Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A novel peptide bacteriocin produced by the lactic acid bacterium Carnobacterium piscicola JG126 isolated from spoiled ham was purified and characterized. This bacteriocin, designated piscicolin 126, inhibited the growth of several gram-positive bacteria, especially the food-borne pathogen Listeria monocytogenes, but had no effect on the growth of a number of yeasts and gram-negative bacteria. Bactericidal activity was not destroyed by exposure to elevated temperatures at low pH values; however, bactericidal activity was lost at high pH values, especially when high pH values were combined with an elevated temperature. Piscicolin 126 activity was not affected by catalase, lipase, or lysozyme but was destroyed by exposure to a range of proteolytic enzymes. Piscicolin 126 was purified to homogeneity and was found to be a peptide having a molecular weight of 4,416.6 +/- 1.9. A sequence analysis revealed that this compound is a cystibiotic (class IIa) bacteriocin containing 44 amino acid residues and one intrapeptide disulfide ring. Piscicolin 126 has regions of homology with some other bacteriocins obtained from lactic acid bacteria and is most closely related to sakacin P and pediocin PA-1 (levels of identity, 75 and 55%, respectively). Addition of piscicolin 126 to a devilled ham paste test food system inhibited the growth of L. monocytogenes for at least 14 days. Piscicolin 126 was more effective than two commercially available bacteriocin preparations tested in the same system.
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PMID:Characterization of the chemical and antimicrobial properties of piscicolin 126, a bacteriocin produced by Carnobacterium piscicola JG126. 870 82

The effectiveness of polyphosphates or lipases to increase the lytic activity of lysozyme was evaluated both on Listeria monocytogenes suspended in buffer and on growing cultures incubated at different temperatures. At 5 degrees C and 37 degrees C polyphosphates combined with lysozyme did not result in the decrease of the number of non-growing L. monocytogenes cells. At the same incubation conditions, the addition of lipase to lysozyme significantly enhanced the bactericidal activity of lysozyme to an extent determined by pH, NaCl concentration and temperature.
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PMID:Effect of combined lysozyme and lipase treatment on the survival of Listeria monocytogenes. 888 Mar 43

A method for the detection of hydrophobic patches on the surfaces of protein tertiary structures is presented. It delineates explicit contiguous pieces of surface of arbitrary size and shape that consist solely of carbon and sulphur atoms using a dot representation of the solvent-accessible surface. The technique is also useful in detecting surface segments with other characteristics, such as polar patches. Its potential as a tool in the study of protein-protein interactions and substrate recognition is demonstrated by applying the method to myoglobin, Leu/IIe/Val-binding protein, lipase, lysozyme, azurin, triose phosphate isomerase, carbonic anhydrase, and phosphoglycerate kinase. Only the largest patches, having sizes exceeding random expectation, are deemed meaningful. In addition to well-known hydrophobic patches on these proteins, a number of other patches are found, and their significance is discussed. The method is simple, fast, and robust. The program text is obtainable by anonymous ftp.
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PMID:A method for detecting hydrophobic patches on protein surfaces. 891 27

Lactobacillus amylovorus LMG P-13139, isolated from corn steep liquor, produces two bactericidal peptides with respective estimated molecular masses of 4.5 and 6.0 kDa upon denaturing sodium dodecyl sulfatepolyacrylamide gel electrophoresis. The antimicrobial activity detected in the fermentation supernatant fraction of L. amylovorus LMG P-13139 was heat stable (20 min, 121 degrees C), displayed a narrow inhibitory spectrum, and was sensitive to proteinase K, trypsin, and alpha-chymotrypsin but insensitive to alpha-amylase, lysozyme, catalase, and lipase. The 4.5-kDa bacteriocin was purified and characterized and designated lactobin A. Lactobin A was isolated as a floating pellicle from culture supernatant brought to 35% saturation with ammonium sulfate. Upon this ammonium sulfate treatment, crude lactobin A was incorporated, together with Tween 80 as a major contaminant, in high-molecular-mass complexes sized at approximately 670 kDa by gel filtration chromatography. Contaminating fatty acids were removed from these micelles by a simple one-step methanol-chloroform extraction without loss of activity. Both inhibitory peptides were separated in an isocratic isopropanol gradient on a PepRPC 5/5 reversed-phase column, and both peptides retained activity towards Lactobacillus helveticus ATCC 15009 upon separation. Lactobin A has a molecular mass determined by electrospray mass spectrometry of 4,879 +/- 0.69 Da. Its peptide chain contains 50 unmodified amino acids, of which 26% are glycine residues and 40% are hydrophobic residues (A, V, L, I, and P). It displays the highest structural homology (42% identity and 28% similarity) with the lafX gene product, encoded by the second open reading frame of the lactacin F operon. These data strongly indicate that lactobin A belongs to the class IIb bacteriocins according to the classification of Klaenhammer.
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PMID:Isolation, purification, and amino acid sequence of lactobin A, one of the two bacteriocins produced by Lactobacillus amylovorus LMG P-13139. 897 34

