Biocatalysis centers on enzyme molecules or cell-based catalytic systems and achieves highly efficient and highly selective transformations under mild conditions through precise control of substrate recognition, transition-state stabilization, and reaction-pathway selection. With the continued development of enzyme discovery technologies, protein engineering, immobilization strategies, cofactor recycling systems, and continuous manufacturing platforms, industrial enzymology has evolved from a traditional processing-support technology into an important technical foundation for green manufacturing, fine synthesis, and the upgrading of bio-based industries.
Keywords: biocatalysis; industrial enzymology; enzyme engineering; immobilized enzymes; cofactor regeneration; continuous manufacturing; green chemistry; chiral synthesis; multi-enzyme cascades; biomanufacturing
I. Basic Concepts of Biocatalysis and Industrial Enzymology
1.1 Fundamental connotations of biocatalysis
(1) Molecular basis of enzymatic catalysis
The core function of enzymes is not limited to accelerating reaction rates, but more importantly lies in the high-precision recognition, directional binding, and transition-state stabilization of substrates through the active site, thereby reshaping reaction energy barriers and reaction pathways at the molecular scale. Compared with traditional chemical catalysis, enzymatic catalysis relies more strongly on three-dimensional structural information and local microenvironmental control, and therefore usually exhibits higher levels of chemoselectivity, regioselectivity, and stereoselectivity.
(2) System-level attributes of industrial enzymology
The object of study in industrial enzymology is not an isolated enzyme molecule, but rather a complete technical system encompassing enzyme discovery, expression, preparation, modification, immobilization, reactor adaptation, process scale-up, and quality control. An enzyme with true industrial value must not only possess substantial initial activity, but also balance stability, scalability, economic feasibility, and process compatibility.
1.2 The technical relationship between industrial enzymology and traditional chemical catalysis
(1) Not simple replacement, but pathway reconstruction
Industrial enzymology is not merely a straightforward substitution for existing chemical routes. Its more important significance lies in reconstructing reaction pathways and manufacturing logic. In scenarios involving complex molecular late-stage modification, highly selective transformation, processing under mild conditions, and low-carbon manufacturing, biocatalysis can often provide process solutions that are difficult to achieve with conventional technologies.
(2) From condition-driven to structure-driven control
Traditional processes usually drive reactions forward through temperature, pressure, pH, and catalyst strength, whereas biocatalysis places greater emphasis on precise control through enzyme structure, cofactor cycling, local microenvironment, and process integration. This difference determines the unique methodological value of industrial enzymology in advanced manufacturing.
II. Major Categories of Industrial Enzymes and Functional Division of Catalysis
2.1 Industrial enzymes classified by catalytic reaction type
(1) Oxidoreductases
Oxidoreductases mainly catalyze oxidation, reduction, hydroxylation, and electron-transfer-related reactions. Dehydrogenases, reductases, oxidases, monooxygenases, and peroxidases all belong to this category. These enzymes are widely used in the preparation of chiral alcohols, chiral amines, complex natural product derivatives, and pharmaceutical intermediates, and occupy an important position in high-value fine synthesis.
(2) Transferases
Transferases catalyze the directed transfer of amino, methyl, glycosyl, acyl, phosphate, and other functional groups between different substrates. They show clear advantages in natural product modification, nucleoside analog construction, glycosylation engineering, and highly selective functional-group installation, but are often accompanied by strong cofactor dependence.
(3) Hydrolases
Hydrolases are the most broadly applied class of industrial enzymes and mainly include lipases, esterases, proteases, amylases, cellulases, pectinases, and phytases. These enzymes can be used not only for substrate cleavage, but also for reverse synthesis in low-water-activity systems, making them foundational enzyme classes in the food, feed, detergent, textile, paper, and bioenergy industries.
