Showing papers on "Melibiose published in 1969"

Studies on the Decomposition of Raffinose by α-Galactosidase of Mold

Abstract: A mold which produced α-galactosidase and little invertase was isolated and identified as Mortierella vinacea. α-Galactosidase formation of the mold was induced by galactose, melibiose, raffinose and lactose. Among these inducers lactose showed the most stimulative effect. α-Galactosidase was produced by either Koji method or submerged culture method, but in the latter most α-galactosidase was found in the mycelium fraction.Hydrolysis of raffinose in beet molasses was studied with the α-galactosidase in the mycelium fraction and about 80% of raffinose was found to be hydrolyzed by the enzyme preparation.

Antigenic structure of human gonadotropins: contribution of carbohydrate moiety to the antigenic structure of pituitary follicle-stimulating hormone.

Abstract: Precipitating, complement-fixing and neutralizing antibody was produced in rabbits by immunization with a partially purified human pituitary FSH preparation. Apparent serological specificity of this antiserum was increased after absorption with human serum and HCG. Attempts were made to examine immunologic carbohydrate determinant groups of human pituitary FSH by complement-fixation inhibition reactions between the absorbed antiserum and homogeneous human pituitary FSH preparations, using mono- and disaccharides, and by treatment of the hormone preparations with several carbohydrate-hydrolyzing enzymes. Of the saccharides tested, galactose, β-methyl- D-galactopyranoside lactose and melibiose were active in the inhibition test, and the disaccharides were more effective than the monosaccharides on an equimolar basis. Ovarian weight augmentation activity of FSH was completely abolished, but its complement-fixing property was not affected after treatment with neuraminidase. Both biologic and immunologic prope...

Genetic Analysis of Carbohydrate Transport-deficient Mutants of Salmonella typhimurium

Abstract: Mutants (car) isolated from Salmonella typhimurium were unable to utilize or ferment the following carbohydrates (all d-configuration): glucose, fructose, mannose, N-acetylglucosamine, sorbitol, mannitol, maltose, melibiose, and glycerol. The mutants did utilize galactose, glucose 6-phosphate, gluconic acid, glucuronic acid, pyruvate, and l-lactate. Biochemical analysis showed that there were two classes of mutants, each lacking one component of a phosphotransferase system. CarA mutants were deficient in enzyme I; carB lacked the phosphate carrier protein, HPr. Mapping experiments showed that the carA gene was located near pro; the carB gene mapped near purC.

Studies on the Decomposition of Raffinose by α-Galactosidase of Mold:Part I. α-Galactosidase Formation and Hydrolysis of Raffinose by the Enzyme Preparation

Abstract: A mold which produced α-galactosidase and little invertase was isolated and identified as Mortierella vinacea. α-Galactosidase formation of the mold was induced by galactose, melibiose, raffinose and lactose. Among these inducers lactose showed the most stimulative effect. α-Galactosidase was produced by either Koji method or submerged culture method, but in the latter most α-galactosidase was found in the mycelium fraction.Hydrolysis of raffinose in beet molasses was studied with the α-galactosidase in the mycelium fraction and about 80% of raffinose was found to be hydrolyzed by the enzyme preparation.

Survey of Some Actinomycetales for α-Galactosidase Activity

Abstract: The enzyme alpha-galactosidase offers potential to (i) eliminate possibly the flatus-inducing factor(s) in edible beans, (ii) eliminate raffinose during beet-sugar processing, and (iii) determine raffinose analytically. Accordingly, 20 genera of the order Actinomycetales Buchanan 1917 were tested for evidence of alpha-galactosidase activity. Test filtrates were prepared with a medium containing D-galactose and soybean meal. Enzyme activity was demonstrated through cellulose thin-layer chromatography. Of 123 strains tested, 28 produced extracellular alpha-galactosidase. Almost all were streptomycetes. Members of the genera Actinoplanes Couch 1950, Micromonospora varphiOrskov 1923, and Promicromonospora Krasil'nikov et al. 1961 also exhibited alpha-galactosidase activity. Additional tests led to the selection of five strains whose filtrates degraded melibiose, raffinose, and stachyose but not lactose and sucrose. Tests also were made with several soybean preparations.

Production and properties of galactosidases from Corticium rolfsii.