Three cases are presented where modified chitins have been extensively administered to volunteers, as dressings for wounded soft and bone tissues, as anticholesterolemic dietary foods, and in the controlled delivery of anti-inflammatory drugs. The interactions of the modified chitins with human enzymes is critically examined. In the context of drug carrier resorption and wound healing, chitooligomers and monomers, generated by lysozyme, N-acetylglucosaminidase and human chitinase, activate macrophages and stimulate fibroblasts, respectively; the effects are production of smooth, vascularized and physiologically normal tissues. In the dietary food area, lipase, amylase, 3-hydroxy-3-methylglutaryl CoA reductase, glucokinase and the enzymes of prostaglandin synthesis are involved in the oral administration of chitosan: lipid adsorption is depressed mainly because of the physical form of the chitosan-lipid aggregates, which are unsuitable as substrates. When chitosan is used as a drug carrier, chitosan-drug complexes are present. The uniqueness of chitosan among polysaccharides is underlined in terms of susceptibility to enzymatic depolymerization, cationicity, supply of cell-activating oligomers, and supply of N-acetylglucosamine for rebuilding of other biopolymers. Advances in molecular recognition and biocompatibility are also presented.
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PMID:Human enzymatic activities related to the therapeutic administration of chitin derivatives. 911 1

Atomic force microscopy (AFM) images at the molecular level have been obtained for a number of different protein and virus crystals. They can be utilized in some special cases to obtain information useful to crystal structure analyses by x-ray diffraction. In particular, questions of space group enantiomer, the packing of molecules within a unit cell, the number of molecules per asymmetric unit, and the dispositions of multiple molecules within the asymmetric unit may be resolved. In addition, because of the increasing sensitivity and resolution of the AFM technique, some molecular features of very large asymmetric units may be within reach. We describe here high-resolution studies, using AFM, to visualize individual molecules and viruses in their crystal lattices. These investigations included fungal lipase, lysozyme, thaumatin, canavalin, and satellite tobacco mosaic virus (STMV).
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PMID:Molecular resolution imaging of macromolecular crystals by atomic force microscopy. 912 39

Four bacteriocin producing lactic acid bacteria isolated from vegetables were identified as Lactococcus lactis strains on the basis of physiological and biochemical characteristics, carbohydrate fermentation patterns and analysis of total soluble protein pattern by SDS PAGE. The bacteriocins had a wide spectrum of activity as antagonism was detected not only towards a variety of lactic acid bacteria, but also to Staphylococcus aureus and Listeria monocytogenes. These bacteriocins were resistant to heating at 121 degree C for 15 minutes and showed highest activity at low pH (<5.0). They were inactivated by the proteolytic enzymes alpha-chymotrypsin and proteinase K, but not by lipase, alpha-amylase, catalase or lysozyme. These bacteriocinogenic Lactococcus strains were all immune to the bacteriocins produced as well as to commercial nisin. Bacteriocin producer culture supernatants showed a high degree (70 or 100%) of cross-reactivity in the nisin ELISA, suggesting similarity of the produced bacteriocins to nisin. The potential application of bacteriocin producing lactococci of vegetable origin for safety assurance of vegetable foods and controlling vegetable fermentations is discussed.
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PMID:Production of nisin-like bacteriocins by Lactococcus lactis strains isolated from vegetables. 926 41