(4) Lyases, isomerases, and ligases
Lyases are well suited for cleavage and formation of C-C, C-N, and C-O bonds in the absence of water participation; isomerases are used for rearrangement of molecular skeletons and chiral centers; ligases catalyze molecular coupling under energy-supplying conditions. Although the overall usage volume of these enzyme classes is relatively low, they play irreplaceable roles in the construction of high-value molecules and complex biosynthetic processes.
2.2 Enzymatic modules classified by industrial application function
(1) Raw material pretreatment enzymes
These enzymes mainly serve processes such as starch liquefaction, fiber degradation, cell wall disruption, protein pre-hydrolysis, and impurity removal, with the primary purpose of improving downstream processing efficiency and substrate availability.
(2) Selective transformation enzymes
These enzymes directly determine the structure, purity, and enantioselectivity of target products. They are commonly used in chiral resolution, asymmetric reduction, site-specific oxidation, and directed functional-group modification, and serve as key catalytic units in the manufacture of pharmaceuticals, flavors and fragrances, and high-end intermediates.
(3) Quality improvement enzymes
In industries such as food, textiles, pulp, and leather, many enzymes are not used solely to generate entirely new compounds, but rather to regulate viscosity, mouthfeel, softness, surface properties, and processing performance, reflecting the precise control that industrial enzymology exerts over system physicochemical properties and product quality.
Table 1. Major enzyme classes and representative enzymes in the application system of biocatalysis and industrial enzymology
Enzyme Category | Representative Enzymatic Modules | Core Catalytic Tasks | Typical Industrial Scenarios | Technical Characteristics |
Oxidoreductases | Dehydrogenases, monooxygenases, peroxidases, laccases | Catalyze oxidation, reduction, hydroxylation, and electron transfer reactions | Chiral intermediate synthesis, late-stage modification of natural products, green oxidation, dye degradation | High selectivity; often requires cofactor regeneration or oxygen supply systems |
Transferases | Transaminases, glycosyltransferases, methyltransferases, acyltransferases | Enable directed transfer of functional groups such as amino, glycosyl, methyl, and acyl groups | Chiral amine preparation, glycosylation modification, structural optimization of natural products, modification of high-value molecules | Strong functional-group selectivity, but system design usually depends more heavily on cofactors and substrate matching |
Hydrolases | Lipases, esterases, proteases, amylases, cellulases, xylanases, pectinases, lactases, etc. | Catalyze cleavage of ester bonds, peptide bonds, glycosidic bonds, and related linkages; some systems can also be used for reverse synthesis | Lipid modification, biodiesel production, starch processing, juice clarification, lignocellulose saccharification, food and feed processing | The most widely used enzyme class in industry; broad substrate scope; suitable for bulk processing and immobilized scale-up |
Isomerases | Glucose isomerase, xylose isomerase, etc. | Catalyze molecular skeletal rearrangement and aldose-ketose isomerization | High-fructose syrup production, xylose utilization, biorefining | Mature process technology; suitable for large-scale continuous conversion |
Lyases/Ligases | Aldolases and other C-C bond-forming enzymes, ATP-dependent ligases | Catalyze directed bond cleavage and formation for construction of complex molecular scaffolds or molecular coupling | Synthesis of chiral hydroxy ketones, construction of complex intermediates, high-value fine synthesis | Usually used at relatively low volume, but highly valuable in the manufacture of complex molecules |
III. Core Advantages and Practical Boundaries of Biocatalysis
3.1 Outstanding advantages of biocatalysis
(1) High selectivity
When dealing with substrates containing multiple functional groups, complex scaffolds, or multiple chiral centers, enzymes can usually avoid the extensive reliance on protection-deprotection strategies commonly seen in traditional chemical reactions, thereby reducing by-product formation, shortening process routes, and improving target product purity.
(2) Mild operating conditions
Most industrial enzymes can operate under normal pressure, at low to moderate temperatures, and near neutral pH. This feature is particularly suitable for the processing of heat-sensitive substrates, oxidation-prone substrates, and complex natural molecules, while also helping reduce equipment energy consumption and safety risks.
