Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Xylanase, beta-glucosidase, beta-xylosidase, endoglucanase and polygalacturonase production from Curvularia inaequalis was carried out by means of solid-state and submerged fermentation using different carbon sources. beta-Glucosidase, beta-xylosidase, polygalacturonase and xylanase produced by the microorganisms were characterized. beta-Glucosidase presented optimum activity at pH 5.5 whereas xylanase, polygalacturonase and beta-xylosidase activities were optimal at pH 5.0. Maximal activity of beta-glucosidase was determined at 60 degrees C, beta-xylosidase at 70 degrees C, and polygalacturonase and xylanase at 55 degrees C. These enzymes were stable at acidic to neutral pH and at 40-45 degrees C. The crude enzyme solution was studied for the hydrolysis of agricultural residues.
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PMID:Production, characterization and properties of polysaccharide depolymerizing enzymes from a strain of Curvularia inaequalis. 1183 Sep 41

The invertase inhibitory protein isolated from Cyphomandra betacea Sendt and Solanum tuberosum inhibited the invertase activity from different species, genera and even plant family. Furthermore, proteinaceous inhibitors are not invertase specific; fungal, bacterial and higher plant enzymes including polygalacturonase, pectinase, pectin lyase, alpha-L-arabinofuranosidase and beta-glucosidase are also shown to be inhibited. Both inhibitors exhibited an in vitro antibacterial action against phytopathogenics strains of Xanthomonas campestris pvar vesicatoria CECT 792, Pseudomonas solanacearum CECT 125, Pseudomonas corrugata CECT 124, Pseudomonas syringae and Erwinia carotovora var carotovora.
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PMID:Inhibition of hydrolytic enzyme activities and plant pathogen growth by invertase inhibitors. 1236 59

Larval and adult Psacothea hilaris feed on mulberry wood and leaves, respectively. High levels of endogenous activity against the major dietary carbohydrates, cellulose, hemicellulose, starch and soluble sugars were secreted in the gut of larvae and adults. Activity against pectin was also high and multiple polygalacturonase (EC 3.2.1.15) components were secreted in the gut of larvae. One glycanase component, beta-EG1, which was primarily an endo-beta-1,4-glucanase (EC 3.2.1.4) and another, beta-EG2, which was mostly an endo-beta-1,4-xylanase (EC 3.2.1.8), were also secreted, while at least four additional components hydrolysed laminarin, lichenin and crystalline cellulose. The beta-glycosidase component beta-GD1 was associated with most of the beta-mannosidase (EC 3.2.1.25) and beta-xylosidase (EC 3.2.1.37) activity secreted in the gut of larvae, while another, beta-GD2, was a beta-glucosidase (EC 3.2.1.21), the activity of which was directed against cellobiose and other beta-linked disaccharides, and a beta-fucosidase (EC 3.2.1.38). A beta-galactosidase (EC 3.2.1.23), which did not hydrolyse lactose, was also secreted, as were distinct beta-N-acetylhexosaminidase (EC 3.2.1.52), trehalase (EC 3.2.1.28), alpha-L-arabinosidase (EC 3.2.1.55), alpha-galactosidase (EC 3.2.1.22) and a minimum of four alpha-glucosidase (EC 3.2.1.20) components, one of which was also likely to be associated with a peak of alpha-mannosidase (EC 3.2.1.24) activity. The alpha-glucosidase components varied in their specificity for alpha-linked disaccharides, but none was active against sucrose, which was hydrolysed by a beta-fructofuranosidase (EC 3.2.1.26) component. Overall average levels of activity in larvae were twice those of adults, but the secretion of individual carbohydrases in both was not regulated in response to the relative abundance of particular carbohydrate components in their respective diets.
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PMID:Diet and carbohydrate digestion in the yellow-spotted longicorn beetle Psacothea hilaris. 1277 Apr 76

Thanatephorus cucumeris is a ubiquitous fungus responsible for many types of plant diseases worldwide. All isolates from infected Hevea brasiliensis trees secreted pectolytic enzymes; polygalacturonase (PG), pectin lyase (PL) and cellulolytic enzymes; beta-glucosidase and cellobiase in culture. The extracts of the rubber tree leaf tissues, inoculated with T. cucumeris did not show any PG activity. However, PL activity was detected in tissue with the establishment of the infection. The levels of beta-glucosidase, an inherent enzyme in Hevea spp. increased rapidly following infection. However, cellobiase was detected only with the initiation of infection. Molecular weights of PG in all isolates were similar and in the range of 53,000 to 58,000. PL also followed the same pattern showing a molecular weight around 39,000.
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PMID:Characterization of cell wall degrading enzymes of Thanatephorus cucumeris. 1500 48

I examined the role of aerobic microbial populations in cellulose digestion by two sympatric species of desert millipedes, Orthoporus ornatus and Comanchelus sp. High numbers of bacteria able to grow on media containing cellulose, carboxymethyl cellulose, or cellobiose as the substrate were found in the alimentary tracts of the millipedes. Enzyme assays indicated that most cellulose and hemicellulose degradation occurred in the midgut, whereas the hindgut was an important site for pectin degradation. Hemicellulase and beta-glucosidase in both species and possibly C(x)-cellulase and pectinase in O. ornatus were of possible microbial origin. Degradation of [C]cellulose by millipedes whose gut floras were reduced by antibiotic treatment and starvation demonstrated a reduction in CO(2) release and C assimilation and an increase in C excretion over values for controls. It appears that the millipede-bacterium association is mutualistic and makes available to millipedes an otherwise mostly unutilizable substrate. Such an association may be an important pathway for decomposition in desert ecosystems.
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PMID:Role of aerobic microbial populations in cellulose digestion by desert millipedes. 1634 74

