| HS Code | 415681 |
| Product Name | Beta-Glucosidase Glycanase |
| Enzyme Type | Beta-glucosidase / glycanase complex |
| Source | Typically derived from Aspergillus niger or Trichoderma reesei |
| Ec Number | EC 3.2.1.21 |
| Molecular Weight | Approximately 100-150 kDa |
| Optimal Ph | 4.5-5.5 |
| Optimal Temperature | 50-60°C |
| Substrate | Beta-1,4 glycosidic linkages in cellulose and other beta-glucans |
| Specificity | Hydrolyzes terminal non-reducing beta-D-glucose residues with release of beta-D-glucose |
| Activity Unit | Defined as one unit liberating 1 micromole of glucose per minute under assay conditions |
| Solubility | Readily soluble in water and aqueous buffers |
| Storage Conditions | Store at 4°C; avoid repeated freeze-thaw cycles |
| Typical Inhibitors | Gluconolactone, high concentrations of glucose, and heavy metal ions |
| Applications | Degradation of cellulose, plant cell wall modification, juice clarification, and biofuel production |
As an accredited Beta-Glucosidase Glycanase factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Beta-Glucosidase Glycanase is packaged in a sealed amber glass bottle with a tamper-evident cap, containing 100 mL. |
| Container Loading (20′ FCL) | One 20-foot container loaded with Beta-Glucosidase Glycanase, properly packed, secured, and documented for safe transport. |
| Shipping | Ship Beta-Glucosidase Glycanase refrigerated (2–8°C) or frozen, depending on formulation, using insulated packaging with ice packs or dry ice. Ensure leak-proof vials, absorbent material, and clear biological/enzyme labeling. Protect from heat, light, and physical damage. Include safety data sheet and temperature indicator for compliance. |
| Storage | Beta-Glucosidase Glycanase, an enzyme, should be stored under refrigeration at 2–8°C. Keep the container tightly closed and desiccated to prevent moisture uptake. For long-term stability, store at -20°C in single-use aliquots, minimizing freeze-thaw cycles. Protect from exposure to high temperatures and direct sunlight. Always handle with clean utensils and adhere to the supplier's specific storage recommendations to preserve enzymatic activity. |
| Shelf Life | Beta-Glucosidase Glycanase remains stable for up to 12 months when stored at -20°C; avoid repeated freeze-thaw cycles. |
In dilute acid-pretreated lignocellulosic feedstocks, cellobiose accumulation above 25 g/L exerts feedback inhibition on endo-cellulase activity, and β-glucosidase activity becomes rate-limiting once water-insoluble solids exceed 10%. In a 200,000 L horizontal saccharification vessel using a helical impeller at 15–20% dry matter, pH 4.8–5.2, and 48–52 °C, untreated hydrolysis may retain 28–42 g/L cellobiose after 72 h. The glycanase fraction cleaves β-1,4 and β-1,3 mixed-linkage bonds, reducing apparent slurry viscosity from approximately 3,500 mPa·s to 1,200 mPa·s at 20% solids over 24 h; torque reduction on 45 kW drive motors is observed, but published data for this specific configuration is limited. Compliance reference: NREL/TP-510-42628 for enzymatic saccharification and ASTM D4806-20a for denatured fuel ethanol.
Addition ratio is 0.03–0.08 wt% of dry biomass, equivalent to 0.4–1.2 L/t slurry. Typical activity ranges are 200–350 U/g β-glucosidase by pNPG assay at pH 5.0 and 50 °C, and 700–1,200 U/g glycanase on barley β-glucan substrate. Enzyme is injected after neutralization with aqueous ammonia and cooling to 48–52 °C because residual acetic acid above 5 g/L suppresses β-glucosidase activity. The neutralized slurry enters a static mixer before the first saccharification stage, then simultaneous saccharification and fermentation proceeds in a 500,000 L jacketed stirred fermenter with Saccharomyces cerevisiae at 72–96 h residence. Terminal product types include denatured fuel ethanol under ASTM D4806-20a and cellulosic glucose syrup for organic acid fermentation. The enzyme loses more than 50% activity above 68 °C or below pH 3.8; dosing before pH 4.8 or into unneutralized acid hydrolysate is not recommended.
