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HS Code |
998544 |
| Product Name | Chymotrypsin |
| Enzyme Class | Serine protease |
| Ec Number | 3.4.21.1 |
| Cas Number | 9004-07-3 |
| Source | Bovine pancreas |
| Activity Optimum Ph | 7.8-8.0 |
| Molecular Weight | 25 kDa |
| Substrate Specificity | Cleaves peptide bonds on the carboxyl side of aromatic amino acids |
| Form | Lyophilized powder |
| Storage Temperature | -20°C |
| Solubility | Soluble in water or buffer |
| Inhibitors | Serine protease inhibitors (e.g., PMSF) |
| Unit Definition | One unit hydrolyzes 1 µmol of substrate per minute at pH 7.8 and 25°C |
| Applications | Protein digestion, peptide mapping, cell dissociation |
| Stability | Stable for months when stored properly |
As an accredited Chymotrypsin factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Chymotrypsin is supplied in a sealed amber glass vial containing 100 mg, clearly labeled with product details, storage instructions, and hazard warnings. |
| Shipping | Chymotrypsin is shipped as a lyophilized powder or frozen solution, packaged in tightly sealed containers, and transported under temperature-controlled conditions (usually refrigerated or with ice packs) to preserve enzyme stability and activity. All shipments comply with applicable regulations for biological materials and include proper labeling and documentation for safe handling. |
| Storage | Chymotrypsin should be stored at -20°C in a tightly sealed container, protected from moisture and light. If supplied as a lyophilized powder, it should be reconstituted with cold buffer or water just before use. For short-term storage of liquid solutions, keep at 2–8°C. Avoid repeated freeze-thaw cycles to maintain enzyme activity and stability. |
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Purity 99%: Chymotrypsin Purity 99% is used in enzymatic protein hydrolysis, where it ensures high-efficiency peptide bond cleavage and minimal contaminant introduction. Activity 1000 USP units/mg: Chymotrypsin Activity 1000 USP units/mg is used in cell culture media digestion, where it provides rapid and precise cell dissociation for reproducible downstream analysis. Molecular Weight 25.7 kDa: Chymotrypsin Molecular Weight 25.7 kDa is used in pharmaceutical intermediate processing, where it enables selective substrate targeting for accurate bioactive compound modification. pH Stability Range 7.0–9.0: Chymotrypsin pH Stability Range 7.0–9.0 is used in biomedical research protocols, where it maintains optimal catalytic activity for consistent experimental results. Endotoxin Level <0.1 EU/mg: Chymotrypsin Endotoxin Level <0.1 EU/mg is used in therapeutic protein purification, where it reduces immunogenic risks and supports clinical safety requirements. Storage Temperature -20°C: Chymotrypsin Storage Temperature -20°C is used in long-term reagent preservation, where it retains enzymatic potency and prevents degradation. Particle Size <50 µm: Chymotrypsin Particle Size <50 µm is used in industrial-scale peptide synthesis, where it allows uniform dispersion and accelerates substrate conversion rates. |
Competitive Chymotrypsin prices that fit your budget—flexible terms and customized quotes for every order.
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Working in a factory that specializes in producing enzymes like chymotrypsin gives us a firsthand understanding of both the technical side and the demands from laboratories, pharmaceutical companies, and biotech research. Chymotrypsin comes from bovine pancreas and falls under the category of serine proteases, known for breaking down proteins into smaller peptides and amino acids. Over time, our process has improved, not just in extraction and purification, but in honing the qualities that set our product apart for those who need consistency and reliability.
Years of research and adapting to feedback from end users have taught us that purity, specific activity, and batch consistency often matter more to scientists and manufacturers than generic statements about grade. Some factories produce enzyme powder and don’t look back, but here, we monitor every batch from the raw pancreas tissue through to the final vacuum-dried product. This approach means our chymotrypsin exhibits low trypsin contamination, stable activity measurements, and a color that reflects minimal oxidized impurities—results of a well-controlled crystallization and drying process.
In performance, our chymotrypsin typically delivers specific activity greater than 60 units/mg protein (measured against standard synthetic substrates and supported by documentation from every lot). Clients trust these numbers, because analysis—done in our in-house QC labs—matches results independently confirmed by large pharmaceutical groups. Unlike more commodity-grade preparations, these specifications are upheld without selling on mere price or cutting corners with chemical stabilizers that can interfere with sensitive reactions.
Most requests we receive focus on biopharmaceutical use, tissue dissociation, and peptide mapping. For these fields, end users demand an enzyme free from unwanted proteases, preservatives, or pyrogens. Instead of marketing chymotrypsin as a general protease, we provide detailed profiles so researchers know what they’re getting. In practical terms, enzyme purification steps involve differential salt precipitation, careful selection of buffer pH, and repeated ultrafiltration cycles. Technicians test residues at each stage, keeping contamination low and producing a crystalline powder that reconstitutes cleanly in buffered solutions.
