The product has been successfully added to your shopping list.

endo-1,3(4)-β-D-Glucanase (Trichoderma sp.)

Product code: E-LAMSE

100 Units

Prices exclude VAT

This product is currently unavailable, please contact

North American customers click here
Content: 100 Units
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: > 1 year under recommended storage conditions
Enzyme Activity: endo-1,3(4)-β-Glucanase
EC Number:
CAZy Family: GH16
CAS Number: 62213-14-3
Synonyms: glucan endo-1,3(4)-beta-D-glucosidase
Source: Trichoderma sp. 
Molecular Weight: 32,000
Concentration: Supplied at ~ 50 U/mL
Expression: Purified from Trichoderma sp.
Specificity: Hydrolysis of (1,3)-β-D-glucosidic linkages in (1,3)-β-D Glucans and (1,3)(1,4)-β-D-glucosidic linkages in mixed linkage β-D-Glucans.
Specific Activity: > 10 U/mg (40oC, pH 4.5 on CM-Curdlan)
Unit Definition: One Unit of endo-1,3-β-D-Glucanase activity is defined as the amount of enzyme required to release one µmole of glucose-reducing-sugar equivalents per minute in the presence of CM-Curdlan (5 mg/mL) in sodium acetate buffer (200 mM) at pH 4.5 and 40oC.
Temperature Optima: 40oC
pH Optima: 4.5
Application examples: Applications in carbohydrate and biofuels research and in the food and feeds industries.

High purity endo-1,3(4)-β-D-Glucanase (Trichoderma sp.) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

View our full Carbohydrate Active enZYme products list.

Certificate of Analysis
Safety Data Sheet
Data Sheet

Properties of corn-expressed carbohydrase AC1 in swine diets and its effects on apparent ileal digestibility, performance, hematology, and serum chemistry.

Lessard, P. A., Li, X., Broomhead, J. N., Parker, M. H., Bailey, C. & Raab, R. M. (2021). Heliyon, 7(8), e07696.

Carbohydrases are often incorporated into livestock feed as digestive aids to improve animal performance. AC1 is a thermostable carbohydrase with β-1,4-glucanase, endo-cellulase, and cellobiohydrolase activity. AC1 has been expressed in corn, where it accumulates in the grain for easy inclusion in animal diets. Incorporating the enzyme in high-fiber diets (corn-soy supplemented with distiller's dry grains with solubles) that were fed to 5-week-old pigs led to a trend of decreasing viscosity of the digesta as the dose of the enzyme increased (P = 0.092). AC1 also tended to increase the apparent ileal digestibility (AID) of neutral detergent fiber (P = 0.076). When fed diets containing 2126 U/kg AC1, pigs experienced no adverse effects in terms of performance metrics (body weights, average daily gain, average daily feed intake and gain-to-feed ratio), hematology, blood chemistry or general health when compared to pigs fed a control diet that lacked AC1.

Hide Abstract
Induced mutations in tomato SlExp1 alter cell wall metabolism and delay fruit softening.

Minoia, S., Boualem, A., Marcel, F., Troadec, C., Quemener, B., Cellini, F., Petrozza, A., Vigouroux, J., Lahaye, M., Carriero, F. & Bendahmane, A. (2016). Plant Science, 242, 195-202.

Fruit ripening and softening are key traits for many fleshy fruit. Since cell walls play a key role in the softening process, expansins have been investigated to control fruit over ripening and deterioration. In tomato, expression of Expansin 1 gene, SlExp1, during fruit ripening was associated with fruit softening. To engineer tomato plants with long shelf life, we screened for mutant plants impaired in SlExp1 function. Characterization of two induced mutations, Slexp1-6_W211S, and Slexp1-7_Q213Stop, showed that SlExp1 loss of function leads to enhanced fruit firmness and delayed fruit ripening. Analysis of cell wall polysaccharide composition of Slexp1-7_Q213Stop mutant pointed out significant differences for uronic acid, neutral sugar and total sugar contents. Hemicelluloses chemistry analysis by endo-β-1,4-D-glucanase hydrolysis and MALDI-TOF spectrometry revealed that xyloglucan structures were affected in the fruit pericarp of Slexp1-7_Q213Stop mutant. Altogether, these results demonstrated that SlExp1 loss of function mutants yield firmer and late ripening fruits through modification of hemicellulose structure. These SlExp1 mutants represent good tools for breeding long shelf life tomato lines with contrasted fruit texture as well as for the understanding of the cell wall polysaccharide assembly dynamics in fleshy fruits.