(3) Potential for green manufacturing
Enzymatic catalysis typically involves lower dependence on heavy metals, fewer side reactions, and simpler impurity profiles. It therefore offers significant advantages in the context of green processes, low-carbon manufacturing, and sustainable development.
3.2 Key limiting factors of biocatalysis
(1) Insufficient enzyme stability
Many natural enzymes are readily inactivated under conditions of high substrate concentration, organic solvents, interfacial stress, and elevated temperature. As a result, natural enzymes are often unable to directly meet industrial operational requirements and must be improved through enzyme engineering and process optimization.
(2) Limited substrate scope and reaction window
Some enzymes are highly sensitive to changes in substrate structure, which limits their industrial applicability. During process scale-up, insufficient substrate adaptability often has a more decisive impact than insufficient catalytic activity under laboratory conditions.
(3) Cofactor dependence increases process complexity
For oxidoreductases and some transferases, cofactor cost and regeneration efficiency directly determine economic feasibility. If an efficient recycling system cannot be established, their industrial competitiveness is substantially reduced.
IV. Discovery, Screening, and Enzyme Engineering Optimization of Industrial Enzymes
4.1 Expansion of industrial enzyme sources
(1) Development of natural enzyme resources
Traditional industrial enzyme discovery mainly relied on microbial isolation, cultivation, and functional screening. Enzymes derived from soils, oceans, hot springs, salt lakes, and other extreme ecological niches often possess unique thermostability, salt tolerance, solvent tolerance, or substrate adaptability.
(2) Metagenomic and database-driven mining
With advances in sequencing technology and bioinformatics, industrial enzyme discovery has expanded from cultivable microorganisms to environmental genetic resources. Metagenomic technology is particularly suitable for discovering novel enzymes and catalytic scaffolds from uncultivable microorganisms and complex ecosystems.
4.2 Enzyme engineering is the core driving force for industrial application
(1) Rational design
Through structural analysis, molecular docking, and active-site identification, site-directed modification of key amino acid residues can improve enzyme activity, thermostability, solvent tolerance, and enantioselectivity. This strategy is suitable for enzyme systems whose structural and mechanistic information is relatively well understood.
(2) Directed evolution
Directed evolution simulates natural selection through the construction of mutation libraries and high-throughput screening, allowing the acquisition of enzyme variants with higher activity, greater stability, or broader substrate scope. Its advantage lies in not being completely dependent on mechanistic elucidation and being particularly suitable for the modification of complex phenotypes.
(3) Semi-rational design and algorithm-assisted optimization
Current enzyme engineering increasingly emphasizes the integration of structure prediction, sequence co-evolution analysis, and machine learning-assisted design. Its core value lies in reducing mutation space, increasing screening hit rates, and shortening the development cycle from enzyme discovery to industrial adaptation.
V. Enzyme Stability, Cofactor Cycling, and Immobilization Technologies
5.1 Enzyme stability is a prerequisite for industrial usability
(1) Thermostability and operational stability
Industrial reactions usually require catalytic systems to maintain activity over extended periods. Therefore, thermostability and long-term operational stability often carry greater industrial significance than instantaneous enzyme activity. If an enzyme rapidly loses activity during the operating cycle, its industrial value remains very limited even if its initial activity is high.
(2) Solvent tolerance and product tolerance
High substrate concentration, hydrophobic substrates, and organic cosolvents are common conditions in industrial systems. Whether an enzyme can adapt to such environments directly affects space-time yield and process feasibility.
5.2 Cofactor regeneration systems determine the economics of redox processes
(1) Core issues in cofactor-dependent reactions
Systems involving dehydrogenases, reductases, and monooxygenases usually depend on NADH, NADPH, or ATP. If these cofactors are added in a single-use manner, the cost is generally unacceptable. Efficient regeneration systems are therefore essential.
