| HS Code | 155681 |
| Product Name | Beta-Glucanase |
| Enzyme Class | Hydrolase |
| Source | Aspergillus niger, Bacillus subtilis, Trichoderma reesei |
| Substrate | Beta-glucans (e.g., barley beta-glucan, oat beta-glucan) |
| Reaction Product | Glucose and oligosaccharides |
| Optimal Ph | 4.5 - 6.5 |
| Optimal Temperature | 40°C - 60°C |
| Molecular Weight | 20,000 - 45,000 Da |
| Activity Units | Defined as micromoles of reducing sugar released per minute |
| Form Available | Liquid, powder, or granulated |
| Applications | Animal feed, brewing, baking, juice processing, bioethanol production |
As an accredited Beta-Glucanase factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Beta-Glucanase is supplied in 25 kg sealed fiber drums with an inner polyethylene liner for safe handling. |
| Container Loading (20′ FCL) | Beta-Glucanase loaded in 20′ FCL container, packed on pallets, secured firmly, kept dry, ventilated, and protected from moisture and sunlight. |
| Shipping | Beta-Glucanase ships as a powder or liquid in sealed, labeled containers. Temperature-controlled packaging is often required to preserve enzyme activity. It is generally non-hazardous, but containers should remain dry and protected from extreme heat. Standard ground freight with proper documentation and handling guidelines is typically suitable. |
| Storage | Store Beta-Glucanase in a tightly sealed, light-resistant container at 2–8°C. For long-term stability, freeze at -20°C and avoid repeated freeze-thaw cycles. Keep dry and away from moisture, heat, and strong oxidizers. Under proper conditions, enzyme activity is generally maintained for extended periods. Always follow the manufacturer’s specific storage instructions. |
| Shelf Life | Beta-Glucanase has a typical shelf life of 12 months when stored sealed in a cool, dry place. |
In brewhouses operating with grist bills exceeding 25% unmalted barley or rye, mixed-linkage β-glucan concentrations above 3.5 g/100 g measured by EBC 4.16.1 routinely produce mash bed compaction and lautering pressure differentials above 180 mbar. Endo-1,3(4)-β-glucanase (EC 3.2.1.6) is added at 0.15–0.30 L of a 700 BGU/g liquid preparation per tonne of grist, either at mash-in or during the 48–55 °C glucan rest before saccharification at 62–72 °C. The enzyme is not effective when added after the α-amylase rest because activity declines sharply above 60 °C. On a 24 hL pilot brewhouse using a 1.8 m diameter lauter tun, untreated high-glucan mashes produce run-off velocities below 1.2 L/m²·min and require rake speed reductions, while treated mashes recover run-off velocity to 2.0–2.4 L/m²·min and shorten lautering from roughly 150 min to 95–110 min under matched loads. EU compliance is governed by Regulation (EC) No 1332/2008 for food enzymes, with wort β-glucan control referenced to EBC 4.16.1 and ASBC Wort-18. Terminal finished products include all-malt pilsner, high-adjunct lager, barrel-aged barleywine, and non-alcoholic beer requiring low residual β-glucan to prevent centrifuge sludge and flash-pasteurizer fouling.
Barley inclusion in broiler and swine formulations introduces intestinal digesta viscosity from mixed-linkage β-glucans, reducing contact between nutrients and mucosal enzymes. Commercial beta-glucanase concentrates standardized to 700–1,100 BGU/g are incorporated at 25–75 g/t complete feed, with the upper bound applied when barley or oats exceed 30% of the formulation. In the EU, the additive is regulated under Regulation (EC) No 1831/2003, Annex I, functional group 4a as a digestibility enhancer and evaluated under EFSA FEEDAP guidance; production sites supplying feed enzymes are audited against ISO/TS 22002-6:2016 for prerequisite programmes in feed and animal food production. In compound feed mills using a 3.0 mm ring-die pellet mill with conditioning at 82 °C for 45 s, unprotected liquid enzyme added before conditioning suffers recovery losses of 30–50%; therefore coated dry formulations or post-pelleting liquid application at 55–65 °C are employed for pelleted broiler grower feed. The enzyme acts in the proximal small intestine, but published data for specific ileal viscosity reductions on commercial lines are limited because barley cultivar β-glucan content varies between 2.5 g/100 g and 5.0 g/100 g. Terminal finished product types include crumbled broiler starter feed, pelleted grower-finisher feed, and swine weaner diets containing hulled barley; liquid post-pelleting application is preferred over dry premix inclusion to avoid enzyme segregation at low trace-mineral addition rates.
