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β-Glucanase Assay Kit (Malt and Microbial)

Play Training Video

00:01    Introduction
00:19    Theory of the Analytical Procedure
01:18      Kit Content
01:48     Reagent Preparation
03:30    Milling Samples
04:26    Weighing Samples
05:09    Enzyme Extraction
06:28    Assay of Malt Beta Glucanase Activity
12:02     Calculations

beta-Glucanase Assay Kit Malt and Microbial K-MBGL Scheme
   
Product code: K-MBGL
€267.00

100 assays per kit

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Content: 100 assays per kit
Shipping Temperature: Ambient
Storage Temperature: Short term stability: 2-8oC,
Long term stability: See individual component labels
Stability: > 1 year under recommended storage conditions
Analyte: endo-Cellulase, β-Glucanase/Lichenase
Assay Format: Spectrophotometer
Detection Method: Absorbance
Wavelength (nm): 590
Signal Response: Increase
Limit of Detection: 100 U/kg of malt
Reproducibility (%): ~ 7%
Reaction Time (min): ~ 35 min
Application examples: Malt extracts, wort, beer and other materials.
Method recognition: RACI Standard Method

β-Glucanase (Malt and Microbial) Assay Kit is suitable for the measurement and analysis of malt and bacterial β-glucanase and endo-1,4-β-glucanase.

Looking for other assay kits? See our full range of enzyme assay kits.

Scheme-K-MBGL MBGL Megazyme

Advantages
  • Very cost effective 
  • All reagents stable for > 2 years during use 
  • Only kit available 
  • Very specific 
  • Simple format 
  • Standard included
Validation of Methods
Documents
Certificate of Analysis
Safety Data Sheet
Assay Protocol Product Performance
Publications
Megazyme publication
Novel approaches to the automated assay of β-glucanase and lichenase activity.

Mangan, D., Liadova, A., Ivory, R. & McCleary, B. V. (2016). Carbohydrate Research, 435, 162-172.

We report herein the development of a novel assay procedure for the measurement of β-glucanase and lichenase (EC 3.2.1.73) in crude enzyme extracts. Two assay formats based on a) a direct cleavage or b) an enzyme coupled substrate were initially investigated. The ‘direct cleavage’ substrate, namely 4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-31-cellotriosyl-β-glucopyranoside (MBG4), was found to be the more generally applicable reagent. This substrate was fully characterised using a crude malt β-glucanase extract, a bacterial lichenase (Bacillus sp.) and a non-specific endo-1,3(4)-β-glucanase from Clostridium thermocellum (EC 3.2.1.6). Standard curves were derived that allow the assay absorbance response to be directly converted to β-glucanase/lichenase activity on barley β-glucan. The specificity of MBG4 was confirmed by analysing the action of competing glycosyl hydrolases that are typically found in malt on the substrate. Manual and automated assay formats were developed for the analysis of a) β-glucanase in malt flour and b) lichenase enzyme extracts and the repeatability of these assays was fully investigated.

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Megazyme publication

Measurement of dietary fibre components: the importance of enzyme purity, activity and specificity.

McCleary, B. V. (2001), “Advanced Dietary Fibre Technology”, (B. V. McCleary and L. Prosky, Eds.), Blackwell Science, Oxford, U.K., pp. 89-105.

Interest in dietary fibre is undergoing a dramatic revival, thanks in part to the introduction of new carbohydrates as dietary fibre components. Much emphasis is being placed on determining how much fibre is present in a food. Linking a particular amount of fibre to a specific health benefit is now an important area of research. The term 'dietary fibre' first appeared in 1953, and referred to hemicelluloses, celluloses and lignin (Theandere/tf/.1995). Trowell (1974) recommended this term as a replacement for the no longer acceptable term 'crude fibre'. Burkitt (1995) has likened the interest in dietary fibre to the growth of a river from its first trickle to a mighty torrent He observes that dietary fibre 'was first viewed as merely the less digestible constituent of food which exerts a laxative action by irritating the gut', thus acquiring the designation 'roughage' - a term later replaced by 'crude fibre' and ultimately by 'dietary fibre'. Various definitions of dietary fibre have appeared over the years, partly due to the various concepts used in deriving the term (i.e. origin of material, resistance to digestion, fermentation in the colon, etc.), and partly to the difficulties associated with its measurement and labelling (Mongeau et al. 1999). The principal components of dietary fibre, as traditionally understood, are non-starch polysaccharides (which in plant fibre are principally hemicelluloses and celluloses), and the non-carbohydrate phenolic components, cutin, suberin and waxes, with which they are associated in nature. In 1976, the definition of dietary fibre was modified to include gums and some pectic substances, based on the resistance to digestion of these components in the upper intestinal tract. For the purposes of labelling, Englyst et al. (1987) proposed that dietary fibre be defined as 'non-starch polysaccharides (NSP) in the diet that are not digested by the endogenous secretions of the human digestive tract'. Methods were concurrently developed to specifically measure NSP (Englyst et al. 1994).

