0000000000587021

AUTHOR

Raffaele Porta

showing 3 related works from this author

Fennel waste-based films suitable for protecting cultivations.

2007

Biodegradable, flexible, and moisture-resistant films were obtained by recycling fennel waste and adding to fennel homogenates the bean protein phaseolin that was modified or not modified by the enzyme transglutaminase. All films were analyzed for their morphology, mechanical properties, water vapor permeability, and susceptibility to biodegradation under soil-like conditions. Our experiments showed that transglutaminase treatment of the phaseolin-containing fennel waste homogenates allowed us to obtain films comparable in their mechanical properties and water vapor permeability to the commercial films Ecoflex and Mater-Bi. Furthermore, biodegradability tests demonstrated that the presence …

Time FactorsPolymers and PlasticsFennel waste-based filmFood HandlingOligonucleotidesIndustrial WasteBioengineeringBiocompatible MaterialsEnvironmentBioplasticIndustrial wasteBiomaterialschemistry.chemical_compoundBotanyMaterials ChemistryFood scienceCelluloseCellulosedegradationPlant ProteinsTransglutaminasesAgricultureFabaceaeBiodegradationEnvironmentally friendlyCarbonBacilluPhaseolinBiodegradation EnvironmentalchemistryFoeniculumPlant proteinMicroscopy Electron ScanningPectinsSpectrophotometry UltravioletValorisationPlasticsSettore AGR/16 - Microbiologia AgrariaBiomacromolecules
researchProduct

Mass spectrometric identification of the amino donor and acceptor sites in a transglutaminase protein substrate secreted from rat seminal vesicles.

1991

Four different transglutaminase-modified forms of a protein secreted by the rat seminal vesicles (SV-IV) were synthesized in vitro and characterized. FAB maps of both the native protein and its derivatives, produced by the purified guinea pig liver enzyme in the presence or absence of the polyamine spermidine, were obtained by mass spectrometric analysis after proteolytic digestions. Two differently derivatized SV-IV molecular forms, both possessing only one glutamine residue out of two (Gln-86) cross-linked to endogenous lysine residues, were produced when spermidine was omitted from the reaction mixture: (i) an insoluble homopolymer in which Lys-2, -4, -59, -78, -79, and -80 were involved…

MaleTissue transglutaminaseSeminal Plasma ProteinsLysineGuinea PigsMolecular Sequence DataBiochemistryMass SpectrometrySubstrate SpecificityResidue (chemistry)chemistry.chemical_compoundAnimalsAmino Acid Sequencechemistry.chemical_classificationIsopeptide bondTransglutaminasesbiologyHydrolysisSeminal Plasma ProteinsProstatic Secretory ProteinsProteinsSeminal VesiclesRats Inbred StrainsRatsSpermidineSecretory proteinchemistryBiochemistryLiverbiology.proteinPolyamineChromatography LiquidBiochemistry
researchProduct

Substance P inactivation by transglutaminase in vitro.

1992

Gamma(glutamyl5)spermine derivative of substance P (Spm-SP) was synthesized in vitro in the presence of purified guinea pig liver transglutaminase and Ca2+. The spermine adduct of the neuropeptide was purified by HPLC on a reversed-phase column and characterized by fast atom bombardment mass spectrometry. The biological activities of Spm-SP were tested by assaying, in comparison with substance P, its ability to induce both the contractions of smooth muscle in vitro and the edema formation in vivo. Spm-SP was shown not to elicit contractile responses in the isolated rat stomach strip and duodenum and not to antagonize the spasmogenic effect evoked by the native neuropeptide. Furthermore, Spm…

medicine.medical_specialtyPhysiologyGuinea PigsMolecular Sequence DataHistamine AntagonistsNeuropeptideSpermineSubstance PSubstance PPharmacologyBiochemistryCellular and Molecular Neurosciencechemistry.chemical_compoundEndocrinologyIn vivoInternal medicinemedicineAnimalsEdemaAmino Acid SequenceReceptorPeptide modificationTransglutaminasesChemistryExtremitiesMuscle SmoothBiological activityIn vitroEndocrinologyLiverHistamineMuscle Contraction
researchProduct