(2) Engineering significance of regeneration strategies
Common regeneration strategies include glucose dehydrogenase-coupled regeneration, formate dehydrogenase-based regeneration, electrochemical regeneration, and light-driven regeneration. Regeneration systems influence not only raw material cost, but also significantly alter reaction equilibrium, substrate conversion, and by-product profiles.
5.3 Immobilization technology drives the transition of enzymatic catalysis toward continuous operation
(1) Core purpose of immobilization
Immobilization technology can improve enzyme reusability, operational stability, and reactor compatibility. Through carrier adsorption, covalent coupling, entrapment, or cross-linking, enzymes can be constructed into solid-phase catalytic systems more suitable for industrial operation.
(2) Immobilization strategies must be designed in coordination with the process
Although immobilization may improve stability, it may also introduce mass-transfer resistance, active-site shielding, or local conformational constraints. Therefore, carrier properties, pore structure, coupling methods, and the local microenvironment must be optimized in coordination with specific substrates and reactor formats.
VI. Biocatalytic Reaction Systems and Process Integration
6.1 Reaction media and mass-transfer design
(1) Expansion of reaction media
Industrial enzymatic reactions are not limited to pure aqueous systems. Water-organic biphasic systems, ionic liquids, deep eutectic solvents, and low-water-activity systems can all be used to improve the solubility of hydrophobic substrates, optimize the enzyme microenvironment, and regulate reaction equilibrium.
(2) Mass-transfer control is often a decisive factor
In interfacial reactions, immobilized-enzyme systems, and high-substrate-concentration systems, reaction rates are often affected by substrate diffusion, oxygen transfer, product release, and local cofactor recycling efficiency. Accordingly, optimization of industrial enzyme reactions cannot focus only on the enzyme molecule itself, but must also attach importance to material transfer behavior within the reactor.
6.2 Batch, continuous flow, and multi-enzyme cascades
(1) Batch reactions are suitable for process development
Batch systems offer high flexibility and are well suited for parameter exploration and small-scale production of high-value products, but they usually exhibit an upper efficiency limit in scenarios requiring continuous manufacturing and high space-time productivity.
(2) Continuous-flow reactions are suitable for industrial scale-up
When enzyme immobilization, substrate feeding, and online control systems become sufficiently mature, continuous-flow reactors can significantly improve space-time productivity, reduce manual intervention, and enhance product quality consistency.
(3) Multi-enzyme cascades help compress process workflows
By integrating multiple enzymatic steps within the same system, it is possible to reduce intermediate isolation, shorten process routes, and improve atom economy. However, multi-enzyme cascades also introduce more complex engineering challenges such as condition coupling, rate imbalance, and intermediate toxicity.
VII. Application Systems of Biocatalysis in Major Industrial Sectors
7.1 Pharmaceutical and fine chemical manufacturing
(1) Preparation of chiral intermediates
Ketoreductases, transaminases, esterases, lipases, and nitrile hydratases play central roles in the preparation of chiral pharmaceutical intermediates. Their main advantages lie in high enantioselectivity and excellent batch-to-batch consistency.
(2) Late-stage modification of complex scaffolds
For natural product derivatives, heterocyclic drugs, and multifunctional molecules, monooxygenases, methyltransferases, and glycosyltransferases can provide site specificity and regioselectivity in late-stage modification that are difficult to achieve with conventional chemical methods.
7.2 Food, feed, and fermentation industries
(1) Raw material processing and quality improvement
Amylases, proteases, pectinases, and lactases have been widely used in starch sugar production, baking improvement, juice clarification, and preparation of low-lactose dairy products. The emphasis of such applications lies in improving processing efficiency and enhancing final product quality.
(2) Nutrient release and improvement of utilization efficiency
Phytases, cellulases, and proteases can improve the availability of minerals, carbohydrates, and proteins in feed, while reducing the environmental burden caused by undigested components.