Hide Abstract

Regulation of the cellulose synthase-like gene family by light in the maize mesocotyl.

Van Erp, H. & Walton, J. D. (2009). Planta, 229(4), 885-897.

The cellulose synthase-like (ZmCSL) gene family of maize was annotated and its expression studied in the maize mesocotyl. A total of 28 full-length CSL genes and another 13 partial sequences were annotated; four are predicted to be pseudogenes. Maize has all of the CSL subfamilies that are present in rice, but the CSLC subfamily is expanded from 6 in rice to 12 in maize, and the CSLH subfamily might be reduced from 3 to 1. Unlike rice, maize has a gene in the CSLG subfamily, based on its sequence similarity to two genes annotated as CSLG in poplar. Light regulation of glycan synthase enzyme activities and CSL gene expression were analyzed in the mesocotyl. A Golgi-localized glucan synthase activity is reduced by ~50% 12 h after exposure to light. Β-1,4-Mannan synthase activity is reduced even more strongly (>85%), whereas Β-1,4-xylan synthase, callose synthase, and latent IDPase activity respond only slightly, if at all, to light. At least 17 of the CSL genes (42%) are expressed in the mesocotyl, of which four are up-regulated at least twofold, seven are down-regulated at least twofold, and six are not affected by light. The results contribute to our understanding of the structure of the CSL gene family in an important food and biofuel plant, show that a large percentage of the CSL genes are expressed in the specialized tissues of the mesocotyl, and demonstrate that members of the CSL gene family are differentially subject to photobiological regulation.

Hide Abstract
Dietary fibers from mushroom sclerotia: 3. In vitro fermentability using human fecal microflora.

Wong, K. H., Wong, K. Y., Kwan, H. S. & Cheung, P. C. K. (2005). Journal of Agricultural and Food Chemistry, 53(24), 9407-9412.

The in vitro fermentability of three novel dietary fibers (DFs) prepared from mushroom sclerotia, namely, Pleurotus tuber-regium, Polyporous rhinocerus, and Wolfiporia cocos, was investigated and compared with that of the cellulose control. All DF samples (0.5 g each) were fermented in vitro with a human fecal homogenate (10 mL) in a batch system (total volume, 50 mL) under strictly anaerobic conditions (using oxygen reducing enzyme and under argon atmosphere) at 37°C for 24 h. All three novel sclerotial DFs exhibited notably higher dry matter disappearance (P. tuber-regium, 8.56%; P. rhinocerus, 13.5%; and W. cocos, 53.4%) and organic matter disappearance (P. tuber-regium, 9.82%; P. rhinocerus, 14.6%; and W. cocos, 57.4%) when compared with those of the cellulose control. Nevertheless, only the W. cocos DF was remarkably degraded to produce considerable amounts of total short chain fatty acids (SCFAs) (5.23 mmol/g DF on organic matter basis, with a relatively higher molar ratio of propionate) that lowered the pH of its nonfermented residue to a slightly acidic level (5.89). Variations on the in vitro fermentability among the three sclerotial DFs might mainly be attributed to their different amounts of interwoven hyphae present (different amounts of enzyme inaccessible cell wall components) as well as the possible different structural arrangement (linkage and degree of branching) of their β-glucans.

Hide Abstract
Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
Customers also viewed
endo-1-3-beta-D-Glucanase barley E-LAMHV
endo-1,3-β-D-Glucanase (barley)
Phytase Assay Kit
Xylazyme AX Tablets T-XAX
Xylazyme AX Tablets
endo-1-4-beta-Xylanase Neocallimastix patriciarum E-XYLNP
endo-1,4-β-Xylanase (Neocallimastix patriciarum)
Pectate Lyase Aspergillus sp E-PCLYAN
Pectate Lyase (Aspergillus sp.)
endo-1-4 beta-Mannanase Aspergillus niger E-BMANN
endo-1,4 β-Mannanase (Aspergillus niger)
Lichenase endo-1-3-1-4-beta-D-Glucanase Bacillus subtilis E-LICHN
Lichenase (endo-1,3:1,4-β-D-Glucanase) (Bacillus subtilis)
beta-Glucuronidase Escherichia coli E-BGLAEC
β-Glucuronidase (Escherichia coli)