The glycosylated monoterpene fraction in white must remains olfactorily inactive until β-glucosidase cleaves the β-D-glucopyranoside linkage to release linalool, geraniol, nerol, and α-terpineol. The glycanase fraction hydrolyzes grape berry cell wall β-glucans after crushing, raising free-run recovery by 3–8% and reducing lees viscosity. In clarified white juice, the addition rate is 2–5 g/hL after first racking with contact of 48 h–14 days at 12–18 °C. In red prefermentation cold soak, the rate is 3–6 g/hL at 8–12 °C for 36–72 h. Compliance framework: Commission Delegated Regulation (EU) 2019/934 for oenological processing aids and JECFA General Specifications for Enzyme Preparations. Batch-to-batch variance in free-run aromatic intensity is observed with grape maturity, skin contact time, and endogenous glycosidase load.
Destemmed grapes are fed to a pneumatic press at 0.6–1.0 bar; red must passes through a tube-in-shell chiller to 8–12 °C, and enzyme is injected by peristaltic pump into the crusher discharge line. Cap management is performed every 6 h during cold soak. White juice is clarified with 0.3–0.8 g/L bentonite, and enzyme is dosed after bentonite racking because simultaneous addition binds protein and lowers activity. Glucose above 20 g/L inhibits β-glucosidase; red wine dosing is therefore preferred post-fermentation, or juice is processed before sugar accumulation. Avoid simultaneous addition with charcoal-based fining agents. Terminal product types: aromatic still wine, must concentrate, and de-aromatized juice for blending.
| Downstream segment | Compliance reference | Analytical or process test method |
|---|---|---|
| Cellulosic ethanol and lignocellulosic sugar platform | NREL/TP-510-42628; ASTM D4806-20a | pNPG β-glucosidase assay at pH 5.0, 50 °C; DNS reducing-sugar assay |
| Wine and aromatic must processing | Commission Delegated Regulation (EU) 2019/934; JECFA General Specifications for Enzyme Preparations | Activity reporting under OIV Code of Oenological Practice; free monoterpene recovery by GC-MS |
| Barley/rye animal feed | Regulation (EU) 1831/2003; AAFCO Official Publication 2024 | Pelleted feed recovery by viscometric method after feed extraction |
| High-adjunct brewing | ASBC Wort-18; EBC 4.16.1 | Wort β-glucan by Calcofluor flow injection analysis |
| Oat β-glucan hydrolysate | AOAC 995.16; ISO 16128-2:2017 | HPSEC molecular weight distribution; total β-glucan content |
| Soy isoflavone aglycone | 21 CFR 111; USP Soy Isoflavones monograph | HPLC aglycone profile for genistein, daidzein, glycitein |
In poultry and swine diets containing 30–60% barley or 15–30% rye, soluble mixed-linkage β-glucan raises digesta viscosity and impairs nutrient absorption in the jejunum. Beta-Glucosidase Glycanase is applied at 0.1–0.3 kg/t complete feed as a dry granular formulation, or 0.05–0.15 L/t as liquid post-pelleting. Compliance reference: Regulation (EU) 1831/2003 zootechnical additive category and AAFCO Official Publication 2024 enzyme ingredient definitions. Downstream process: hammer milling through a 3 mm screen, conditioning at 70–85 °C for 20–40 s, pelleting through a 2.5–4.0 mm die; liquid enzyme is sprayed onto cooled pellets with 2–5% fat coating if die temperature exceeds 85 °C. Dry granular batches stored above 35 °C or above 12% moisture lose 15–30% activity within 90 days. Terminal product types: pelleted broiler rations, layer mash, and piglet creep feed based on barley or rye.