7.3 Textile, detergent, pulp, and leather industries
(1) Replacement of highly polluting chemical steps
Proteases, cellulases, xylanases, and laccases can be used for desizing, polishing, bleaching assistance, and surface modification, thereby reducing dependence on traditional strong alkali, strong oxidants, and high-temperature treatment steps.
(2) Functional regulation of material surfaces
The value of industrial enzymes in these fields lies not only in impurity removal, but also in the fine regulation of fiber surface properties, softness, color, and processing stability.
7.4 Bioenergy and bio-based materials
(1) Lignocellulosic biorefining
Cellulases, hemicellulases, and related auxiliary enzymes are key technological supports for lignocellulosic saccharification and subsequent fermentative utilization, directly determining the construction efficiency of bio-based sugar platforms.
(2) Lipid biotransformation
Lipases can be used in biodiesel production and structured lipid modification, showing significant advantages in the processing of feedstocks with high free fatty acid content and in mild transesterification reactions.
VIII. Key Evaluation Metrics in Industrial Scale-Up
8.1 Process performance should not be evaluated solely by substrate conversion
(1) Space-time yield better reflects industrial efficiency
In laboratory studies, conversion is often used to evaluate biocatalytic performance, whereas industrial systems focus more on product generation per unit volume and per unit time. If the space-time yield is low, even a reaction that eventually reaches completion is unlikely to constitute a competitive industrial route.
(2) High substrate-loading capability is critical for scale-up
Industrial processes usually require high substrate concentration and high final product concentration in order to reduce equipment occupancy and separation cost. Therefore, enzyme stability and mass-transfer adaptability under high-loading conditions are more meaningful for scale-up than initial activity under low-concentration conditions.
8.2 Overall process economics determine final feasibility
(1) Upstream enzyme production and downstream separation are equally important
The fermentation expression level, purification cost, storage stability, and formulation difficulty of enzymes directly affect overall process economics. At the same time, post-reaction separation and purification, residual control, and quality consistency are also critical factors determining whether industrial application can be realized.
(2) Regulatory and quality-system constraints cannot be ignored
Particularly in the pharmaceutical, food, and feed fields, industrial enzymatic routes must possess not only technical feasibility, but also meet requirements for regulatory compliance, controllable impurity profiles, and batch-to-batch consistency.
IX. Development Trends in Biocatalysis and Industrial Enzymology
9.1 From single-enzyme applications toward platform-based manufacturing
(1) Multi-enzyme cascades and modular design
Future industrial enzymology will place greater emphasis on modular design, integrating substrate activation, scaffold construction, functional-group modification, and cofactor regeneration into unified platforms in order to improve the manufacturing efficiency of complex molecules.
(2) Parallel development of cell factories and cell-free enzyme systems
In certain application scenarios, engineered microorganisms are better suited to undertake complex metabolic flux reconstruction; by contrast, in high-value fine transformations, cell-free enzyme systems are more conducive to precise control of substrates, reaction sequence, and by-product profiles. Over the long term, these two approaches will develop in a complementary manner.
9.2 Digitalization and intelligence accelerate enzymology development
(1) Computational design accelerates enzyme engineering
Structure prediction, molecular docking, kinetic simulation, and machine learning are significantly improving the efficiency of enzyme screening and mutation design, driving enzyme engineering from experience-based development toward data-driven development.
(2) Process development is moving toward predictable control
The integration of online analysis, process modeling, and automated control will shift biocatalytic process development from trial-and-error optimization toward model-based design, thereby improving the success rate from pilot study to scale-up.