Spectroscopic techniques (UV absorbance, circular dichroism, fluorescence emission and anisotropy, and light scattering) were used to investigate enzyme solubilization in Aerosol-OT (AOT) reversed micelles in which a bile salt, sodium taurocholate (NaTC), is used as a novel cosurfactant. NaTC significantly increases the water capacity and size of the reversed micelles through surfactant reorganization. The solubilization of several enzymes, including lysozyme, chymotrypsin, lipase, lipoxidase, carbonic anhydrase, and ribonuclease A, was demonstrated. These enzymes, ranging in mass from 10(4) to 10(5) Da, are incorporated in the micelles in stable, optically transparent solutions. Several other proteins were not successfully solubilized. The presence of NaTC in the reversed micelles significantly altered the conformations of the solubilized enzymes, apparently by promoting unfolding of the enzyme through interactions with the interior micellar interface. Lysozyme and lipase respond to solubilization in the AOT/NaTC micelles by altering their conformations to accommodate the micellar structure. The effect of NaTC is greatest for lysozyme, inducing a higher degree of order and helicity in the enzyme structure. Chymotrypsin, on the other hand, disrupts the micellar structure and reorganizes the surfactants to accommodate its own preferred conformation. Addition of NaTC to the reversed micelles causes a 3-fold increase in the enzymatic activity of solubilized chymotrypsin. Copyright 1997Academic Press
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PMID:Enzyme Solubilization in a Reversed Micellar Microreactor with a Bile Salt Cosurfactant 929 86

Bacteria isolated from radish were identified as Lactococcus lactis subsp. cremoris R and their bacteriocin was designated lactococcin R. Lactococcin R was sensitive to some proteolytic enzymes (proteinase-K, pronase-E, proteases, pepsin, alpha-chymotrypsin) but was resistant to trypsin, papain, catalase, lysozyme and lipase, organic solvents, or heating at 90 degrees C for 15, 30 and 60 min, or 121 degrees C for 15 min. Lactococcin R remained active after storage at -20 and -70 degrees C for 3 months and after exposure to a pH of 2-9. The molecular weight of lactococcin R was about 2.5 kDa. Lactococcin R was active against many food-borne pathogenic and food spoilage bacteria such as Clostridium, Staphylococcus, Listeria, Bacillus, Micrococcus, Enterococcus, Lactobacillus, Leuconostoc, Streptococcus and Pediococcus spp., but was not active against any Gram-negative bacteria. Lactococcin R was produced during log phase and reached a maximum activity (1600 AU ml-1) at early stationary phase. The highest lactococcin R production was obtained in MRS broth with 0.5% glucose, at 6.5-7.0 initial pH values, 30 degrees C temperature and 18-24-h incubation times. Lactococcin R adsorbed maximally to its heat-killed producing cells at pH 6-7 (95%). Crude lactococcin R at 1280 AU ml-1 was bactericidal, reducing colony counts of Listeria monocytogenes by 99.98% in 3 h. Lactococcin R should be useful as a biopreservative to prevent growth of food-borne pathogenic and food spoilage bacteria in ready-to-eat, dairy, meat, poultry and other food products. Lactococcin R differs from nisin in having a lower molecular weight, 2.5 kDa vs 3.4 kDa, and in being sensitive to pepsin and alpha-chymotrypsin to which nisin is resistant.
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PMID:Detection and characterization of a bacteriocin produced by Lactococcus lactis subsp. cremoris R isolated from radish. 1020 54

Human milk provides the infant with protection against infectious diseases. This protection is conferred through several mechanisms: specific antibody targeted protection against pathogens in the infant's environment (through milk IgA, IgG, and IgM) and broad-spectrum, nonspecific protection provided through several distinct mechanisms. These are: bactericidal effects (lactoferrin), bacteriostatic action (lactoferrin, lysozyme), lysis of microorganisms (lysozyme), antiviral effects (lactoferrin, products of milk fat digestion), antiprotozoan activity (free fatty acids produced during gastric and intestinal digestion of milk fat), and ligand action (inhibition of Helicobacter pylori adhesion to gastric mucosa by kappa-casein). In addition to these protective functions of the proteins and lipids of human milk, several enzymes present in human milk might provide protection by generating components that are bactericidal (bile salt dependent lipase, peroxidase), prevent inflammatory reactions (platelet-activating factor acetylhydrolase), or protect the integrity of milk proteins (antiproteases).
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PMID:Protective function of proteins and lipids in human milk. 969 Nov 57


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