Mashing with 30–45% raw barley or unmalted barley adjunct generates wort β-glucan concentrations above 300 mg/L, increasing lauter differential pressure and slowing runoff below 2.0 L/m²/min. Beta-Glucosidase Glycanase is dosed at 0.02–0.06% of total grist mass, equivalent to 2–6 g/hL. The mash schedule is 50 °C for 20 min for β-glucan solubilization, 63 °C for 45 min, and 72 °C for 30 min at pH 5.2–5.6. Equipment: lauter tun with 3–4 mm mill gap, rake speed 0.5–1.0 rpm, and runoff 2–3 L/m²/min. Compliance reference: ASBC Wort-18 and EBC 4.16.1 for wort β-glucan quantification; enzyme preparation meets JECFA General Specifications for Enzyme Preparations. The β-glucosidase component releases glucose from oligomeric glucosides and may raise apparent attenuation by 1–3%, requiring adjusted grist bills in high-gravity lager production. Terminal product types: high-gravity lager wort, ale wort, and reduced-viscosity spent grain streams. Dosage above 0.08% over-degrades β-glucan and reduces mouthfeel; avoid pH below 5.0 and temperature above 75 °C for more than 30 min.
| Downstream segment | Addition ratio | Process window | Residence time | Terminal product type |
|---|---|---|---|---|
| Cellulosic ethanol / lignocellulosic sugar | 0.03–0.08 wt% dry biomass | 48–52 °C, pH 4.8–5.2 | 72–120 h | Fuel ethanol; cellulosic glucose syrup |
| Wine and aromatic must | 2–5 g/hL white; 3–6 g/hL red | 8–18 °C | 36 h–14 days | Aromatic still wine; must concentrate |
| Barley/rye animal feed | 0.1–0.3 kg/t dry; 0.05–0.15 L/t liquid | 70–85 °C conditioning | 20–40 s conditioning | Pelleted broiler feed; piglet creep feed |
| High-adjunct brewing | 0.02–0.06% grist mass | 50–72 °C, pH 5.2–5.6 | 95 min total mash | High-gravity lager wort; ale wort |
| Oat β-glucan hydrolysate | 0.05–0.2% dry oat bran | 50–55 °C, pH 5.8–6.5 | 60–120 min | β-glucan hydrolysate powder; cosmetic humectant |
| Soy isoflavone aglycone | 0.05–0.25% dry substrate | 48–52 °C, pH 5.0–5.5 | 40–90 min | Isoflavone aglycone concentrate; fermented soy extract |
At 6–10% solids in an oat bran slurry at pH 5.8–6.5, the glycanase fraction reduces oat β-glucan molecular weight from native 2,000–3,000 kDa to 40–200 kDa, producing a clear heat-stable hydrolysate. Addition ratio is 0.05–0.2% of dry oat bran mass, equivalent to 0.5–2.0 L/t dry bran. Downstream process: jacketed shear mixer at 50–55 °C for 60–120 min, inactivation at 90 °C for 10 min, scroll decanter centrifugation, 10 kDa ultrafiltration, and spray drying at inlet 170–190 °C and outlet 80–90 °C with maltodextrin carrier. Compliance reference: AOAC 995.16 for β-glucan content; ISO 16128-2:2017 for natural origin index in cosmetic ingredients; JECFA General Specifications for Enzyme Preparations for food-grade enzyme. Terminal product types: oat β-glucan hydrolysate powder for nutraceutical soluble fiber, cosmetic humectant solution, and clear oat beverage stabilizer. Dosages above 0.3% or hydrolysis beyond 180 min push the molecular weight below 10 kDa, and if free glucose exceeds 5% of dry weight, Maillard browning during spray drying increases. Published data for the exact molecular weight distribution at this pilot configuration is limited.