X. Aladdin-Related Products
Catalog No. | Product Name | Grade and Purity | Enzyme Category | Typical Industrial Application |
myo-Inositol dehydrogenase | -- | Oxidoreductase | Polyol oxidation and fine synthesis | |
Recombinant Alcohol Dehydrogenase (ADH) | Bioactive, ActiBioPure™, High Performance, EnzymoPure™, ≥90%(SDS-PAGE), ≥100 U/mg protein | Oxidoreductase | Chiral alcohol/ketone conversion; synthesis of pharmaceutical intermediates | |
Alcohol Dehydrogenase from Saccharomyces cerevisiae | EnzymoPure™, ≥300 units/mg protein | Oxidoreductase | Alcohol redox conversion; cofactor-coupled biotransformation | |
Recombinant Glucose Dehydrogenase (GDH-FAD) | ActiBioPure™, Bioactive, High Performance, EnzymoPure™, Recombinant, ≥700 U/mg powder | Oxidoreductase | Cofactor regeneration; redox cascade reactions | |
Recombinant Glucose Dehydrogenase (GDH-FAD) | ActiBioPure™, Bioactive, High Performance, EnzymoPure™, Recombinant, ≥95%(SDS-PAGE), ≥300 U/mg powder | Oxidoreductase | Cofactor regeneration; continuous reduction systems | |
Recombinant Glucose Dehydrogenase (GDH-FAD) | ActiBioPure™, Bioactive, Recombinant, High Performance, EnzymoPure™, ≥475 U/mg powder | Oxidoreductase | Cofactor cycling; enzyme-coupled reactions | |
Recombinant Glucose Dehydrogenase (GDH-FAD) | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,≥90%(SDS-PAGE),≥450 U/mg enzyme powder | Oxidoreductase | Cofactor regeneration; support for process scale-up | |
Tyrosine 3-monooxygenase | -- | Oxidoreductase | Hydroxylation modification; late-stage modification of natural products | |
Peroxidase from horseradish | Type I, essentially salt-free, lyophilized powder,≥50 units/mg solid (using pyrogallol) | Oxidoreductase | Oxidative coupling; dye decolorization; analytical catalysis | |
Peroxidase from horseradish | Type X, ammonium sulfate suspension | Oxidoreductase | Mild oxidation; environmental remediation | |
Lactoperoxidase from Bovine Milk | EnzymoPure™, ≥35 units/mg dry weight | Oxidoreductase | Oxidative reactions; food and bioprocessing | |
Peroxidase from horseradish（HRP） | EnzymoPure™, ≥180 U/mg powder, Rz≥2.0 | Oxidoreductase | High-efficiency oxidation; detection and fine biotransformation | |
Laccase | Bioactive,Recombinant,ActiBioPure™,EnzymoPure™,≥1 U/mg Liquid; from Aspergillus sp. | Oxidoreductase | Oxidation of aromatic compounds; pulp bleaching; wastewater treatment | |
Laccase from Trametes versicolor | EnzymoPure™,≥0.5 U/mg,from Trametes versicolor | Oxidoreductase | Lignin modification; green oxidation | |
Laccase | Native,EnzymoPure™,≥1000 LAMU/g; from Aspergillus sp. | Oxidoreductase | Material surface modification; dye degradation | |
β-Alanine-pyruvate transaminase | -- | Transferase | Amino transfer; chiral amine construction | |
Alanine Aminotransferase (ALT/GPT) | Bioactive, ActiBioPure™，Native，High Performance，EnzymoPure™，from Porcine Heart；≥90 U/mg enzyme powder | Transferase | Amino transfer; preparation of amino acid derivatives | |
alpha-1,2-Fucosyltransferase (α1,2FucT) | -- | Transferase | Glycosylation modification; glycoengineering | |
α-1,4-Galactosyltransferase | EnzymoPure™, ≥95%(SDS-PAGE) | Transferase | Oligosaccharide synthesis; directed glycosylation modification | |
beta-1,3-Galactosyltransferase (CgtB) | -- | Transferase | Glycoside construction; glycan chain elongation | |
Beta-1,4-Galactosyltransferase 1 (Y285L) | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,His Tag,expressed in HEK293；>1000 U/mg protein；Protein concentration: See COA | Transferase | Directed galactosylation; glycoengineering development | |
