Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.10.3.2 (laccase)
 4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Food dispersions have become essential vehicles to carry and deliver functional ingredients such as bioactive compounds, flavors, antimicrobials, antioxidants, colors and vitamins. Most of these systems are thermodynamically unstable tending to break down over time. Much research has therefore been carried out to develop methodologies to improve their long-term stability. In this review, we will introduce readers to a new approach that has been developed over the past years to stabilize food dispersions, i.e. by use of various enzymes. First, basic design principles of modern food dispersions including conventional emulsions, multiple emulsions, multilayered emulsions, solid lipid particle suspensions, and liposomes are discussed. Enzymes able to generate intra- and intermolecular crosslinks between proteins and/or polysaccharides will be reviewed and specific reactions catalyzed by, e.g., transglutaminase, laccase, tyrosinase, sulfhydryl oxidase, glucose oxidase, lipoxygenase, polyphenol oxidase, peroxidase, and lysyl oxidase will be highlighted. Finally, potential applications of this enzymatic approach in the food industry will be critically discussed.
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PMID:Stabilization of food dispersions by enzymes. 2442 78

Oxidases are found to play a growing role in providing functional chemistry to marine adhesives for the permanent attachment of macrofouling organisms. Here, we demonstrate active peroxidase and lysyl oxidase enzymes in the adhesive layer of adult Amphibalanus amphitrite barnacles through live staining, proteomic analysis, and competitive enzyme assays on isolated cement. A novel full-length peroxinectin (AaPxt-1) secreted by barnacles is largely responsible for oxidizing phenolic chemistries; AaPxt-1 is driven by native hydrogen peroxide in the adhesive and oxidizes phenolic substrates typically preferred by phenoloxidases (POX) such as laccase and tyrosinase. A major cement protein component AaCP43 is found to contain ketone/aldehyde modifications via 2,4-dinitrophenylhydrazine (DNPH) derivatization, also called Brady's reagent, of cement proteins and immunoblotting with an anti-DNPH antibody. Our work outlines the landscape of molt-related oxidative pathways exposed to barnacle cement proteins, where ketone- and aldehyde-forming oxidases use peroxide intermediates to modify major cement components such as AaCP43.
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PMID:Oxidase Activity of the Barnacle Adhesive Interface Involves Peroxide-Dependent Catechol Oxidase and Lysyl Oxidase Enzymes. 2827 14