Soy isoflavone aglycone production via enzymatic glycoside cleavage replaces solvent-intensive acid hydrolysis in defatted soybean meal and isoflavone concentrate. The enzyme hydrolyzes genistin, daidzin, and glycitin to genistein, daidzein, and glycitein, while the glycanase fraction degrades β-glucan in cotyledon cell walls to release bound glycosides. Addition ratio is 0.05–0.25% of dry substrate, equivalent to 0.5–2.5 kg/t. Downstream process: defatted soybean meal is slurried at 10–15% solids, pH adjusted to 5.0–5.5 with food-grade citric acid, heated to 48–52 °C in a 10,000 L agitated stainless steel vessel, and held for 40–90 min. Inactivation is conducted at 85 °C for 10 min, followed by filtration and drying. Compliance reference: dietary supplement ingredient manufacture under 21 CFR 111, specification testing under the USP Soy Isoflavones monograph, and enzyme preparation under JECFA General Specifications for Enzyme Preparations. Terminal product types: isoflavone aglycone concentrates standardized to 20–40% total aglycones, fermented soy extracts, and defatted soy ingredients with reduced glycoside load. Batch-to-batch variance in endogenous glycoside distribution requires residence-time revalidation. Avoid pH below 4.5 or above 7.0, where β-glucosidase activity falls by 40–60%; do not combine with residual organic solvent extraction systems without complete phase separation, as enzyme denatures at the solvent interface.
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A dual-activity enzyme preparation designated β-Glucosidase Glycanase is supplied as model BGX-500L in liquid concentrate form and as model BGX-50P in freeze-dried powder form. The liquid preparation is standardized at a density of 1.10–1.20 g/cm³ at 20 °C and an as-supplied pH of 4.0–5.0. β-Glucosidase activity (EC 3.2.1.21) is determined by p-nitrophenyl-β-D-glucopyranoside hydrolysis at 50 °C and pH 5.0. Glycanase activity is determined against barley β-glucan at 50 °C and pH 5.5. The liquid product is filtered through a 0.2 µm membrane and is supplied with lot-specific certificates of analysis reporting activity, protein content, pH, and microbial load. The formulation combines cellobiose-hydrolyzing capacity with endo-β-glucanase activity for processes in which soluble β-glucan viscosity and cellobiose inhibition occur simultaneously.
| Parameter | Test method | Specification |
|---|---|---|
| β-Glucosidase activity | pNPG hydrolysis, 50 °C, pH 5.0 | ≥ 500 U/mL |
| Glycanase activity | Barley β-glucan hydrolysis, 50 °C, pH 5.5 | ≥ 1000 U/mL |
| Filter-paper cellulase side activity | Filter-paper assay | ≤ 50 FPU/mL |
| Protein content | Bradford method | 25–60 g/L |
| Total viable count | ISO 4833-1:2013 | ≤ 5 × 10³ CFU/g |
| Salmonella | ISO 6579-1:2017 | Absent in 25 g |
| Enterobacteriaceae | ISO 21528-2:2017 | Absent in 1 g |
| Heavy metals as Pb | Ph. Eur. 2.4.8 | ≤ 10 mg/kg |
| Density | ASTM D891-18 | 1.10–1.20 g/cm³ |
| pH | ISO 10523 | 4.0–5.0 |
| Shelf life, sealed at 4 °C | Accelerated stability | ≥ 90% initial activity at 12 months |
In lignocellulosic hydrolysis at solids loadings above 15% w/w dry matter, cellobiose concentrations above 5–10 g/L suppress endoglucanase turnover through competitive inhibition. The β-glucosidase component converts cellobiose to 2 mol glucose per mole of cellobiose, reducing this inhibition and increasing volumetric glucose productivity. The glycanase component hydrolyzes mixed-linkage β-glucan fractions that form high-viscosity gels in pretreated corn stover, wheat straw, and barley husk slurries. In high-solids reactors with pitched-blade impellers operating at 80–120 rpm, the viscosity reduction depends on feedstock type, pretreatment severity, and particle size distribution. The product is therefore used where simultaneous cellobiose control and β-glucan depolymerization are required, rather than in systems with only one of these constraints.
When the liquid preparation is added to a simultaneous saccharification and fermentation process, the dosing point is placed downstream of temperature conditioning at 50–55 °C for initial saccharification before yeast inoculation at 30–35 °C. The β-glucosidase component continues to hydrolyze cellobiose during fermentation, while ethanol accumulation above 15% v/v progressively reduces enzyme activity. The glycanase component lowers viscosity during the initial high-temperature hydrolysis phase, improving heat transfer and mixing in jacketed fermentors. A starting dose of 0.05–0.20% v/w liquid product is evaluated based on initial β-glucan content and the target glucose release rate. Because batch-to-batch feedstock variance is significant, dose adjustment is performed by measuring β-glucan content and glucose yield after a 4 h hydrolysis check. Published data for this specific enzyme blend in all feedstocks is limited; validation on the actual feedstock lot is required before full-scale use.
