Glycosylases TRIZ Cases

Yeast expression replaces Jack Bean extraction to produce active β-hexosaminidase with lower contamination risk, easier purification, and better reproducibility.

Low-temperature protease treatment extracts nutrients from fibrous plant material while preserving protein function, beta glucan, and filtration efficiency.

Controlled α-amylase and β-glucanase levels preserve β-glucan during starch liquefaction, cutting purification cost and effort.

Using α-amylase and cellulase raises viscosity and water retention in plant-based yogurt without added thickeners or emulsifiers.

Combining exo- and endo-type cellulases from different origins raises water-soluble dietary fiber and cuts residues in plant-based liquids.

See how α-galactosidase hydrolysis supplies free galactose before fermentation, enabling EPS-producing bacteria to create smooth, creamy vegetable milk food.

Gene editing disables myrosinase, AOP2, and CYP79F1 targets to reduce mustard pungency and bitterness for fresh consumption.

A 0–5°C protease treatment lasting under 30 minutes recovers nutrients from fibrous plant waste while preserving protein and beta glucan.

Glucoamylase and α-glucosidase modify rice starch to limit cold-storage hardening, moisture loss, and cooking-pot sticking.

This case uses recombinant CTS1 to detect fungal antigen or antibodies by ELISA, improving early coccidioidomycosis diagnosis.

De-starch corn fiber, extract arabinoxylan at pH 5–14, and separate a food-suitable product without extra purification.

A tandem genetic construct integrates multiple expression cassettes into a single unit within filamentous fungal host cells.

Soluble fiber and controlled enzyme hydrolysis adjust beverage viscosity and lubricity, resolving the trade-off between fat content and sensory creaminess.

Segmented endoglucanase polypeptides resolve complex cellulose breakdown bottlenecks to boost ethanol production efficiency.

Overexpressing regulatory genes in Trichoderma increases enzymatic activity while reducing biomass consumption and nutrient usage.

Soil-derived GH5 endoglucanase maintains activity at 58°C and pH 4-9, resolving thermal instability limits in lignocellulosic biomass conversion.

Beta-1,3-galactanase enzymes solubilize carbohydrates from roasted coffee beans to increase soluble solid yield.

Targeted amino acid substitutions in variant endoglucanases improve total activity and pH tolerance, resolving industrial performance bottlenecks.

Fusing human and archaeal domains creates a hybrid enzyme that selectively cleaves T:G mispairs without disrupting base pairing context.

Targeting chelator-induced instability via segmentation and local quality principles, these variants maintain activity while reducing mutagenesis complexity.

Adding a solubility-promoting compound to corn tissue homogenate dissolves bound Amy797E alpha-amylase, enabling ELISA detection at 1:1000 dilution.

Sequential enzymatic modification of oat base using specific alpha-amylases and endoprotease prevents flocculation in hot acidic beverages.

Amino acid modifications at defined positions improve thermostability and resistance to denaturing conditions in detergent applications.

GH114 glycosyl hydrolase polypeptides degrade biofilm components to prevent soil redeposition and malodor in laundry detergents.

Deleting the cellulose-binding module increases enzyme activity while maintaining thermal stability at 70°C.

Intein-modified proteins insert inteins at specific sites to control enzymatic activity, preventing host growth degradation from hydrolytic enzymes.

Segmented enzyme treatment boosts oat drink foaming and stability while retaining natural flavor and nutrients.

Elevated temperature processing with Trichoderma reesei enzymes degrades residual pectin, resolving cloudiness and filtration bottlenecks.

Specific amino acid substitutions enable engineered amylases to resist thermal denaturation at 90°C for effective starch stain removal.

Synthetic codon-optimized amylase genes integrate into Bacillus genomes to boost enzyme concentration while resolving productivity consistency trade-offs.

Site-directed mutagenesis replaces tyrosine with histidine at position 25, increasing production yield by 1.68-fold while maintaining thermostability.