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.

Method for producing fructosyl valyl histidine oxidase preparation

Abstract: Object An object of the present invention is to provide a highly stable FVHO preparation and a low-hygroscopicity dried FVHO preparation. Means for achieving the object A method for producing a FVHO preparation comprising a step of allowing at least one member selected from phosphoric acid, casein peptone, D-glucosamine hydrochloride, melibiose, sorbose, lactose, fructose, melezitose, glucono-1,5-lactone, and ribitol; and a method for producing a dried FVHO preparation, comprising a step of allowing Bicine to coexist.

Salt-resistant proteinase-resistant alpha-galactosidase AgaAHJ8 and gene thereof

Abstract: The invention discloses a salt-resistant proteinase-resistant alpha-galactosidase AgaAHJ8 and a gene thereof. The invention provides an alpha-galactosidase AgaAHJ8 of which the amino acid sequence is disclosed as SEQ ID NO.1, a gene agaAHJ8 for coding the alpha-galactosidase, a recombinant vector comprising the gene, and a recombinant strain comprising the gene. The alpha-galactosidase can maintain the enzyme activity at 72% above when the pH value is 4.0-8.0. The optimum temperature is 50 DEG C, and the alpha-galactosidase is stable at 37 DEG C. The alpha-galactosidase has favorable salt resistance and proteinase resistance, and can hydrolyze melibiose, raffinose and guar gum. The alpha-galactosidase AgaAHJ8 is applicable to the field of processing of high-salt food and marine products, and is especially applicable to fermentation of high-salt food (such as high-salt diluted soy sauce).

Production, purification, characterization, and applications of α-galactosidase from Bacillus flexus JS27 isolated from Manikaran hot springs

Abstract: Abstract α-Galactosidase hydrolyzes the α-1,6-linkage present at the non-reducing end of the sugars and results in the release of galactosyl residue from oligosaccharides like melibiose, raffinose, stachyose, etc. In the present study we report, α-galactosidase from Bacillus flexus isolated from Manikaran hot springs (India). Maximum enzyme production was obtained in guar gum and soybean meal after 72 h at 150 rpm. While, the temperature/pH of production was optimized at 50 °C and 7.0, respectively. Isoenzymes (α-gal I and II) were obtained and characterized based on temperature/pH optima along with their stability profile. JS27 α-Gal II was purified with a final purification fold of 11.54. Native and SDS-PAGE were used to determine the molecular weight of the enzyme as 86 and 41 kDa, respectively, indicating its homodimeric form. JS27 α-Gal II showed optimum enzyme activity at 55 °C and pH 7 (10 min). The enzyme displayed Km value of 2.3809 mM and V max of 2.0 × 104 µmol/min/ml with pNPG as substrate. JS27 α-Gal II demonstrated substrate hydrolysis and simultaneous formation of transgalactosylation products (α-GOS) with numerous substrates (sugar/sugar alcohols, oligosaccharides, and complex carbohydrates) which were verified by TLC and HPLC analysis. α-GOS are significant functional food ingredients and can be explored as prebiotics.

A study on fungal speciation and drug susceptibility testing

Abstract: Fungal infections affect many people but most of these do not come to light as they are mild in clinical presentation. Candidiasis is the frequent fungal infection involving mucosa, skin, nails and internal organs caused by different species of Candida and Candida albicans being the prototype. The clinical manifestations vary with duration and severity. It occurs mostly as a comorbid disease with a primary disease or disorder. Candida comes under the phylum Fungi Imperfecti, order Moniliales and family Cryptococcaceae. Genus Candida comprises of 20 important species recognised as pathogenic in humans, of which 7 are renowned opportunistic pathogens. The following are some of the known species: Candida albicans, Candida tropicalis, Candida krusei, Candida glabrata, Candida guilliermondii, Candida parapsilosis, Candida lusitaniae, Candida kefyr, Candida rugosa, Candida dubliniensis and Candida viswanathii. Among all the fungi, 600 species are identified to be causing infections in human. Candida albicans being one of the normal human commensals may cause infections from mild to severe forms, which is influenced by molecules that helps in adhesion and invasion, hydrolases, yeast to hyphal transition, biofilms etc. In general, equal importance has not been give to fungal infections as is being given for bacterial infections. Nowadays newly emerging species are on the tract as to cause infections and their identification profile being indeterminate, which could be confirmed only by molecular methods. Overall C.tropicalis was the frequent species causing infections clinically and resistance was demonstrated against azoles and caspofungin by C.albicans and C.krusei. This may be due to extensive use of echinocandins as empirical therapy without susceptibility testing which can increase the development of resistance and may deduct treatment options. Hence, routine antifungal susceptibility testing has to be done. Out of all these things accurate epidemiological analysis and data can be provided regarding the burden of fungal infections around the globe. As tip of the iceberg, most of the fungal infections are not being reported as it is unnoticed without prominent clinical presentation and due to lack of complete documentation.

A mutant sialidase having trans-sialidase activity for use in production of sialylated glycans

Abstract: The invention provides a mutant enzyme having trans-sialidase activity (EC 3.2.1.18), characterized by an enhanced trans-sialidase:sialidase ratio when compared to its parent sialidase enzyme. Further the enzyme may be used in a method for trans-sialylating mono- and oligo-saccharides, including galacto-oligosaccharides (GOS), fructo-oligosaccharides (FOS), malto-oligosaccharides (MOS), isomalto-oligosaccarides (IMO), lactulose, melibiose, maltose, glycosyl sucrose, lactosucrose and fucose. Trans-sialidated mono- and oligo- saccharides, produced with the mutant enzyme, are useful in preparing infant formula, a prebiotic nutritional supplement, and a food supplement.