Beta-1,4-galactosyltransferase 1 | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,His Tag,expressed in Baculovirus-BTI-TN-5B1-4 Cells；>2000 U/mg protein；Protein concentration: See COA | Transferase | Glycan modification; biocatalytic glycosylation | |
Galactosyltransferase | -- | Transferase | Glycosylation engineering; preparation of functional oligosaccharides | |
Fucosyltransferase 6 | -- | Transferase | Fucosylation modification; glycoengineering | |
Fucosyltransferase 8 | -- | Transferase | Fucosylation of proteins/oligosaccharides | |
Fucosyltransferase 9 | -- | Transferase | Construction of complex glycans | |
Bovin beta-1,4-galactosyltransferase 1 | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,His Tag,expressed in Baculovirus-BTI-TN-5B1-4 Cells；>2000 U/mg protein；Protein concentration: See COA | Transferase | Glycosylation scale-up; directed glycan elongation | |
Bovin beta-1,4-galactosyltransferase 1 (Y289L) | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,His Tag,expressed in HEK293；>1000 U/mg protein；Protein concentration: See COA | Transferase | Engineered glycosyl transfer; substrate scope expansion | |
Immobilized Candida antarctica Lipase B (Immobilized CALB) | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,≥5000PLU/g; Immobilized on Porous methyl methacrylate resin; expressed in Aspergillus niger | Hydrolase | Immobilized catalysis; transesterification; chiral resolution | |
Immobilized Candida antarctica Lipase B (Immobilized CALB) | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,≥12000PLU/g; Immobilized on Porous methyl methacrylate resin; expressed in Aspergillus niger | Hydrolase | Continuous-flow reactions; non-aqueous catalysis | |
Immobilized Thermomyces lanuginosus Lipase (TLL) | Bioactive,ActiBioPure™,High Performance,EnzymoPure™,>3000PLU/g dry weight; Immobilized on hydrophobic carrier; from Thermomyces lanuginosus | Hydrolase | Lipid modification; biodiesel production; immobilized processing | |
Immobilized Rhizomucor miehei Lipase | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,≥9000PLU/g; Immobilized on Porous methyl methacrylate resin; expressed in Aspergillus niger | Hydrolase | Transesterification; preparation of structured lipids | |
Lipase PS, from Burkholderia cepacia | Recombinant, EnzymoPure™, ≥23,000 U/g, pH 7.0, 50 °C,expressed in Burkholderia cepacia | Hydrolase | Chiral resolution; fine chemical preparation | |
lipase PS-IM | EnzymoPure™, ≥500 U/gimmobilized on diatomaceous earth | Hydrolase | Immobilized chiral resolution; continuous manufacturing | |
Lipase | Bioactive,ActiBioPure™,High Performance,EnzymoPure™,from Aspergillus oryzae; ≥20000 LU/g | Hydrolase | Lipid hydrolysis; food processing | |
Lipase from Candida sp. | EnzymoPure™, ≥5000 LU/g | Hydrolase | Transesterification; fine organic synthesis | |
Lipase from Thermophila sparsiformis | EnzymoPure™, ≥100000 U/g | Hydrolase | High-load lipid conversion; industrial scale-up | |
Lipase from Aspergillus niger | technical grade, ≥100 U/mg powder | Hydrolase | Bulk enzymatic processing; industrial lipid treatment | |
β-Galactosidase (GAL) | EnzymoPure™,≥50 units/mg dry weight,Originating from Escherichia coli | Hydrolase | Low-lactose products; preparation of functional oligosaccharides | |
β-Galactosidase from Escherichia coli(Purified) | EnzymoPure™,≥300 units/mg protein | Hydrolase | Lactose hydrolysis; optimization of food processing | |
Cellulase (Carrier for dextrine) | EnzymoPure™, powder,10,000U/g | Hydrolase | Lignocellulose saccharification; biomass utilization | |