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Megazyme publication

New developments in the measurement of α-amylase, endo-protease, β-glucanase and β-xylanase.

McCleary, B. V. & Monaghan, D. (2000). “Proceedings of the Second European Symposium on Enzymes in Grain Processing”, (M. Tenkanen, Ed.), VTT Information Service, pp. 31-38.

Over the past 8 years, we have been actively involved in the development of simple and reliable assay procedures, for the measurement of enzymes of interest to the cereals and related industries. In some instances, different procedures have been developed for the measurement of the same enzyme activity (e.g. α-amylase) in a range of different materials (e.g. malt, cereal grains and fungal preparations). The reasons for different procedures may depend on several factors, such as the need for sensitivity, ease of use, robustness of the substrate mixture, or the possibility for automation. In this presentation, we will present information on our most up-to-date procedures for the measurement of α-amylase, endo-protease, β-glucanase and β-xylanase, with special reference to the use of particular assay formats in particular applications.

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Megazyme publication

Soluble, dye-labeled polysaccharides for the assay of endohydrolases.

McCleary, B. V. (1988). Methods in Enzymology, 160, 74-86.

A range of methods has been developed for the assay of polysaccharide endohydrolases, and these include viscosimetric and nephelometric methods and procedures based on the measurement of increase in reducing sugar equivalents and on the rate of release of soluble, dye-labeled fragments on hydrolysis of chromogenic polysaccharide substrates. Assays based on the use of chromogenic (dye-labeled) substrates have several advantages over more conventional assays including specificity and simplicity in use. However, as dyeing generally reduces the solubility of the polysaccharide, most commercially available dye-labeled substrates are insoluble and have the inherent disadvantages of heterogeneity in the assay tube and the difficulties associated with dispensing a solid substrate routinely with accuracy. This chapter describes methods for the preparation of soluble dye-labeled substrates for the assay β-D-mannanase, endo-1,4-β-D-glucanase , endo-1,3(4)-β-o-glucanase, and &alpha-amylase.

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Megazyme publication
Assay of malt β-glucanase using azo-barley glucan: an improved precipitant.

McCleary, B. V. & Shameer, I. (1987). Journal of the Institute of Brewing, 93(2), 87-90.

A procedure recently described for the assay of malt β-glucanase, which employs a dye-labelled and chemically-modified barley β-glucan substrate, has been improved by changing the precipitant solution used to terminate the reaction. The new precipitant solution contains 0•4% (w/v) zinc acetate and 4% (w/v) sodium acetate dissolved in 80% (v/v) aqueous methyl cellosolve. With this precipitant the procedure can be directly applied to the assay of cellulase activity, and with minor modification, to the assay of lichenase activity.

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Megazyme publication

Measurement of malt beta-glucanase.

McCleary, B. V. (1986). Proceedings of the 19th Convention of the Institute of Brewing (Aust. and N.Z. section), 181-187.

A Procedure has been developed for the assay of malt β-glucanase [a(1→3)(1→4)-β-D-glucanase] which employs as substrate, barley β-glucan dyed with Remazolbrilliant Blue and chemically modified with carboxymethyl groups to increase solubility. The described assay procedure together with a modified extraction format allows analysis of up to ten malt samples in less than 80 min. Also, the procedure is specific for enzymes active on barley β-glucan, is accurate and reliable, and can be readily applied to the analysis of β-glucanase in malt, green malt and wort.

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Megazyme publication
A soluble chromogenic substrate for the assay of (1→3)(1→4)-β-D-glucanase (lichenase).

