muramidase and maltodextrin

muramidase has been researched along with maltodextrin* in 5 studies

Reviews

1 review(s) available for muramidase and maltodextrin

ArticleYear
Oral rehydration solutions in non-cholera diarrhea: a review.
    The American journal of gastroenterology, 2009, Volume: 104, Issue:10

    The use of oral rehydration solution (ORS) has revolutionized the management of acute diarrhea. The implementation of the standard World Health Organization ORS (WHO-ORS) has resulted in decreased mortality associated with acute diarrheal illnesses in children, although in general stool volume and diarrhea durations are not reduced. Decreased morbidity and mortality have occurred because of improved hydration status. Decreased morbidity has also been described in adults who used this therapy. Various modifications to the standard ORS have been derived. These modifications have included hypo-osmolar or hyperosmolar solutions, use of rice-based ORS, zinc supplementation, and the use of amino acids, including glycine, alanine, and glutamine. Some of these variations have been successful, some have not, and others are still under investigation. ORS has been used for travelers' diarrhea and to decrease intravenous (IV) fluid requirements in patients with short bowel syndrome (SBS) who require parenteral nutrition (PN). This paper reviews the standard WHO-ORS and its mechanism of action, followed by more contemporary reduced osmolarity ORS and rice-based ORS in non-cholera diarrhea. Various modifications to improve ORS are also discussed.

    Topics: Amino Acids; Animals; Bicarbonates; Clinical Trials as Topic; Diarrhea; Flavoring Agents; Fluid Therapy; Glucose; Humans; Lactoferrin; Muramidase; Oryza; Osmolar Concentration; Polysaccharides; Potassium Chloride; Sodium Chloride; Zinc

2009

Other Studies

4 other study(ies) available for muramidase and maltodextrin

ArticleYear
Use of a maltodextrin-based feed with a lysozyme product to alter bacterial in the ileum of market-aged broilers.
    Poultry science, 2019, Dec-01, Volume: 98, Issue:12

    Poultry meats can become contaminated with pathogenic bacteria through digesta leakage during processing. Reducing the bacteria load in digesta of market-aged broilers prior to processing reduces the incidence of fecal contamination at the processing plant. A lysozyme product was incorporated in a maltodextrin-based feed offered during the pre-shipping feed withdrawal period to reduce bacteria in ileal contents of market-aged broilers. Twenty 36-day-old broilers were randomly allocated to each of 16 pens. For a 9 h period each pen was randomly assigned to one of the following treatments: no feed, maltodextrin-based feed with a lysozyme product (Inovapure) added at 0, 10, or 20 g per kg of feed. Feed consumption was determined and a minimum of 3 birds were randomly selected from each pen and euthanized. The ileal contents were removed and weighed. Samples were analyzed for Clostridium perfringens, aerobic bacteria, Enterobacteriaceae, E. coli, and coliform numbers using standard culturing techniques and next generation sequencing was performed to determine population shifts. Bacteria counts were transformed to log10 colony forming units (cfu) and analyzed as a completely randomized design. The data from next generation sequencing was analyzed as a 3 × 5 factorial design using Proc Mixed of SAS. Lysozyme did not affect feed consumption nor were the weight of ileal contents different for birds fed maltodextrin-based feeds compared to birds on traditional feed withdrawal. E. coli/coliforms and Enterobacteriaceae plates had no signs of bacterial growth. The number of Clostridium perfringens and aerobic bacteria in the ileal contents of market-aged broilers was not different between treatments using the traditional culturing techniques. Next generation sequencing was a useful alternative to traditional culture techniques as results revealed that bacilli were reduced and clostridia increased for the 20 g lysozyme treatment. Addition of lysozyme to a maltodextrin based feed did not change overall numbers of bacteria but was effective in altering the participants in the bacteria community in ileal contents of market-aged broilers.

    Topics: Animal Feed; Animals; Chickens; Diet; Dietary Supplements; Dose-Response Relationship, Drug; Ileum; Male; Muramidase; Polysaccharides; Random Allocation

2019
Protein spheres prepared by drop jet freeze drying.
    International journal of pharmaceutics, 2012, Nov-15, Volume: 438, Issue:1-2