Production of carbohydrases by Alternaria solani is inhibited by glucose under low growth conditions. In an enriched medium, glucose has little effect on the production of polygalacturonase and cellulase while it still suppresses production of beta-glucosidase. Low levels of all three enzymes were produced in the absence of their respective substrates. Such regulation has been found with many organisms. However, far greater production of these carbohydrases occurred with additions of adenosine phosphates to the growth media. Highest stimulation of enzyme production was by adenosine 5'-phosphate. Adenosine 5'-triphosphate and cyclic 3', 5'-adenosine monophosphate gave lesser amounts. Starvation appears to induce production of extracellular carbohydrases and adenosine 5'-phosphate may have a role in the starvation process.
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PMID:Effect of Glucose and Adenosine Phosphates on Production of Extracellular Carbohydrases of Alternaria solani. 1665 49

Approximately 1 million metric tons of grapefruit were processed in the 2003/04 season resulting in 500,000 metric tons of peel waste. Grapefruit peel waste is usually dried, pelletized, and sold as a low-value cattle feed. This study tested different loadings of commercial cellulase and pectinase enzymes and pH levels to hydrolyze grapefruit peel waste to produce sugars. Pectinase and cellulase loadings of 0, 1, 2, 5, and 10mgprotein/g peel dry matter were tested at 45 degrees C. Hydrolyses were supplemented with 2.1mg beta-glucosidase protein/g peel dry matter. Five mg pectinase/g peel dry matter and 2mgcellulase/g peel dry matter were the lowest loadings to yield the most glucose. Optimum pH was 4.8. Cellulose, pectin, and hemicellulose in grapefruit peel waste can be hydrolyzed by pectinase and cellulase enzymes to monomer sugars, which can then be used by microorganisms to produce ethanol and other fermentation products.
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PMID:Hydrolysis of grapefruit peel waste with cellulase and pectinase enzymes. 1693 53

The ability of a commercial Trichoderma reesei cellulase preparation (Celluclast 1.5L), to hydrolyze the cellulose and xylan components of pretreated corn stover (PCS) was significantly improved by supplementation with three types of crude commercial enzyme preparations nominally enriched in xylanase, pectinase, and beta-glucosidase activity. Although the well-documented relief of product inhibition by beta-glucosidase contributed to the observed improvement in cellulase performance, significant benefits could also be attributed to enzymes components that hydrolyze non-cellulosic polysaccharides. It is suggested that so-called "accessory" enzymes such as xylanase and pectinase stimulate cellulose hydrolysis by removing non-cellulosic polysaccharides that coat cellulose fibers. A high-throughput microassay, in combination with response surface methodology, enabled production of an optimally supplemented enzyme mixture. This mixture allowed for a approximately twofold reduction in the total protein required to reach glucan to glucose and xylan to xylose hydrolysis targets (99% and 88% conversion, respectively), thereby validating this approach towards enzyme improvement and process cost reduction for lignocellulose hydrolysis.
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PMID:Optimization of enzyme complexes for lignocellulose hydrolysis. 1705 83

Pektofoetidin and Pectinex, enzyme preparations with the highest polygalacturonase and beta-glucosidase activities, were covalently immobilized on DEAE cellulose and Aminosilochromes 10 and 30. After treatment of cherry plum wine material with the soluble and immobilized enzyme preparations, the content of phenolics increased by 26 and 40%, respectively. The increase was accompanied by a decrease in the protein content (by up to 37%), carbohydrate content (by 17% on the average), and antioxidant activity (5-37%). The most efficient treatment involved Pektofoetidin immobilized on Aminosilochrome 10. It increased the clarity of the wine material and its antioxidant activity by 100 and 10%, respectively.
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PMID:[Comparison of the efficiency of polygalacturonase and beta-glucosidase enzyme preparations in stabilization of cherry plum wine material]. 1716 99

To improve efficiency and reduce cost, solid state simultaneous saccharification and fermentation of peashrub woody biomass was investigated under anaerobic conditions at 50 degrees C, with a cellulase-inoculant mixture consisting of Trichoderma koningii cellulase, Aspergillus niger cellulase, and Lactobacillus. Experimental formulations were prepared according to uniform prescription design principles. By crude protein, crude fiber models constructed using multivariate regression in SPSS and solutions analysis through unconstrained mathematical optimization in Microsoft Excel, it was clearly revealed that low pH value (3.8) from lactic acid accumulation produced by Lactobacillus would ultimately limit enzymatic hydrolysis during long-term fermentation (30 days). It was shown that a cellulase complex with filter paper cellulase/carboxymethyl cellulase/cotton lyase/beta-glucosidase/pectinase of activity ratios of 0.6:1:0.3:1:2.6 could effectively break peashrub cell wall structure by biodegradation of easily digested components and, then, release cellular contents to improve crude protein content. Thus, the enzymatic hydrolysis of peashrub biomass by the optimized cellulase complex could improve crude protein content by 45.3% (from 8.45 to 12.28%), although it only biodegraded about 10.90% of the crude fiber (from 44.45 to 40.08%).
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PMID:Optimization of cellulase complex formulation for peashrub biomass hydrolysis. 1734 18


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