McCleary, B. V. (1986). Carbohydrate Polymers, 6(4), 307-318.

A simple procedure for the assay of (1→3)(1→4)-β-D-glucanase (lichenase) has been developed. This assay employs as substrate barley (1→3)(1→4)-β-D-glucan dyed with Remazolbrilliant Blue R and chemically modified with carboxymethyl groups to increase solubility. Preparation of this substrate required the development of an improved procedure for the extraction and purification of barley β-glucan. Assays based on the use of the described chromogenic substrate at pH 6•5 are sensitive and specific for enzymes active on barley β-glucan.

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Megazyme publication

Problems caused by barley beta-glucans in the brewing industry.

McCleary, B. V. (1986). Chemistry in Australia, 53, 306-308.

Brewing, the oldest application of bio-technology is now a mix of trade art and modern science. This article describes new applications of enzyme chemistry to trouble-shooting in beer production.

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Publication

Supplementation of carbohydrate enzymes plus protease to the diet of finishing pigs containing 2 protein levels on the effects of growth performance, toxic gas emissions, meat quality, and colonic microbiota community.

Zhang, Q., Cho, S., Song, J., Jeong, J., Yu, M., Mun, S., Han, K. & Kim, I. (2022), Europe PMC, In Press.

Dietary supplementation with exogenous enzymes may positively affect the traits of finishing pigs. The present study investigated the effects of different protein levels and exogenous carbohydrate enzymes plus protease on growth performance, meat quality, toxic gas emissions, and the structure and function of colonic microbiota in finishing pigs.

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Publication

Whole-Genome Sequence and Interaction Analysis in the Production of Six Enzymes From the Three Bacillus Strains Present in a Commercial Direct-Fed Microbial (Norum™) Using a Bliss Independence Test.

Hernandez-Patlan, D., Solis-Cruz, B., Latorre, J. D., Merino-Guzman, R., Rodríguez, M. M., Ausland, C., Hernandez-Velasco, X., Holguin, O. R., Delgado, R., Hargis, B. M., Singh, P. & Tellez-Isaias, G. (2022). Frontiers in Veterinary Science, 9.

The three Bacillus strains present in Norum™ were initially selected by their excellent to good relative enzyme activity (REA) production score for amylase, protease, lipase, phytase, cellulase, β-glucanase, and xylanase. Further studies confirmed that the three isolates also showed an antibacterial activity, Gram-positive and Gram-negative poultry pathogens. Norum™ (Eco-Bio/Euxxis Bioscience LLC) is a Bacillus spore direct-fed microbial (DFM). The Bacillus isolates were screened and selected based on in vitro enzyme production profiles. Moreover, in chickens fed high non-starch polysaccharides, this DFM demonstrated to reduce digesta viscosity, bacterial translocation, increase performance, bone mineralization, and balance the intestinal microbiota. In the present study, we present the whole-genome sequence of each of the three isolates in Norum™, as well as the synergistic, additive, or antagonistic effects on the enzyme production behavior of the three Bacillus strains and their combinations when grown together vs. when grown individually. The whole-genome sequence identified isolate AM1002 as Bacillus subtilis (isolate 1), isolate AM0938 as Bacillus amyloliquefaciens (isolate 2), and isolate JD17 as Bacillus licheniformis (isolate 3). The three Bacillus isolates used in the present study produce different enzymes (xylanase, cellulase, phytase, lipase, protease, and β-glucanase). However, this production was modified when two or more Bacillus strains were combined, suggesting possible synergistic, antagonistic, or additive interactions. The Bliss analysis suggested (p < 0.05) that the combination of Bacillus strains 1-2 and 1-2-3 had intermediate effects and predicted that the combination of Bacillus strains 2-3 could have better effects than the combination of all the three Bacillus strains. In summary, the current study demonstrated the need of selecting Bacillus strains based on quantitative enzyme determination and data analysis to assess the impacts of combinations to avoid antagonistic interactions that could limit treatment efficacy. These results suggest that using Bacillus strains 2-3 together could lead to a new generation of DFMs with effects superior to those already examined in Bacillus strains 1-2-3 and, therefore, a potential alternative to growth-promoting antibiotics. More research utilizing poultry models is being considered to confirm and expand the existing findings.

