Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The immature sugar cane stalks studied contained less than 7% sucrose, and showed the activities of enzymes such as invertase, alpha-galactosidase, alpha-mannosidase, beta-N-acetylglucosaminidase, beta-glucosidase, beta-xylosidase, and beta-galactosidase. The alpha-galactosidase was highly purified by ammonium sulfate fractionation, gel filtration on a Sephadex G-100 column, ionexchange chromatography on DEAE-cellulose, and CM-cellulose columns, and heat treatment (60 degrees C, 15 min) in the presence of 0.2 m D-galactose. In polyacrylamide gel electrophoresis, the purified enzyme was homogeneous, having a molecular weight of approximately 46,000. In gelfiltration, it was approximately 47,000. The activity was optimum at pH 4.5 and at 60 degrees C. The purified enzyme hydrolyzed p-nitrophenyl-alpha-D-galactopyranoside (Km, 0.83 mM; Vmax, 25.0 mumol/mg/min), raffinose (Km, 25.9 mM; Vmax, 15.4 mumol/mg/min), and stachyose (Km, 13.0 mM; Vmax 2.7 mumol/mg/min), in addition to melibiose, guar gum, and locust bean gum. The hydrolysis of p-nitrophenyl-alpha-D-galactopyranoside was markedly inhibited by HgCl2, AgNO3, p-chloromercuribenzoate (PCMB), L-ascorbic acid, melibiose, stachyose, and D-galactose. Also the purified enzyme showed a lectin activity with trypsinized erythrocytes.
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PMID:Purification and properties of alpha-galactosidase from immature stalks of Saccharum officinarum (sugar cane). 627 79

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

Acetyl esterase (AE) activity present in the culture filtrate of Termitomyces clypeatus was separated into lower molar mass (LMM) and higher molar mass (HMM) protein fractions during BioGel P-200 gel chromatography. AE was purified as a 30 kDa nonglycosylated protein from LMM fractions by CM-Sepharose ion exchange chromatography and HPGPLC. Although the HMM fraction had a number of enzyme activities (sucrase, beta-xylosidase, beta-glucosidase, and alpha-L-arabinofuranosidase) other than AE, protein present in the fraction was eluted as a single protein peak in HPGPLC and gave a single band in native PAGE. The fraction, subsequently purified by DEAE-Sephadex chromatography, was a SDS-PAGE homogeneous 80 kDa glycoprotein, but with both AE and cellobiase activities. The aggregate dissociated during ConA-Sepharose chromatography and 30 kDa AE and 56 kDa glycosylated cellobiase were purified separately. The dissociation caused significant loss of cellobiase activity but not that of AE. AE purified from both HMM and LMM fractions was characterized to be the same enzyme in terms of molar masses, pI (7.3), and other physicochemical properties. AE as an aggregate with cellobiase showed higher thermostability, temperature optimum, and resistance toward chemical denaturants than those of purified AE. Compared to cellobiase purified earlier from the same fungus, the enzyme present with AE in the aggregate also showed higher catalytic activity, thermostability, and temperature optimum. The study indicated that the formation of such SDS-resistant enzyme aggregate was associated with significant changes in the physicochemical properties of the enzymes, mainly toward improvement of rigidity of enzymes, and sometimes with the improvement of catalytic activity.
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PMID:Protein-protein interaction conferring stability to an extracellular acetyl (xylan) esterase produced by Termitomyces clypeatus. 1279 Jun 30

Antibodies were raised against carrot (Daucus carota) cell wall beta-fructosidase that was either in a native configuration (this serum is called anti-betaF(1)) or chemically deglycosylated (anti-betaF(2)). The two antisera had completely different specificities when tested by immunoblotting. The anti-betaF(1) serum reacted with beta-fructosidase and many other carrot cell wall proteins as well as with many proteins in extracts of bean (Phaseolus vulgaris) cotyledons and tobacco (Nicotiana tabacum) seeds. It did not react with chemically deglycosylated beta-fructosidase. The anti-betaF(1) serum also reacted with the bean vacuolar protein, phytohemagglutinin, but not with deglycosylated phytohemagglutinin. The anti-betaF(2) serum reacted with both normal and deglycosylated beta-fructosidase but not with other proteins. These results indicate that the betaF(2) antibodies recognize the beta-fructosidase polypeptide, while the betaF(1) antibodies recognize glycan sidechains common to many glycoproteins. We used immunoadsorption on glycoprotein-Sepharose columns and hapten inhibition of immunoblot reactions to characterize the nature of the antigenic site. Antibody binding activity was found to be associated with Man(3)(Xyl)(GIcNAc)(2)Fuc, Man(3)(Xyl)(GIcNAc)(2), and Man(Xyl) (GIcNAc)(2) glycans, but not with Man(3)(GIcNAc)(2). Treatment of phytohemagglutinin, a glycoprotein with a Man(3)(Xyl)(GIcNAc)(2)Fuc glycan, with Charonia lampas beta-xylosidase (after treatment with jack-bean alpha-mannosidase) greatly diminished the binding between the antibodies and phytohemagglutinin. We conclude, therefore, that the antibodies bind primarily to the xylosebeta, 1--> 2mannose structure commonly found in the complex glycans of plant glycoproteins.
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PMID:Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins. 1666 70

Orange peels is the principal solid by-product of the citrus processing industry and the disposal of the fresh peels is becoming a major problem to many factories. Dry citrus peels are rich in pectin, cellulose and hemicellulose and may be used as a fermentation substrate. Production of multienzyme preparations containing pectinolytic, cellulolytic and xylanolytic enzymes by the mesophilic fungi Aspergillus niger BTL, Fusarium oxysporum F3, Neurospora crassa DSM 1129 and Penicillium decumbens under solid-state fermentation (SSF) on dry orange peels was enhanced by optimization of initial pH of the culture medium and initial moisture level. Under optimal conditions A. niger BTL was by far the most potent strain in polygalacturonase and pectate lyase, production followed by F. oxysporum F3, N. crassa DSM 1129 and P. decumbens. N. crassa DSM 1129 produced the highest endoglucanase activity and P. decumbens the lowest one. Comparison of xylanase production revealed that A. niger BTL produced the highest activity followed by N. crassa DSM 1129, P. decumbens and F. oxysporum F3. N. crassa DSM 1129 and P. decumbens did not produce any beta-xylosidase activity, while A. niger BTL produced approximately 10 times more beta-xylosidase than F. oxysporum F3. The highest invertase activity was produced by A. niger BTL while the lowest ones by F. oxysporum F3 and P. decumbens. After SSF of the four fungi, under optimal conditions, the fermented substrate was either directly exposed to autohydrolysis or new material was added, and the in situ produced multienzyme systems were successfully used for the partial degradation of orange peels polysaccharides and the liberation of fermentable sugars.
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PMID:Fungal multienzyme production on industrial by-products of the citrus-processing industry. 1760 24