Abstract: When Corticum rolfsii was grown in a medium containing bran extract under aerobic conditions, it secreted alpha-D-galactosidase and beta-D-galactosidase into the culture fluid. Pectin also stimulated the production of these enzymes, whereas galactose, glucose, and sucrose stimulated their production to a lesser degree. C. rolfsii produced greater amounts of both enzymes than Aspergillus niger. Both galactosidases in the culture medium hydrolyzed alpha- and beta-p-nitrophenyl-D-galactosides as well as lactose, stachyose, melibiose, and raffinose. Both exhibited optimal activity at pH 2 to 4 and were quite stable under acidic conditions. alpha-Galactosidase was separated from beta-galactosidase by column chromatography.

Comparative Studies of Yeast and Sugarcane Invertase

Abstract: Comparative studies of sugarcane invertase and a commercial yeast invertase were conducted. There were two objectives: 1, To identify specific enzyme types on the basis of action patterns against a series of substrates; and 2, to determine whether cane invertase, derived from a highly developed plant species, is identical with the invertase of a primitive plant form. Cane invertase was prepared from lyophilized immature storage tissues, while yeast invertase was obtained commercially as a desiccated extract of yeast cells. Substrates included sucrose, raffinose, stachyose, melibiose, inulin, and soluble potato starch. The cane-invertase complex gave evidence of three carbohydrases: s-fructosidase, α -galactosidase, and α -glucosidase. Yeast invertase gave only s-fructosidase activity. Both types of invertase were readily inhibited by silicon, and possible modes of silicon action are discussed. Similarities were noted between sugarcane invertase and sugarcane amylase. The two cane systems appear more nearly identical than cane and yeast invertase. Cane invertase, a more highly versatile enzyme complex than yeast invertase, apparently reflects the more complicated biochemical requirements of a higher plant species.

Free amino acids and sugars of the adult sugar cane froghopper (aeneolamia varia saccharina) (homoptera: cercopidae) in relation to those of its host

Abstract: Glucose, fructose, sucrose, raffinose and glucuronic acid were present in both adult froghopper excrement and in sugar cane leaf sap. Melibiose was also present in the excrement but did not occur in the plant sap. Sugars were not recovered in the salivary glands of the insect, but in the haemolymph, glucose, fructose, sucrose and trehalose were determined. Most of the amino acids (alanine, arginine, asparagine, aspartic acid, cysteine/cysteic acid, cystine, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, phenylalanine, proline, serine, tryptophan, tyrosine and valine) in the leaf sap were present in the froghopper haemolymph and salivary glands. Nine of these acids also occurred in the excrement of the insect. RESUME LES ACIDES AMINES LIBRES ET LES SUCRES DE L'ADULTE DU CERCOPIDE DE LA CANNE A SUCRE, AENEOLAMIA VARIA SACCHARINA (HOMOPTERA: CERCOPIDAE), COMPARES A CEUX DE SA PLANTE-HOTE Le glucose, le fructose, le sucrose, le raffinose et l'acide glucuroniquc se retrouvent a la fois dans les excrements du Cercopide adulte et dans le jus extrait des feuilles de la canne a sucre. Le melibiose est present dans les excrements de l'insecte mais non dans la seve. Aucun sucre ne fut decele dans les glandes salivaires de l'insecte mais dans l'hemolymphe on a identifie du glucose, du fructose, du sucrose et du trehalose. La plupart des acides amines de l'extrait foliaire (alanine, arginine, asparagine, acide aspartique, cysteine et acide cysteique, cystine, acide glutamique, glutamine, glycine, histidine, iso-leucine, leucine, lysine, phenylalanine, proline, serine, tryptophane, tyrosine et valine) existent aussi dans le sang du Cercopide et dans ses glandes salivaires. 9 de ces acides amines se retrouvent egalement dans les excrements de l'insecte.

Control of Synthesis of Malate Dehydrogenase in Aerobacter aerogenes

Abstract: An inverse linear relationship was observed between the levels of l-malate dehydrogenase (MDH) and growth rates of Aerobacter aerogenes when grown under aerobic and anaerobic conditions on various substrates which served as the sole carbon and energy sources. Deviations from this linearity were found. MDH levels of cells grown aerobically on oxalacetate, l-malate, d-mannose and d-galactose, and of cells grown anaerobically on l-malate and d-mannose were higher than those expected according to this relationship. Enzyme levels of cells grown aerobically on maltose, d-glucuronate, pyruvate, and possibly melibiose and sucrose were lower than the expected ones. Experiments in which the cells were grown on a mixture of two substrates showed that substrates which gave low levels of MDH repressed the synthesis of this enzyme even in the presence of l-malate or other “high-level substrates.” Repressed levels were also observed when the mixture contained l-malate together with “intermediate” or high-level substrates. Identical MDH patterns were obtained by acrylamide gel electrophoresis for all the enzymatic preparations.