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Publication

Expression of a wheat β-1,3-glucanase in Pichia pastoris and its inhibitory effect on fungi commonly associated with wheat kernel.

Zhang, S. B., Zhang, W. J., Zhai, H. C., Lv, Y. Y., Cai, J. P., Jia, F., Wang, J. S. & Hu, Y. S. (2019). Protein Expression and Purification, 154, 134-139.

β-1,3-glucanases, the plant PR-2 family of pathogenesis-related (PR) proteins, can be constitutively expressed and induced in wheat crop to enhance its anti-fungal pathogen defense. This study aimed to investigate the inhibitory effect of wheat β-1,3-glucanase on fungi most commonly associated with wheat kernel. A β-1,3-glucanase from wheat was successfully expressed in Pichia pastoris X-33 and its biochemical and antifungal properties were characterized herein. The molecular weight of recombinant β-1,3-glucanase is approximately 33 kDa. β-1,3-glucanase displays optimal activity at pH 6.5, remaining relatively high at pH 5.5–8.0. The optimal reaction temperature of β-1,3-glucanase is 50 °C, retaining approximately 84.0% residual activity after heat-treated at 50°C for 1 h. The steady-state kinetic parameters of β-1,3-glucanase against laminarin was determined and the Km and Vmax were 1.32 ± 0.20 mg/ml and 96.4 ± 4.4 U mg−1 protein, respectively. The inhibitory effect of purified β-1,3-glucanase against the seven fungi commonly associated with wheat kernel was assessed in vitro. β-1,3-glucanase exerted differential inhibitory effects on hyphal growth of Fusarium graminearum, Alternaria sp., A. glaucus, A. flavus, A. niger, and Penicillium sp. Spore formation and mycelial morphology of Alternaria sp., A. flavus, and A. niger were significantly affected by β-1,3-glucanase (1U). The present results would help elucidate the mechanism underlying the inhibition of wheat β-1,3-glucanases on pathogens.

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Publication

Scalable Trehalose‐Functionalized Hydrogel Synthesis for High‐Temperature Protection of Enzymes.

Panescu, P. H., Ko, J. H. & Maynard, H. D. (2019). Macromolecular Materials and Engineering, 304(6), 1800782.

Herein, a scalable, two‐step synthesis of a trehalose hydrogel for the thermostabilization of enzymes is reported. A reaction between vinylbenzyl chloride and trehalose in base, followed by a redox‐initiated radical polymerization of the resulting mixture, produces the gel in 88% yield. The reaction scale can be increased 100‐fold while maintaining a 76% yield. Additionally, various solvents are investigated for purification, and more sustainable manufacturing solvents are selected. When the three major enzymes utilized in animal feed, phytase, β‐glucanase, and xylanase, are heated to 90°C in the hydrogel, greater than 98% activity is retained. Lastly, quantitative release of enzyme from the gel within 4 h is demonstrated. The scalable synthesis of the trehalose hydrogel, combined with its ability to stabilize and release a variety of animal feed enzymes, makes this technology promising for use with enzymes important in animal food production.

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Publication
Influence of oat components on lipid digestion using an in vitro model: Impact of viscosity and depletion flocculation mechanism.

Grundy, M. M., McClements, D. J., Ballance, S. & Wilde, P. J. (2018). Food Hydrocolloids, 83, 253-264.

Depletion flocculation is a well-known instability mechanism that can occur in oil-in-water emulsions when the concentration of non-adsorbed polysaccharide exceeds a certain level. This critical flocculation concentration depends on the molecular characteristics of the polysaccharide molecules, such as their molecular weight and hydrodynamic radius. In this study, a range of analytical methods (dynamic shear rheology, optical microscopy, and static light-scattering) were used to investigate the interaction between lipid droplets and polysaccharides (guar gum and β-glucans) of varying weight-average molecular weight and hydrodynamic radius, and concentration. The aim of this work was to see if the health benefits of soluble fibers like β-glucans could be explained by their influence on the structure and digestibility of lipid emulsions. The apparent viscosity of the emulsions increased with increasing polysaccharide concentration, molecular weight, and hydrodynamic radius. Droplet flocculation was observed in the emulsions only at certain polysaccharide concentrations, which was attributed to a depletion effect. In addition, the water-soluble components in oat flakes, flour, and bran were extracted using aqueous solutions, to examine their impact on emulsion stability and properties. Then, the rate and extent of lipolysis of a sunflower oil-in-water emulsion in the presence of these oat extracts were monitored using the pH-stat method. However, the inhibition of lipolysis was not linearly related to the viscosity of the oat solutions. The water-soluble extracts of β-glucan collected from oat flakes had a significant inhibitory effect on lipolysis. The results of this study increase our understanding of the possible mechanisms influencing the impact of oat constituents on lipid digestion. This work also highlights the importance of considering the molecular properties of polysaccharides, and not just their impact on solution viscosity.

