Influence of pH on the Structure and Function of Kiwi Pectin Methylesterase Inhibitor
| Autor: | Alfonso Giovane, Rossana D'Avino, Alessandro Bonavita, Maria Antonietta Ciardiello, Luigi Servillo, Vitale Carratore |
|---|---|
| Přispěvatelé: | Bonavita, Alessandro, Carratore, Vitale, Ciardiello, Maria Antonietta, Giovane, Alfonso, Servillo, Luigi, D'Avino, Rossana |
| Rok vydání: | 2016 |
| Předmět: |
0106 biological sciences
0301 basic medicine Models Molecular Circular dichroism food.ingredient Pectin protein-inhibitor interaction Actinidia Molecular Sequence Data pectin methylesterase Cleavage (embryo) 01 natural sciences thiol-disulfide reshuffling 03 medical and health sciences food kiwi pectin methylesterase inhibitor (PMEI) Amino Acid Sequence Enzyme Inhibitors unfolding Plant Proteins chemistry.chemical_classification Actinidia deliciosa biology Circular Dichroism Chemistry (all) pH-induced conformational changes food and beverages Plant physiology General Chemistry Protein Biochemistry Hydrogen-Ion Concentration biology.organism_classification Enzyme assay pH-induced conformational change pH-dependent protein stability 030104 developmental biology Enzyme Agricultural and Biological Sciences (all) chemistry Biochemistry biology.protein General Agricultural and Biological Sciences Carboxylic Ester Hydrolases iosa 010606 plant biology & botany |
| Zdroj: | Journal of agricultural and food chemistry (2016). doi:10.1021/acs.jafc.6b01718 info:cnr-pdr/source/autori:Alessandro Bonavita, Vitale Carratore, Maria Antonietta Ciardiello, Alfonso Giovane, Luigi Servillo, and Rossana D'Avino/titolo:Influence of pH on the Structure and Function of Kiwi Pectin Methylesterase Inhibitor/doi:10.1021%2Facs.jafc.6b01718/rivista:Journal of agricultural and food chemistry/anno:2016/pagina_da:/pagina_a:/intervallo_pagine:/volume |
| ISSN: | 1520-5118 |
| DOI: | 10.1021/acs.jafc.6b01718 |
| Popis: | Pectin methylesterase is a pectin modifying enzyme that plays a key role in plant physiology. It is also an important quality-related enzyme in plant-based food products. The pectin methylesterase inhibitor (PMEI) from kiwifruit inhibits this enzyme activity and is widely used as an efficient tool for research purposes and also recommended in the context of fruit and vegetable processing. Using several methodologies of protein biochemistry, including circular dichroism and fluorescence spectroscopy, chemical modifications, direct protein-sequencing, enzyme activity, and bioinformatics analysis of the crystal structure, this study demonstrates that conformational changes occur in kiwi PMEI by the pH rising over 6.0 bringing about structure loosening, exposure, and cleavage of a natively buried disulfide bond, unfolding and aggregation, ultimately determining the loss of ability of kiwi PMEI to bind and inhibit PME. pH-induced structural changes are prevented when PMEI is already engaged in complex or is in a solution of high ionic strength. |
| Databáze: | OpenAIRE |
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