Protein sequencing laboratories choose our chymotrypsin when accurate cleavage at aromatic residues (like tyrosine, phenylalanine, and tryptophan) is essential. Compared to trypsin or pepsin, chymotrypsin cuts at fewer sites, creating predictable peptide fragments that simplify mass spectrometry workflows. We hear from academic groups that less consistent preparations can introduce missed cleavages or extra cuts, leading to data ambiguity. The familiarity with our batches comes from long-standing relationships and feedback cycles that go back years.
Having control over the upstream process means we react quickly to any deviations—cloudy solutions during filtration, unexplained drops in activity, or minor shifts in isoenzyme ratios. Plant managers, technicians, and qc analysts work on-site, sharing reports daily with production teams. This hands-on system is different from larger bulk operations that blend finished powders from various sources to meet quota. For us, even a single batch showing reduced solubility or off-odor results in re-processing rather than pushing out substandard material. High cost comes with this philosophy, but so does higher reproducibility and fewer returned lots.
Some suppliers sell “blended” enzymes, containing a mixture of proteases topped up with stabilizers. End-users often only realize after failed reactions. In our operation, chymotrypsin stays single-activity, meaning only one major protease function shows up on electrophoresis gels or HPLC. Where possible, protease activity against non-target residues stays below detection. Typical finished powder contains minimal moisture, and the color reflects both the starting pancreas quality and delicate handling. Each drum is nitrogen flushed and vacuum sealed to prevent moisture and microbial exposure.
Injectables, wound debridement treatments, and enzyme supplements rely on strict standards for purity, pyrogen content, and solvent residue. Endotoxin tests using Limulus amebocyte lysate (LAL) kits flag any batch that doesn’t fit specification, and we run these checks every time new starting material is used. When clients bring up compliance, we’re able to show batch records, supply serialization, and retain samples for third-party testing. Regulatory files often require years of lot traceability, and this is only possible because we never source from intermediaries or unknown partners.
Most factories producing chymotrypsin for pharmaceutical use separate product lines for research versus therapeutic grade. Here, production lines for all grades share the same source material but diverge at the final cleaning and formulation stages. For API-grade, further endotoxin and residual solvent testing comes into play, followed by aseptic filling. Independent audits from client quality teams ensure the process matches their expectations, not just in paperwork but on-the-floor working habits. At one point, a major injectable producer flagged solvent traces in the final API material, which led us to re-engineer parts of our crystallization stage, cutting residuals by over 80 percent the following quarter.
We value open lines of communication with researchers. Many ask for samples before committing to bulk, so they can test performance in tissue culture or hydrolysis protocols. If feedback indicates unusual cleavage patterns or lower yields in standard digest panels, we take the data and re-examine our purification steps. Recently, after several labs flagged a shift in optimum pH curve, process engineers collaborated with QC staff to rein in a minor shift in buffer composition during final formulation. Rather than dismiss these reports, plant supervisors met directly with research users, examining protocol notes together. Only after these fixes did new batches leave the warehouse.
In terms of product forms, both powder and crystalline types leave the factory, depending on the buyer’s needs. Crystalline chymotrypsin, prized in sequencing and pharmaceutical work, takes more rounds of refinement, careful solvent precipitation, and microfiltration. Lyophilized powder, on the other hand, caters more to industrial hydrolysis and secondary research applications, where production scale and storage life take precedence over the highest purity. Users know exactly what to expect, because every shipment leaves with a batch-specific certificate that spells out enzyme activity, protein content, and contaminant levels.
Managing a chymotrypsin facility brings up plenty of daily challenges: sourcing sufficient high-quality pancreas, keeping batch schedules synchronized, and ensuring operators follow cleaning routines without shortcuts. Cross-contamination concerns mean strict segregation of workstations, and the equipment receives daily cleaning-in-place cycles using validated detergents. We train teams to recognize early signs of bacterial growth or material spoilage and to spot deviations fast. These routines keep our chymotrypsin batches free from detectable microbiological contamination and maintain the expected stability profile for at least two years under recommended storage.
Our teams also address waste management from the extraction process—spent tissue, filtered liquids, wash water—and continually refine our approach to minimize the environmental footprint. By working with local processing partners and updating separation equipment, we have achieved measurable reductions in bioburden output and solvent waste. This not only ensures compliance with municipal disposal regulations but supports a culture of accountability and continuous improvement.
People often ask how chymotrypsin stacks up against other proteases, especially trypsin and pepsin. The active sites of these enzymes define what proteins and peptide bonds they cut best. Chymotrypsin prefers cleaving after aromatic amino acids, producing fewer, more predictable peptides, which simplifies mapping proteins for mass spectrometry. Trypsin, by contrast, cleaves after positively charged residues, resulting in more, shorter peptides—good for different analytical purposes but not as ideal where clean separation of specific regions is needed.