    In spray freeze drying (SFD) solutions are frozen by spraying into a very cold environment and subsequently dried by sublimation. In contrast to conventional freeze drying, spray freeze drying has the possibility to produce flowable lyophilizates which offers a variety of new pharmaceutical applications. Here, a drop jet nozzle is proposed as liquid dispenser that is able to produce droplets with a very narrow size distribution compared to standard methods. The drop jet nozzle is mounted in a spray tower designed to prevent direct contact of the product with the freezing medium. Various formulations have been tested containing lysozyme as model protein and stabilizers such as bovine serum albumin, polyvinylpyrrolidone or dextran in various concentrations and mannitol. Excellent free flowing and nearly monodispersed, porous particles are produced where particle properties can be controlled by formulation and process conditions. The particle diameter varied between 231 ± 3 μm and 310 ± 10 μm depending on the formulation composition. The lysozyme activity was >94 ± 5% for all formulations exhibiting a full preservation of enzyme activity. This new method is very promising for the production of nearly monodisperse particulate lyophilizates in various therapeutic applications.

    Topics: Drug Compounding; Freeze Drying; Mannitol; Muramidase; Particle Size; Polysaccharides; Porosity; Povidone; Serum Albumin, Bovine; Surface Properties; Viscosity

2012
Aqueous two-phase protein partitioning using textile dyes as affinity ligands.
    Analytical biochemistry, 1991, Sep-02, Volume: 197, Issue:2

    A simple and inexpensive aqueous two-phase system for the affinity partitioning of proteins is introduced. An aqueous solution consisting of maltodextrin (M100; molecular mass, 1800) and polyvinylpyrrolidone (PVP360; molecular mass, 360,000) formed two phases at 4 degrees C when the concentration of the polymers was 22.5% (w/w) and 4.0% (w/w), respectively. When the amino derivatives of chlorotriazine textile dyes or other azo textile dyes were added to the two-phase system they partitioned asymmetrically, favoring the upper, less dense, PVP360-rich phase. The association of the textile dyes with PVP360 did not prevent them from acting as affinity ligands for proteins. Three of the dyes screened increased the partition coefficient of purified lysozyme nearly 50-fold over a control containing no dye. Parameters such as pH, ionic strength, and dye concentration modulated the affinity-partitioning effect of the system. The partition coefficient of lysozyme in an egg white protein mixture increased severalfold as the total protein content of the system approached 4% (w/w), indicating that protein concentration is also important in determining the partitioning characteristics of this two-phase system. Proteins were efficiently freed of PVP360 and textile dye by recovery in a high-salt solution when another two-phase system was formed upon the addition of a solution of concentrated potassium phosphate to the isolated upper phase of a PVP360/M100/textile dye two-phase system. The affinity-partitioning system presented here allows one to screen large numbers of potentially useful protein ligands to optimize protein separation, followed by direct scaleup to a system size determined by the user.

    Topics: Affinity Labels; Chemical Fractionation; Coloring Agents; Egg Proteins; Ligands; Muramidase; Polysaccharides; Povidone; Proteins; Solubility; Solutions

1991
THE CELL-BOUND ALPHA-AMYLASES OF STREPTOCOCCUS BOVIS.
    The Biochemical journal, 1965, Volume: 94

    1. The cell-bound alpha-amylase of Streptococcus bovis has been isolated from other carbohydrases in the cell extract by chromatography on DEAE-cellulose. The enzyme has been compared with the extracellular alpha-amylase produced by this organism. 2. The two amylases had similar action patterns on amylose, the main product being maltotriose with smaller amounts of maltose and a little glucose. 3. The cell-bound amylase hydrolysed maltopentaose and maltohexaose at a similar rate to the hydrolysis of amylose. Maltotetraose was hydrolysed six times more slowly, and maltotriose 280 times more slowly, than amylose. 4. Studies with end-labelled maltodextrins revealed that the cell-bound alpha-amylase preferentially hydrolysed the third linkage from the non-reducing end, liberating maltotriose. The linkage at the reducing end of maltotriose was more easily hydrolysed than the other. 5. Egg-white lysozyme and the extracellular enzymes of Streptomyces albus lysed the cell walls of Streptococcus bovis, releasing amylase into the medium. In the presence of 0.6 m-sucrose 10% of the maximal amylase activity was released by lysozyme. Suspension of the spheroplasts in dilute buffer caused the rupture of the cytoplasmic membrane and the liberation of amylase. 6. A sensitive method for determining the ability of amylases to degrade starch granules is described.

    Topics: alpha-Amylases; Amylases; Bacteriolysis; Biochemical Phenomena; Biochemistry; Chromatography; Galactosidases; Hydrolysis; Maltose; Muramidase; Oligosaccharides; Polysaccharides; Protoplasts; Research; Starch; Streptococcus; Streptococcus bovis; Sucrose; Trioses; Trisaccharides; Trypsin

1965