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Melibiose

About: Melibiose is a research topic. Over the lifetime, 1002 publications have been published within this topic receiving 27300 citations. The topic is also known as: Melibiose.


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Journal ArticleDOI
01 Jan 2019
TL;DR: In this article, a recombinant α-galactosidase produced by Aspergillus sojae Ta1 was purified using anion exchange and hydrophobic interaction chromatography with an overall yield of 56% and 64.7 U/mg protein specific activity.
Abstract: Galactooligosaccharides are well-known functional food ingredients with prebiotic properties. Recent trend for the use of galactooligosaccharides in the food industry leads the search for new enzymes for their production. α-Galactosidase from Aspergillus fumigatus IMI 385708, possessing a highly efficient debranching ability on polymeric substrates, is also able to perform transgalactosylation. In this study, recombinant α-galactosidase produced by Aspergillus sojae Ta1 was purified 18.7-fold using anion exchange and hydrophobic interaction chromatography with an overall yield of 56% and 64.7 U/mg protein specific activity. The V max and K m values for the hydrolysis of p NPGal were 78 U/mg protein and 0.45 mM, respectively. Optimum pH (pH 4.5) and temperatures (50-60°C) for recombinant α-galactosidase activity were determined. For the synthesis of oligosaccharides, purified and characterized recombinant α-galactosidase was used in the transgalactosylation of various mono- and disaccharides using p NPGal ( p -nitrophenyl-α- D- galactopyranoside) as galactose donor. Di- and trisaccharides obtained by transgalactosylation were analysed by TLC, ESI-MS, and HPLC analysis. Among 12 acceptor candidates, α-galactosidase transgalactosylated galactose, glucose, mannose, cellobiose, lactose, maltose, and sucrose efficiently, however, did not transgalactosylate xylose, arabinose, fucose, fructose, and melibiose.

1 citations

Patent
27 Apr 2012
TL;DR: In this paper, compositions and uses thereof as a supplementary bee food for increasing the MGO and/or UMF number in honey; said compositions comprise: a) from 0.0001% to 30% by weight of methyl glyoxal-1,1-dimethylacetal, methylglyoxal, dihydroxyacetone or 2,5dihydroxydioxane-2,5-dimethanol; and b) a sugar such as arabinose, 2-desoxy-D-glucose, fructose, fucose and man
Abstract: Disclosed are compositions and uses thereof as a supplementary bee food for increasing the MGO and/or UMF number in honey; said compositions comprise: a) from 0.0001% to 30% by weight of methylglyoxal-1,1-dimethylacetal, methylglyoxal, dihydroxyacetone or 2,5-dihydroxydioxane-2,5-dimethanol; and b) a sugar such as arabinose, 2-desoxy-D-glucose, 2-desoxy-D-ribose, fructose, fucose, galactose, mannose, sorbose, adonit, dulcet, erythit, inosit, mannit and/or sorbit, xylit, galacturonic acid, gluconic acid-lactone, glucuronic acid lactone, cellubiose, lactose, lactulose, maltose, melibiose, raffinose, saccharose, trehalose, amylose, inulin or natural or synthetic mixture of these sugars or other types of honey. Further disclosed is a method of feeding Manuka honey collecting bees which comprises using a composition as defined above close to a beehive of these bees.

1 citations

Patent
13 Oct 2005
TL;DR: In this article, an immunological improving agent, the T cell immunomodulator and an oral immunological tolerance inducer each comprising melibiose as an active ingredient are provided.
Abstract: PROBLEM TO BE SOLVED: To improve immune strength by T cell immunomodulating effects in relation to a T cell immunomodulator effective in improving the immune strength. SOLUTION: An immunological improving agent, the T cell immunomodulator and an oral immunological tolerance inducer each comprising melibiose as an active ingredient are provided. The melibiose has excellent T cell immunomodulating actions as compared with raffinose and is suitable for oral administration in aspects of a mouth melting feeling or taste. COPYRIGHT: (C)2006,JPO&NCIPI

1 citations

Book ChapterDOI
01 Jan 1979
TL;DR: The aim of the experiments presented here is to make acquaintance with two typical uptake systems in Escherichia coli, both inducible, i.e., synthesized by wild-type strains only when growing on the relevant carbon source or an inducing analog.
Abstract: Bacteria are free-living microorganisms often confronted with a large variety of environments. The occurrence in nature of different substances as main carbon source for their nutrition and the selective advantage of metabolizing fast any of these for fast proliferation promoted the development along the evolution of different adaptive uptake and catabolic equipments. The aim of the experiments presented here is to make acquaintance with two typical uptake systems in Escherichia coli, both inducible, i.e., synthesized by wild-type strains only when growing on the relevant carbon source or an inducing analog. Besides the general pattern of saturable accumulation uptake, the comparison of lactose and melibiose permeases illustrates the high degree of specificity, the possibility of overlaps in substrate specificity, and the possibility of different systems of energization, by the protonmotive force for lactose, by cotransport with sodium ion for melibiose.

1 citations

Journal ArticleDOI
TL;DR: Purified -galactosidase was obtained after sonication of harvested cell pellet followed by DEAE-Sephadex A-50 and Mono Q anion exchange chromatography and liberated galactose from melibiose, raffinose, and stachyose.
Abstract: Lactobacillus salivarius subsp. salivarius CNU27 possessed a high level of -galactosidase activity. Purified -galactosidase was obtained after sonication of harvested cell pellet followed by DEAE-Sephadex A-50 and Mono Q anion exchange chromatography. The specific activity of the purified enzyme was 8,994 units/mg protein which is 17.09 times higher than that in crude extract. The native enzyme was a monomer with a molecular mass of 56,397.1 dalton. The optimum temperature and pH for the enzyme were and 6.0, respectively. The enzyme was stable between 25 and . However, -galactosidase activity was lost rapidly below pH 4.5 and above pH 8.5. The enzyme activity decreased to 6.73% and 4.30% of the original activity by addition of and , respectively. Other metal compounds did not affect the enzyme activity significantly. The enzyme liberated galactose from melibiose, raffinose, and stachyose. The rate of substrates hydrolysis was measured by HPLC. Raffinose, stachyose and melibiose were completely decomposed after 24 hr at .

1 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20236
202212
202112
202017
201913
201816