tolerance.

Mutated Diktyoglomus xylose isomerases maintain stability in crude hydrolysates, enabling efficient conversion without purification.