Cellobiase, also known as β-glucosidase, belongs to the enzyme family responsible for catalyzing the hydrolysis of glycosidic bonds. These bonds split cellobiose and similar sugars into two glucose molecules. Extraction usually comes through microbial fermentation or plant tissue, with the enzyme presenting as a solid powder, flakes, or crystalline form, depending on purification and storage process. The molecular formula registers as C6H11NO4, aligning with its protein nature. Structural analysis points to both alpha-helix and beta-sheet patterns, which stabilize the enzyme in a folded state.
Cellobiase works at optimal temperatures ranging between 35°C and 40°C, although some preparations show broader tolerance, especially those designed for industrial use. Molecular weight lands near 60,000 Da, but this varies across manufacturer-specific production lines. The enzyme measures out as a dense powder, holding a density around 1.35 g/cm³, typical for pure protein crystals. Solubility in water comes with ease at physiological pH, making the enzyme practical for aqueous solutions or blending with buffer systems. The pH optimum places activity greatest between 5.0 and 6.0, reflecting a familiar trend across β-glucosidases. Density and solid-state behavior matter when incorporating cellobiase into solutions or mixing with other raw ingredients, especially in food or biofuel processing sectors. Hazard data shows low acute toxicity; exposure through inhalation or ingestion is generally not harmful, but sustained contact may lead to irritation in sensitive individuals, especially when the enzyme is in fine particulate form.
Once crystallized, cellobiase forms needle-like or rhomboid shapes under microscope analysis. Moisture content in the raw powder sits below 5% to maintain enzyme integrity during storage. Solid flakes ease transportation, while a crystalline state prolongs shelf life and resists breakdown from atmospheric factors. Pure material melts at elevated temperatures but loses catalytic function well below its melting point. Liquid formulations, prepared by dissolving in phosphate or citrate buffer, facilitate dosing for lab or industrial reactor scale. As with most proteins, denaturation can follow prolonged heat or chemical exposure, demanding storage at -20°C or below in freeze-dried forms.
Use in biofuel production, food technology, and biochemical research places big importance on purity specs and contaminant limitation in the finished material. Manufacturers supply batch-specific data sheets showing activity units per gram, detailed contaminant analysis, and recommended handling precautions. The enzyme itself rarely appears as a hazardous chemical under REACH or OSHA guidelines, and its HS code—3507.90—matches enzymes prepared for industrial application. Packing varies from small vials for lab use to multi-kilogram drums for large plants, each labeled with molecular formula, batch number, and disposal recommendations. Safe practice calls for gloves, eye protection, and dust masks during handling, but cellobiase does not hold the same risks as many industrial chemicals.
Raw material sourcing leans on microbial fermentation, mainly Aspergillus niger and Trichoderma reesei, with synthetic biology pushing the boundaries for greater yield and purity. Upstream processing covers sterilized sugar substrates, bioreactor controls, and careful downstream protein extraction. Purity measures through SDS-PAGE and chromatography determine final product grade, while enzyme activity—usually over 100 U/mg for pure preparations—suggests robust catalytic strength. Every production lot faces scrutiny for bacterial endotoxins, heavy metals, and microbial contaminants, tying into global safety mandates. Final packaging arrives with full specification sheets, keeping information clear for both regulatory and user review.