pectins and potassium-phosphate

pectins has been researched along with potassium-phosphate* in 3 studies

Other Studies

3 other study(ies) available for pectins and potassium-phosphate

ArticleYear
Impact of ingredient replacers on the physicochemical properties and sensory quality of reduced salt and fat black puddings.
    Meat science, 2016, Volume: 113

    Twenty-two black puddings possessing different fat (10%, 5%) and sodium (0.6%, 0.4%) levels were used as base formulations for 11 different salt and fat replacers. Compositional, physicochemical and sensory analyses were conducted. Black pudding samples with 5% fat and 0.6% sodium containing potassium chloride (KCl), potassium chloride and glycine mixture (KClG), and seaweed, respectively, and 10% fat and 0.4% sodium containing carrageen were rated higher (P<0.05) for spiciness and saltiness. Samples with 10% fat and 0.4% sodium containing KClG were rated positively (P<0.05) to fatness. Samples with 5% fat and 0.6% sodium containing pectin and a combination of potassium citrate, potassium phosphate and potassium chloride (KCPCl), as well as samples containing 10% fat and 0.4% sodium with waxy maize starch (WMS) were liked (P<0.05) for flavor and overall acceptance. The Food Safety Authority of Ireland (FSAI) recommends a sodium target level of 0.6% and an even lower sodium level (0.4%) was achieved.

    Topics: Carboxymethylcellulose Sodium; Chondrus; Citrates; Fats; Food Additives; Food Analysis; Food Handling; Glycine; Humans; Meat Products; Pectins; Phosphates; Potassium Chloride; Potassium Citrate; Potassium Compounds; Seaweed; Sensation; Sodium Chloride; Sodium Citrate; Taste

2016
Evaluation of an enzyme-containing capsular shaped pulsatile drug delivery system.
    Pharmaceutical research, 1999, Volume: 16, Issue:9

    To develop an enzymatically-controlled pulsatile drug release system based on an impermeable capsule body, which contains the drug and is closed by an erodible pectin/pectinase-plug.. The plug was prepared by direct compression of pectin and pectinase in different ratios. In addition to the disintegration times of the plugs, the lag times and the release profiles of the pulsatile system were determined as a function of pectin:enzyme ratio, the pH of the surrounding medium, and the addition of buffering or chelating agents.. The disintegration time of the plug, respectively the lag time prior to the drug release was controlled by the pectin:enzyme ratio and the plug weight. The inclusion of a buffering agent within the plug lead to a plug disintegration independent of the surrounding pH. The addition of N(alpha)-EDTA hindered the formation of non-soluble calcium pectinate in the presence of calcium ions in the environment. The addition of effervescent agents to the capsule content resulted in a rapid emptying of the capsule content after plug degradation.. A pulsatile drug delivery system based on an erodible pectin plug containing a pectinolytic enzyme was developed. The drug release was controlled by the enzymatic degradation and dissolution of pectin.

    Topics: Administration, Oral; Antidiarrheals; Buffers; Calcium Chloride; Capsules; Chelating Agents; Delayed-Action Preparations; Drug Delivery Systems; Edetic Acid; Hydrogen-Ion Concentration; Pectins; Phosphates; Polygalacturonase; Potassium Compounds; Pulse Therapy, Drug

1999
Molecular cloning and nucleotide sequence of the gene encoding phosphate-inducible pectin lyase of Bacillus subtilis.
    FEBS letters, 1996, Dec-02, Volume: 398, Issue:2-3

    The gene encoding the pectin lyase (PNL; EC 4.2.2.10) of Bacillus subtilis has been cloned, sequenced, and characterized. A coding sequence for the PNL composed of 345 amino acids including a 24-amino-acid signal peptide was assigned. No sequence resembling a LexA binding site was found upstream of the structural gene. Furthermore, PNL activity of the gene product expressed in Escherichia coli DH5alpha was detected intracellularly, which might suggest that expression of the gene was not controlled by RecA. Regulation of the gene expression seemed to be quite different from that of other bacterial PNL genes previously reported.

    Topics: Amino Acid Sequence; Bacillus subtilis; Base Sequence; Blotting, Southern; Cloning, Molecular; Enzyme Induction; Gene Expression Regulation, Bacterial; Genes, Bacterial; Glycosylation; Hydrogen-Ion Concentration; Molecular Sequence Data; Molecular Weight; Pectins; Phosphates; Polysaccharide-Lyases; Potassium Compounds; Protein Sorting Signals; Rec A Recombinases; Temperature

1996