Where oat-based beverages are manufactured without viscosity reduction, soluble β-glucan concentrations of 3–5 g/100 g in oat flour create shear-thinning slurries with apparent viscosity above 300 mPa·s at 50 s⁻¹, blocking decanters and homogenizer feed valves. Beta-glucanase is applied as a processing aid in accordance with Regulation (EC) No 1332/2008 and the JECFA food enzyme monograph for endo-1,3(4)-β-glucanase, with residual enzyme removed or inactivated before final UHT treatment. The addition ratio is 0.01–0.05% w/w of dry oat mass, typically 0.02% for a 15–18 °Brix oat slurry held at 55–60 °C and pH 5.5–6.0 for 30–60 min. Production-scale systems use a continuous stirred-tank hydrolysis vessel before homogenization at 200–250 bar and UHT sterilization at 135–140 °C for 5 s. Terminal products include chilled oat drink, barista-format oat beverage, oat muesli concentrate, and neutral oat base for dairy analogue production. Over-hydrolysis to below 0.75 g/100 g β-glucan reduces the soluble fibre fraction associated with EFSA cholesterol-lowering health claim guidance and alters mouthfeel, establishing the upper dosage boundary.
Mechanistically, β-glucan hydrolysis prior to dough fermentation alters water distribution in barley- and oat-containing doughs, lowering dough resistance and permitting gas cell expansion during proofing. Addition rates of 10–80 ppm on flour weight are used when whole-grain barley flour exceeds 15–25% of the flour blend; the enzyme is co-dispersed in dough water at 25–30 °C before mixing rather than dry-blended into flour. Bakeries audited to FSSC 22000 Version 6 or BRCGS Food Safety Issue 9 handle the enzyme as a processing aid under EU Regulation (EC) No 1332/2008 or FDA GRAS status, with dough rheology controlled by farinograph per ISO 5530-1:2020 and extensograph per ISO 5530-2:2020. In spiral mixers operating at 60–80 rpm and dough temperatures of 26–28 °C, over-dosage above 100 ppm is associated with sticky dough and loss of pan flow because excessive glucan degradation releases bound water into the gluten phase. Terminal baked goods include high-fibre barley pan bread, oat sandwich bread, multigrain rolls, and frozen dough products; the enzyme is not required for refined wheat flour with β-glucan below 0.3 g/100 g.
At dry-grind ethanol plants receiving barley, rye, or frost-damaged wheat, mixed-linkage β-glucans increase whole stillage viscosity and reduce thin stillage recycling rates. Beta-glucanase is added at 0.20–0.45 L/t dry matter before the jet cooker, but when feedstock glucan exceeds 4.0 g/100 g, split addition—60% at slurry mixing and 40% after liquefaction—prevents high-temperature denaturation losses. Finished ethanol is tested under ASTM D4806-21a or EN 15376:2014 for denatured fuel ethanol, while distillers dried grains with solubles are controlled under feed safety schemes such as ISO/TS 22002-6:2016; enzyme handling and REACH compliance apply to the liquid concentrate. In a 200,000 L fermentor receiving 30% barley dry solids, untreated slurry viscosities above 2,000 cP at 32 °C restrict heat exchanger flow, whereas enzymatic treatment targets 800–1,200 cP. Terminal products are fuel ethanol, industrial ethanol, and distillers dried grains with solubles for ruminant rations; the enzyme operates before yeast propagation and is inactivated during distillation. Published data for specific thin stillage flux recovery in dry-grind barley vary by plant because recirculated thin stillage alters enzyme carryover and pH.
Crossflow filtration trials on botrytised and late-harvest white wines demonstrate that Botrytis cinerea releases high-molecular-weight β-glucan into the must, reducing flux and creating post-bottling haze risk. Liquid beta-glucanase approved under the OIV Code of Oenological Practices and EU Regulation (EC) No 606/2009 is added post-fermentation at 1–3 g/hL, after racking and before polishing filtration. The enzyme acts at wine pH 3.0–3.5 and cellar temperature 12–18 °C, though activity is lower than at optimal pH; wineries therefore extend contact time to 1–2 weeks and conduct a bench-top membrane filterability test before crossflow. Terminal products include Sauternes-style sweet white wine, late-harvest Riesling, and icewine. Published data for specific flux recovery on commercial lines is limited where glucan concentration is not measured uniformly.
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β-Glucanase is supplied as an endo-acting hydrolase assigned to EC 3.2.1.6, with auxiliary lichenase activity conforming to EC 3.2.1.73 where the product series is designated for oat-derived β-glucan. Representative model designations BG-750L and BG-250G identify the liquid food-grade concentrate and microgranulate feed-grade preparation, respectively. The liquid grade is standardized to a declared activity not less than 750 FBG/g when assayed by reducing-sugar method against barley β-glucan at pH 5.5 and 50 °C; the microgranulate grade is standardized to not less than 250 FBG/g under the same substrate conditions. One FBG unit is defined by the supplier as the enzyme quantity liberating 1 µmol of glucose equivalents per minute from barley β-glucan at pH 5.5 and 50 °C.