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Publication

The variation in chemical composition of barley feed with or without enzyme supplementation influences nutrient digestibility and subsequently affects performance in piglets.

Clarke, L. C., Sweeney, T., Curley, E., Duffy, S. K., Rajauria, G. & O'Doherty, J. V. (2018). Journal of Animal Physiology and Animal Nutrition, 102(3), 799-809.

This study investigates the effect of dietary supplementation of a β-glucanase and β-xylanase enzyme mix to barley based diets, at two different chemical compositions achieved through different agronomical conditions on growth performance, coefficient of apparent total tract digestibility (CATTD) of nutrients, selected faecal microbial populations and faecal scores in piglets. Sixty-four piglets (11.7 kg (SD 0.96)) housed in pens of two were assigned to one of four dietary treatments (n = 8). The dietary treatments were as follows: (T1) low quality barley diet, (T2) low quality barley diet containing a β-glucanase and β-xylanase enzyme supplement, (T3) high quality barley diet and (T4) high quality barley diet containing a β-glucanase and β-xylanase enzyme supplement. Piglets offered the low quality barley-based diet had a higher (p < .05) average daily gain (ADG) (0.73 vs. 0.69 kg, SEM 0.001), gain:feed (G:F) ratio (0.61 vs. 0.58 kg, SEM 0.011) and a higher CATTD (p < .001) of dry matter (DM), organic matter (OM), nitrogen (N), ash, gross energy (GE) and neutral detergent fibre (NDF) compared with piglets offered the high quality barley diet. Piglets offered the high quality barley-based diet had reduced faecal scores compared to piglets offered the low quality barley-based diet (2.44 vs. 2.57, SEM 0.036) (p < .05). There was a higher population of Lactobacillus spp. (11.6 vs. 10.5 log gene copy number/g faeces, SEM 0.177) (p < .001) and total volatile fatty acid (VFA) concentration (185 vs. 165 mmol/g faeces, SEM 5.658) (p < .001) in the faeces of piglets offered the high quality barley-based diet compared to piglets offered the low quality barley-based diet. The inclusion of a β-glucanase and β-xylanase enzyme complex had no effect on any variable measured. In conclusion, the higher quality barley-based diet showed beneficial effects on the faecal Lactobacillus spp. population and faecal scores of the piglets; however, the higher level of β-glucans in the diet decreased nutrient digestibility and subsequently decreased the performance.

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Publication
Impact of hydrothermal and mechanical processing on dissolution kinetics and rheology of oat β-glucan.

Grundy, M. M. L-., Quint, J., Rieder, A., Balance, S., Dreiss, C. A., Butterworth, P. J. & Ellis, P. R. (2017). Carbohydrate Polymers, 387-397.

Oat mixed-linkage β-glucan has been shown to lower fasting blood cholesterol concentrations due notably to an increase in digesta viscosity in the proximal gut. To exert its action, the polysaccharide has to be released from the food matrix and hydrated. The dissolution kinetics of β-glucan from three oat materials, varying in their structure, composition and degree of processing, was investigated by incubating the oats at 37°C over multiple time points (up to 72 h). The samples were analysed for β-glucan content, weight-average molecular weight and rheological behaviour. Regardless of the materials studied and the processing applied, the solubilisation of β-glucan was not complete. Mechanical and hydrothermal processing led to differences in the viscosity flow curves of the recovered solutions, with the presence of particulates having a marked effect. This study revealed that the structure and processing methods applied to oat materials resulted in varied and complex rheological properties, especially when particulates are present.

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Safety Data Sheet
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