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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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Book ChapterDOI
TL;DR: The most potent inhibitors of the agglutinin are proteins and glycoproteins such as bovine serum albumin, collagen, thyroglobulin, ovalbumin, mucin, and fetuin.
Abstract: Extracts of ground avocado seeds (Fuerte and Hass varieties), prepared in different buffer solutions (pH 2.0–12.0), show hemagglutinating activity towards A, B, AB, and H (0) human erythrocytes. The extract showing the highest titer of aggulination was extracted at pH 10.5. The crude extract also causes hemolysis of fresh washed erythrocytes. The hemagglutinating factor is not inhibited by most of the simple sugars tested, e.g., D-glucose, D-mannose, D-galactose, and glucose-amine. The only sugars which show some inhibitory effect are N-Acetyl-neuraminic acid, melibiose, and stachiose. Basic amino acids, e.g., lysine and arginine also inhibit its activity. However the most potent inhibitors of the agglutinin are proteins and glycoproteins such as bovine serum albumin, collagen, thyroglobulin, ovalbumin, mucin, and fetuin.

5 citations

Journal ArticleDOI
TL;DR: LTG displayed wide substrate diversity with activity toward a variety of substrates such as stachyose, raffinose, melibiose, locust bean gum, and guar gum, suggesting this fungus may become a useful source of α‐galactosidase for multiple applications.
Abstract: A novel acidic α-galactosidase (EC 32122) designated as Leucopaxillus tricolor α-galactosidase (LTG) has been purified to homogeneity from the fruiting bodies of L tricolor to 855-fold with a specific activity of 956 U mg-1 by the application of chromatography and gel filtration The molecular mass of LTG was estimated to be 60 kDa as determined by both SDS-PAGE and by gel filtration The purified enzyme was identified by LC-MS/MS and four inner amino acid sequences were obtained When 4-nitrophenyl α-D-glucopyranoside (pNPGal) was used as substrate, the optimal pH and optimal temperature of LTG were pH 50 and 50 °C, respectively The enzyme activity was strongly inhibited by Hg2+ , Fe3 , Cu2+ , Cd2+ , and Mn2+ ions The chemical modification agent N-bromosuccinimide (NBS) completely inhibited the enzyme activity of LTG, indicating the paramount importance of tryptophan residue(s) to its enzymatic activity Besides, LTG displayed wide substrate diversity with activity toward a variety of substrates such as stachyose, raffinose, melibiose, locust bean gum, and guar gum Given the good ability of degrading the non-digestible and flatulence-causing oligosaccharides, this fungus may become a useful source of α-galactosidase for multiple applications

5 citations

Journal ArticleDOI
TL;DR: In this paper, the authors described isolation and characterization of three major transgalactosylation products from melibiose, which were used to decompose raffinose in beet sugar production.
Abstract: α-Galactosidases of Absidia and Mortiella sp. have been used to decompose raffinose in industrial beet sugar production. In this paper is described isolation and characterization of three major transgalactosylation products from melibiose

5 citations

Journal ArticleDOI
TL;DR: Modified enzymatic methods for the rapid quantitative determination of mixtures of oligosaccharides and their component monosacchcharides, used in studies of carbohydrate physiology of orchid seedlings are presented.
Abstract: New Phytol. (1972) 71, 307-315. ENZYMATIC QUANTITATIVE DETERMINATION OF HEXOSES, SINGLY AND IN MIXTURES WITH THEIR OLIGOSACCHARIDES BY ROBERT ERNST AND JOSEPH ARDITTI Department of Developmental and Cell Biology, University of California, Irvine, California, 92664, U.S .A. (Received 16 August 1971) SUMMARY Quantitative determinations of a number of naturally ocurring D-hexoses and their oligo- saccharides can be accomplished by combinations of enzymatic methods without prior separa- tion of the sugars. T hese spectrophotometric methods employ readily-available enzymes and o maltose or lactose mixed with galactose and/or glucose; melibiose in mixtures with raffinose, and other combinations. INTRODUCTION Many chemical and enzymatic methods have been described for qualitative and quanti- tative determination of naturally-occurring sugars (Aminoff et al., 1970; HoUigan, 1971; Holligan and Drew, 1971; Lewis and Smith, 1967). The latest employ gas-liquid chroma- tography (GL C). Since GLC is not yet widely available 'to botanists, this paper presents modified enzymatic methods for the rapid quantitative determination of mixtures of oligosaccharides and their component monosaccharides. These methods, which employ readily-available enzymes and commerical reagents, have been used in studies of carbohydrate physiology of orchid seedlings (Ernst, 1967; Ernst, Arditti and Healey, 1972). MATERIALS AND METHODS Sugars. Melibiose and stachyose were obtained from Calbiochem, Los Angeles, California and other sugars from Pfanstiehl Laboratories, Inc., Waukegan, Illinois. Only D-sugars were employed. They were dissolved either in distilled water and kept frozen until used or in methanol-water (7 : 3, v/v) and stored at room temperature. Enzymes. Fructofuranosidase (invertase) melibiase free, u6 U/mg, derived from bakers' yeast, Grade IV was obtained from Sigma Chemical Company, St Louis, Mo. An alternative grade, purchased from Calbiochem Wallerstein invertase activity 873 (Meister, 1965), gave comparable results. Yeast a-glucosidase (maltase) suspension, 2 mg protein/ml (20 U/ml) and galactose dehydrogenase (Galactose UV-test, TC-GA 15921 TGAN) were obtained from Boeh- ringer Mannheim Corporation (BMC), San Francisco, California. P-Galactosidase (lactase), derived from Escherichia coli, 5.5 mg protein/ml (398 U/mg)

5 citations

Patent
18 Jun 2002
TL;DR: A microorganism (A) of the family Enterobacteriaceae, positive for beta-galactosidase, arginine hydrolase, ornithine decarboxylase, production of acetoin, and utilization of citrate, glucose, mannitol, inositol, sorbitol, sucrose, melibiose, amygdalin and arabinose.
Abstract: A microorganism (A) of the family Enterobacteriaceae, positive for beta-galactosidase, arginine hydrolase, ornithine decarboxylase, production of acetoin, and utilization of citrate, glucose, melibiose, amygdalin and arabinose; and negative for lysine decarboxylase, deaminase, cytochrome oxidase and gelatinase, for production of hydrogen sulfide and indole, and for utilization of rhamnose. A microorganism (A) of the family Enterobacteriaceae that is: (a) positive for beta-galactosidase, arginine hydrolase, ornithine decarboxylase, production of acetoin, and utilization of citrate, glucose, mannitol, inositol, sorbitol, sucrose, melibiose, amygdalin and arabinose; and (b) negative for lysine decarboxylase, urease, tryptophan deaminase, cytochrome oxidase and gelatinase, for production of hydrogen sulfide and indole, and for utilization of rhamnose. Independent claims are also included for: (1) mutants of (A); and (2) method for producing a polysaccharide (PS) having the repeating unit (I) by culturing (A) or its mutants. 4)-alpha-L-Fucp-(1-4)-alpha-L-Fucp-(1-3)-beta-D-Glcp-(1- 3 1 alpha-D-Galp 3 1 beta-D-GlcpA 4 1 alpha-D-Galp where Fucp, Glcp, Galp and GlcpA = fucose, glucose, galactose and glucuronic acid residues, respectively.

5 citations


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