The preparation cleaves internal β-1,3 and β-1,4 glycosidic linkages in mixed-linkage glucans from barley, oats, and rye. It releases soluble oligosaccharides rather than free glucose, and the matrix contains no crystalline-cellulase or xylanase side activities above 5% of the reference β-glucanase activity under the defining assay.
Because β-glucanase activity units are not harmonized across suppliers, dose comparisons require identical substrate, blank correction, incubation time, and reducing-sugar detection. The FBG unit is not equivalent to xylanase units or carboxymethyl cellulose units used for cellulase products. A preparation with a high CMCase value may show low barley β-glucanase activity. For quality-control release, activity is measured in duplicate with a relative standard deviation below 5%.
Model selection between BG-750L and BG-250G is governed by process moisture tolerance and post-processing heat load. The liquid grade is metered into aqueous systems with a positive-displacement pump; the microgranulate is dispersed in dry mixes where liquid dosing is not available. The numerical difference in declared activity does not imply a proportional difference in specific activity; the liquid product contains diluents and stabilizers, while the microgranulate is a concentrated dry carrier matrix.
Product differentiation is based on glycosidic-linkage specificity rather than total viscosity-reducing effect. Table 1 provides relative substrate selectivities normalized to the primary substrate of each reference enzyme.
| Assay substrate | BG-750L | Xylanase reference | Cellulase complex reference |
|---|---|---|---|
| Barley β-glucan | 100% | ≤5% | ≤10% |
| Wheat arabinoxylan | ≤5% | 100% | ≤10% |
| Carboxymethyl cellulose | ≤10% | ≤5% | 100% |
| Crystalline cellulose | ≤1% | ≤1% | 40–80% |
| Malt starch | not detected | not detected | not detected unless amylase side activity is present |
Cellulase complexes contain endo-1,4-β-glucanase, cellobiohydrolase, and β-glucosidase components that degrade crystalline cellulose and release glucose or cellobiose. β-Glucanase does not generate glucose from malt starch or β-glucan at measurable levels under AACC 32-23 detection. Xylanase preparations reduce viscosity from wheat or rye arabinoxylan but have little effect on barley β-glucan. Consequently, β-glucanase is selected for high-barley and undermodified-malt grists, whereas xylanase or combined products are applied in wheat-heavy grists. Misapplication of a cellulase-dominated blend to a barley mash can generate cellulose-derived fine particles and may increase filter-bed packing variability.
β-Glucanase is not β-glucosidase; it does not efficiently cleave terminal glucose from cellobiose or short β-oligosaccharides. Complete saccharification of β-glucan to glucose therefore requires β-glucosidase supplementation, particularly in bioethanol applications that demand fermentable glucose recovery from barley-derived streams.
Application in mashing is typically at 0.1–0.5 L/t of dry grist for BG-750L, with the upper end reserved for grists containing more than 2.5 mg/g malt β-glucan. The enzyme is dosed into mash-in water before grain addition to avoid localized gel formation. In a 100 hL lauter tun with a raking control system, a mash viscosity above 1.8 mPa·s at 20 °C is associated with runoff times exceeding 180 min; supplier brewhouse trial summaries report that 0.3 L/t reduces viscosity to approximately 1.5 mPa·s and cuts runoff time below 120 min for a uniformly milled grist. These results are not linear across all grists because mill gap, polyphenol load, and lauter bed height alter filter resistance.
For high-gravity brewing above 18 °P, the dose may be increased to 0.5–0.6 L/t, but only after dose-response testing. Excessive β-glucanase can produce low-molecular-weight glucan fragments that increase wort turbidity if not fully filtered. The enzyme should be added before the saccharification rest; mesophilic fungal β-glucanase loses measurable activity above 65 °C, so addition during kettle boil is ineffective.
β-Glucan values in Congress wort above 250 mg/L are commonly used as a critical process indicator for barley malt filtration performance, though the exact threshold varies with malt variety and mill type. The measurement follows ASBC Wort-18 for β-glucan by enzymatic hydrolysis or AACC 32-23 for β-glucan in grain. Above this concentration, β-glucan can form a gel-like network during wort cooling that blocks lauter screens and requires increased raking. Production-scale variability occurs because β-glucan is not distributed uniformly through the mash; undermodified areas release more glucan and produce local viscosity gradients.
The enzyme effect is most reproducible when mashing-in temperature is held at 45–50 °C for 15–20 min before the saccharification rest, allowing cleavage before starch gelatinization increases medium viscosity. Published data for specific lauter tun configurations is limited for the upper threshold above 300 mg/L, where filtration aids or grist blending may be required instead of enzyme dosing alone.