In biological tissue dissociation, chymotrypsin causes less incidental damage to cell surface proteins compared to trypsin, which can be aggressive and non-selective. Stem cell researchers and primary cell isolation labs often request our chymotrypsin for this reason. Furthermore, it shows less endogenous inhibitor sensitivity than plant-derived proteases, supporting more robust performance under physiological pH and ionic strength conditions found in tissue culture and enzymatic research assays.
Compared against microbial-origin proteases, bovine chymotrypsin maintains higher compatibility with downstream therapeutic applications, since protein structure and glycosylation profiles more closely match human biological systems. This similarity supports trust in pharmaceutical developments that demand safety and traceability. Individuals relying on enzyme supplementation in clinical use report gentler absorption profiles, which aligns with what clinicians have shared after switching from less-specific blends.
Improvements never stop on the factory floor, because new analytical techniques and changes in upstream material quality challenge us season by season. Technicians work directly with production chemists to adapt purification steps and prevent batch-to-batch drift. Recently, adopting high-resolution chromatography for final purification shaved hours off the old gradient elution timelines, leading to improved throughput while maintaining sharp separation from unwanted protease isoforms. Each investment in equipment brings feedback from operators, who see first-hand whether machine upgrades deliver actual gains or simply complicate maintenance schedules.
Documentation and traceability play an equally important role. Every material lot receives a dedicated record from receiving through to shipping. During process validation, we invite third-party auditors to trace a random batch’s life cycle, from raw pancreas sourced from registered suppliers, through extraction, purification, lyophilization, labeling, and warehousing. Any deviations go into written reports, and findings contribute directly to training updates and process control points.
Each outgoing order means more than just shipping an enzyme in a sealed drum. Long-term clients depend on stable performance over years, not just one successful test batch. We receive phone calls about upcoming projects and changing research protocols, and our production managers listen in to clarify whether a new order needs adjusted purity or activity specifications. Only after all details find agreement does the production slot open—helping us avoid last-minute surprises or misdelivery. This system keeps our relationships strong and encourages customers to share constructive criticism.
Logistics teams adapt to varying shipping requirements, whether delivering to a biotech lab in a city center or a pharmaceutical manufacturing zone on another continent. Temperature control, short transit times, and customs paperwork receive close scrutiny for every movement. Any shipment that faces weather delays, lost paperwork, or customs hold-ups gets flagged for follow up. Feedback from logistics partners runs back to management, shaping packaging and route selection for future deliveries.
We work side-by-side with regulatory bodies on documentation, ensuring batches destined for drug manufacturing meet published monographs and pharmacopeia references. Our analytical lab cross-references USP guidelines, balancing those requirements with what customers in proteomics and research desire—meaning we tailor batch testing and documentation to both formal standards and real-world application. Regulatory audits and science-based feedback have led us to edge out avoidable impurities and share transparent records on outstanding lots.
We contribute data and expertise to industry working groups and cross-industry panels focused on enzyme use in pharmaceuticals and biotechnology. Open technical dialogue helps refine both expectations and standards. These exchanges support improvements in batch consistency, contaminant detection, and process optimization.
Decades of manufacturing have shown that enzyme production follows cycles—booms in demand for vaccine research, downturns due to policy change on animal-sourced materials, or sudden requests as new scientific protocols emerge. We have watched some companies try shortcutting supply chains with cheaper starting material or offsite third-party finishing, only to see buyers lose confidence after inconsistent performance. Our choice has been to maintain direct sourcing and in-house finishing, even under market pressures to cut lead times or offer rock-bottom prices.
Going forward, we are adapting to demands for animal-free alternatives by experimenting with recombinant chymotrypsin production via microbial fermentation and expression in yeast or bacterial strains. While these processes still lag the tradition on certain activity and stability points, the research team is closing the gap. We have already provided early-stage samples to key partners willing to pilot new batches under bio-equivalency evaluation, and so far the results seem promising, pointing in the direction of a sustainable supply future without animal derivatives.
Our ongoing investment in careful sourcing, strict process control, and labor-intensive purification pays off over the years because our customers see direct benefits—cleaner digestions, reproducible results, fewer failed lots, and straightforward regulatory compliance. Working inside the production lines has taught us to listen to both client needs and operator experience. This culture of continuous improvement means users get an enzyme that serves real-world research, clinical, and production environments without surprises or hidden compromises.
If you value a supplier that stands behind both science and the practical challenges behind it, experience with manufacturing chymotrypsin means we can help—whether you need a bulk order for bioprocessing or a custom batch for research applications. Our know-how, built on years of direct engagement with the product and its users, sets our chymotrypsin apart on lab bench and production line alike.