Esterase from Porcine Liver | Bioactive, ActiBioPure™, EnzymoPure™, ≥15 U/mg powder | Hydrolase | Ester resolution; analysis and intermediate preparation | |
Esterase, Bacillus stearothermophilus | -- | Hydrolase | Thermostable ester hydrolysis; fine synthesis | |
Esterase, Bacillus subtilis | -- | Hydrolase | Ester bond hydrolysis; mild industrial biotransformation | |
Epoxide hydrolase | -- | Hydrolase | Ring-opening of chiral epoxides; diol preparation | |
Pectinase from Aspergillus niger | EnzymoPure™；≥20 units/mg dry weight | Hydrolase | Juice clarification; plant tissue disruption | |
Pectinase from Aspergillus niger | Native；EnzymoPure™；≥30 000U/g | Hydrolase | Food processing; raw material pretreatment | |
Xylanase | EnzymoPure™；>100 000U/g | Hydrolase | Pulp and paper processing; feed; hemicellulose degradation | |
Xylanase | Recombinant；powder,≥2500 units/g, recombinant, expressed in Aspergillus oryzae | Hydrolase | Biorefining; xylan degradation | |
Xylanase from Pichia pastoris | technical grade；≥100 U/mg powder | Hydrolase | Paper-making aid; lignocellulosic pretreatment | |
Cellulase | Native；EnzymoPure™；≥4500 CNU-R/g | Hydrolase | Cellulose degradation; construction of bio-based sugar platforms | |
Cellulase, enzyme blend | Bioactive；ActiBioPure™；High Performance；EnzymoPure™；>1000 BHU/g | Hydrolase | Composite-enzyme saccharification; biomass conversion | |
Cellulase (Carrier for starch) | EnzymoPure™；from Trichoderma viride，≥20,000U/g，powder | Hydrolase | Fiber degradation; industrial pretreatment | |
Cellulase from Aspergillus sp. | Bioactive；ActiBioPure™；High Performance；EnzymoPure™；≥1000 U/g liquid | Hydrolase | Liquid enzyme formulations; biomass saccharification | |
Cellulase from Trichoderma reesei | aqueous solution,≥700 units/g | Hydrolase | Lignocellulose saccharification; pre-fermentation pretreatment | |
α-Amylase | Bioactive；ActiBioPure™；High Performance；EnzymoPure™；≥135 KNU/g；from Bacillus licheniformis | Hydrolase | Starch liquefaction; high-temperature processing | |
Amylase | EnzymoPure™；480 KNU-B/g | Hydrolase | Bulk starch liquefaction | |
Thermostable α-amylase from Bacillus licheniformis | EnzymoPure™；≥20000 U/mL | Hydrolase | Thermostable starch conversion; continuous processing | |
α-Amylase from Bacillus sp. | EnzymoPure™；≥300 units/g | Hydrolase | Raw material pretreatment; starch processing | |
α-Amylase from Bacillus amyloliquefaciens | EnzymoPure™；liquid，≥250 units/g | Hydrolase | Starch liquefaction; food and fermentation industries | |
Glucose Isomerase from Streptomyces murinus | EnzymoPure™；≥350 U/g | Isomerase | High-fructose syrup production; sugar isomerization | |
Aldolase from rabbit muscle (Suspension) | EnzymoPure™；≥10 units/mg protein，10-45 mg protein/mL | Lyase | C-C bond construction; synthesis of complex molecular scaffolds |
The core value of biocatalysis and industrial enzymology lies in establishing an integrated application system centered on enzymes, spanning molecular recognition, catalytic transformation, and process manufacturing. With the continued convergence of enzyme discovery, enzyme engineering, immobilization technologies, continuous reaction systems, and digital design, industrial enzymology is evolving from a local process-optimization tool into an important technological platform for highly selective, low-carbon, and high-precision manufacturing.
For more related articles, please see below:
[1] EnzymoPure™: Excellence in Enzymatic Solutions for Biological and Chemical Industries
[2] Glucose Oxidase: A Versatile Biocatalyst Across Multiple Fields