Feed-grade BG-250G is intended for barley- and oat-containing poultry and swine diets. In monogastric animals, soluble mixed-linkage β-glucan increases intestinal digesta viscosity and reduces nutrient contact with the intestinal epithelium. The dry microgranulate is mixed into meal at 50–150 g/t of complete feed, with the exact rate established by ileal viscosity reduction or in vivo performance trials. For pelleted feed, post-pelleting recovery of mesophilic β-glucanase declines sharply when conditioning temperatures exceed 80 °C for more than 30 s; thermostable bacterial variants with an optimum of 65–75 °C are used when 80% recovery is required after 85 °C conditioning. Liquid post-pelleting spraying through a rotary atomizer is an alternative for heat-sensitive preparations, provided the application system maintains a coefficient of variation below 10% in enzyme activity across sampled pellets. Feed β-glucan content is monitored by AOAC 995.16, adapted for complete feed matrices.
Thermostable bacterial β-glucanase variants have published temperature optima between 65 °C and 75 °C and pH optima between 6.0 and 7.0, whereas the fungal BG-750L has an optimum from 50 °C to 60 °C and pH 4.5–6.0. The difference is operationally significant in high-temperature processing and accounts for the use of separate thermostable grades.
Table 2 summarizes the major application windows and analytical controls.
| Application | Typical dosing | Analytical control standard | Critical process limitation |
|---|---|---|---|
| Mashing/lautering | 0.1–0.5 L/t dry grist | ASBC Wort-13 viscosity; ASBC Wort-18 β-glucan | Mesophilic grade inactive above 65 °C |
| High-gravity brewing | 0.5–0.6 L/t | AACC 32-23 β-glucan | Increased low-molecular-weight glucan turbidity if overdosed |
| Feed pelleting | 50–150 g/t complete feed | AOAC 995.16, adapted | Conditioning above 80 °C reduces recovery unless thermostable variant is used |
| Oat β-glucan extraction | 0.1–0.3 L/t dry substrate | AOAC 995.16; AACC 32-23 | Heat inactivation at 75 °C for 10 min required to stop molecular weight reduction |
BG-750L is a filtered amber liquid with a density of 1.10–1.20 g/mL at 20 °C. The formulation may contain soluble salts and preservatives to suppress microbial growth during storage; if sodium benzoate or potassium sorbate is present, its behavior in downstream fermentation should be reviewed because yeast culture sensitivity varies by strain. The product should be stored at 0–8 °C in closed containers; supplier stability specifications are based on 12 months at 0–8 °C and activity retention above 90% of declared value. Repeated freeze-thaw cycles above 3 produce protein-rich precipitates that clog metering pumps and alter dosage accuracy. Activity, pH, and microbial count comply with food enzyme specifications aligned with 21 CFR 184 general provisions and the JECFA carbohydrate enzyme monograph.
Oat β-glucan extraction requires a mixed enzyme system because oat β-glucan is a linear polymer with repeating β-1,4-linked cellotriosyl/cellotetraosyl units separated by β-1,3 linkages. BG-750L is used in aqueous extraction at 50 °C and pH 5.5 with a typical dose of 0.1–0.3 L/t of dry substrate. Treatment of high-solids oat slurry reduces apparent viscosity enough to allow decanter centrifugation or plate-and-frame filtration. β-Glucan molecular weight is controlled by limiting enzyme contact time to 15–30 min before heat inactivation at 75 °C for 10 min; longer treatment produces lower-viscosity oligosaccharides that do not meet high-molecular-weight oat β-glucan specifications. Analytical control is performed by AOAC 995.16 and AACC 32-23. Published data for this specific high-solids configuration is limited because starch and protein phases interact with β-glucan during separation.
In post-fermentation processing, β-glucanase can reduce viscosity contributed by yeast cell wall β-glucan during autolysis, but dosing is secondary to mashing and must be validated against turbidity specifications.
Beta-glucanase should not be exposed to oxidizing sanitizers such as sodium hypochlorite at concentrations above 200 ppm free chlorine, because methionine and cysteine residues in the enzyme active site are oxidized and activity loss is rapid. Bentonite and activated carbon adsorb enzyme protein; they should be added only after β-glucan hydrolysis is complete or after enzyme inactivation at 75 °C for 10 min. The enzyme is not a corrective tool for severe malt quality failures where β-glucan concentrations exceed 400 mg/L in Congress wort; grist blending or extended germination is required. The preparation is incompatible with strong acidic conditions below pH 3.0 and strong alkaline conditions above pH 9.0, which irreversibly reduce activity.