For barley-derived process streams in brewing and cereal-based fermentation, β-glucan gel formation reduces lautering flux and increases pressure differentials in mash filters. The endo-β-glucanase component depolymerizes mixed-linkage β-glucan, lowering wort viscosity and reducing filter bed compaction. The β-glucosidase component also hydrolyzes short-chain β-glucosides arising from starch and oligosaccharide degradation. Dosing is typically performed at the start of mashing at 45–55 °C, and the enzyme remains active through the early saccharification rest. In wine and fruit juice processing, β-glucosidase activity can release glycosidically bound aroma precursors at pH 3.5–5.0, but the glycanase component may require removal by bentonite fining or 0.45 µm crossflow filtration to avoid haze in the finished beverage.
The operational envelope is constrained by pH and temperature limits that must be observed to prevent irreversible denaturation. Below pH 3.5, the β-glucosidase component loses more than 50% of initial activity within 24 h; the glycanase component is similarly acid-labile under prolonged exposure. Above pH 6.5, activity loss is slower but glucose yield can be reduced by non-enzymatic alkaline degradation reactions. The liquid product should not be heated above 65 °C; at 70 °C, the β-glucosidase component exhibits a half-life below 30 min in buffer systems. The powder formulation requires storage at ≤ 4 °C and handling at relative humidity below 60% to avoid caking. Enzyme preparations of this type are incompatible with strong oxidants and cationic flocculants; residual cationic polymers in process water can precipitate enzyme protein and reduce filter flux.
A single-activity β-glucosidase product supplies cellobiose conversion capacity but does not reduce soluble β-glucan viscosity. In high-molecular-weight β-glucan streams above 1% w/w, viscosity remains high enough to restrict oxygen transfer and impeller mixing even when cellobiose is fully converted. Crude cellulase mixtures often contain β-glucosidase as a minor component, frequently less than 10% of total cellulase activity, creating a kinetic imbalance: endoglucanase and exoglucanase generate cellobiose faster than β-glucosidase can convert it, leading to accumulation. This product is differentiated by the specified ratio of β-glucosidase to glycanase activity and by the absence of significant protease or lipase side activities. The liquid formulation is heat-filtered for beverage applications, whereas many crude cellulase preparations are not clarified to food-grade microbial specifications.
| Characteristic | β-Glucosidase Glycanase BGX-500L | Single β-glucosidase | Crude cellulase |
|---|---|---|---|
| β-Glucosidase activity | ≥ 500 U/mL | High | Low or variable |
| Endo-β-glucanase activity | ≥ 1000 U/mL | Absent or low | Present |
| Cellobiose conversion capacity | High | High | Often insufficient |
| Viscosity reduction in β-glucan-containing streams | Present | Absent | Variable |
| Typical pH range | 4.0–6.0 | 4.0–6.0 | 3.5–5.5 |
| Clarified preparation for beverage filtration | 0.2 µm filtered | May require additional filtration | May require additional purification |
| Storage form | Liquid or powder | Liquid or powder | Liquid or powder |
In enzyme process validation, the preparation should be assessed against FDA 21 CFR 173.120 for food-contact enzyme preparations and against applicable REACH registration requirements in the jurisdiction of use. The liquid product is not classified as hazardous under CLP regulations, but spill containment and skin protection should follow standard enzyme hygiene procedures because dry enzyme proteins can cause respiratory sensitization if aerosolized. Process-scale trials should confirm that the product activity remains within specification after 24 h at the target process temperature and that glucose release does not create osmotic inhibition in downstream fermentation. The preparation is not suitable for direct addition to untreated slurries above 70 °C, to systems containing cationic flocculants, or to processes requiring activity at pH below 3.5 for extended periods.
