Effects of ionic strength and sulfate upon thermal aggregation of grape chitinases and thaumatin-like proteins in a model system.
Identifieur interne : 000263 ( Main/Curation ); précédent : 000262; suivant : 000264Effects of ionic strength and sulfate upon thermal aggregation of grape chitinases and thaumatin-like proteins in a model system.
Auteurs : Matteo Marangon [Australie] ; Francois-Xavier Sauvage ; Elizabeth J. Waters ; Aude VernhetSource :
- Journal of agricultural and food chemistry [ 1520-5118 ] ; 2011.
Descripteurs français
- KwdFr :
- Chitinase (composition chimique), Cinétique (MeSH), Concentration osmolaire (MeSH), Conformation des protéines (effets des médicaments et des substances chimiques), Protéines végétales (composition chimique), Stabilité enzymatique (effets des médicaments et des substances chimiques), Sulfates (pharmacologie), Température élevée (MeSH), Vin (analyse), Vitis (composition chimique), Vitis (enzymologie).
- MESH :
- analyse : Vin.
- composition chimique : Chitinase, Protéines végétales, Vitis.
- effets des médicaments et des substances chimiques : Conformation des protéines, Stabilité enzymatique.
- enzymologie : Vitis.
- pharmacologie : Sulfates.
- Cinétique, Concentration osmolaire, Température élevée.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Chitinases, Plant Proteins.
- analysis : Wine.
- chemistry : Vitis.
- drug effects : Enzyme Stability, Protein Conformation.
- enzymology : Vitis.
- chemical , pharmacology : Sulfates.
- Hot Temperature, Kinetics, Osmolar Concentration.
Abstract
Consumers expect white wines to be clear. During the storage of wines, grape proteins can aggregate to form haze. These proteins, particularly chitinases and thaumatin-like proteins (TL-proteins), need to be removed, and this is done through adsorption by bentonite, an effective but inefficient wine-processing step. Alternative processes are sought, but, for them to be successful, an in-depth understanding of the causes of protein hazing is required. This study investigated the role played by ionic strength (I) and sulfate toward the aggregation of TL-proteins and chitinases upon heating. Purified proteins were dissolved in model wine and analyzed by dynamic light scattering (DLS). The effect of I on protein aggregation was investigated within the range from 2 to 500 mM/L. For chitinases, aggregation occurred during heating with I values of 100 and 500 mM/L, depending on the isoform. This aggregation immediately led to the formation of large particles (3 μm, visible haze after cooling). TL-protein aggregation was observed only with I of 500 mM/L; it mainly developed during cooling and led to the formation of finite aggregates (400 nm) that remained invisible. With sulfate in the medium chitinases formed visible haze immediately when heat was applied, whereas TL-proteins aggregated during cooling but not into particles large enough to be visible to the naked eye. The data show that the aggregation mechanisms of TL-proteins and chitinases are different and are influenced by the ionic strength and ionic content of the model wine. Under the conditions used in this study, chitinases were more prone to precipitate and form haze than TL-proteins.
DOI: 10.1021/jf104334v
PubMed: 21361294
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During the storage of wines, grape proteins can aggregate to form haze. These proteins, particularly chitinases and thaumatin-like proteins (TL-proteins), need to be removed, and this is done through adsorption by bentonite, an effective but inefficient wine-processing step. Alternative processes are sought, but, for them to be successful, an in-depth understanding of the causes of protein hazing is required. This study investigated the role played by ionic strength (I) and sulfate toward the aggregation of TL-proteins and chitinases upon heating. Purified proteins were dissolved in model wine and analyzed by dynamic light scattering (DLS). The effect of I on protein aggregation was investigated within the range from 2 to 500 mM/L. For chitinases, aggregation occurred during heating with I values of 100 and 500 mM/L, depending on the isoform. This aggregation immediately led to the formation of large particles (3 μm, visible haze after cooling). TL-protein aggregation was observed only with I of 500 mM/L; it mainly developed during cooling and led to the formation of finite aggregates (400 nm) that remained invisible. With sulfate in the medium chitinases formed visible haze immediately when heat was applied, whereas TL-proteins aggregated during cooling but not into particles large enough to be visible to the naked eye. The data show that the aggregation mechanisms of TL-proteins and chitinases are different and are influenced by the ionic strength and ionic content of the model wine. Under the conditions used in this study, chitinases were more prone to precipitate and form haze than TL-proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21361294</PMID><DateCompleted><Year>2011</Year><Month>07</Month><Day>12</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5118</ISSN><JournalIssue CitedMedium="Internet"><Volume>59</Volume><Issue>6</Issue><PubDate><Year>2011</Year><Month>Mar</Month><Day>23</Day></PubDate></JournalIssue><Title>Journal of agricultural and food chemistry</Title><ISOAbbreviation>J Agric Food Chem</ISOAbbreviation></Journal><ArticleTitle>Effects of ionic strength and sulfate upon thermal aggregation of grape chitinases and thaumatin-like proteins in a model system.</ArticleTitle><Pagination><MedlinePgn>2652-62</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jf104334v</ELocationID><Abstract><AbstractText>Consumers expect white wines to be clear. During the storage of wines, grape proteins can aggregate to form haze. These proteins, particularly chitinases and thaumatin-like proteins (TL-proteins), need to be removed, and this is done through adsorption by bentonite, an effective but inefficient wine-processing step. Alternative processes are sought, but, for them to be successful, an in-depth understanding of the causes of protein hazing is required. This study investigated the role played by ionic strength (I) and sulfate toward the aggregation of TL-proteins and chitinases upon heating. Purified proteins were dissolved in model wine and analyzed by dynamic light scattering (DLS). The effect of I on protein aggregation was investigated within the range from 2 to 500 mM/L. For chitinases, aggregation occurred during heating with I values of 100 and 500 mM/L, depending on the isoform. This aggregation immediately led to the formation of large particles (3 μm, visible haze after cooling). TL-protein aggregation was observed only with I of 500 mM/L; it mainly developed during cooling and led to the formation of finite aggregates (400 nm) that remained invisible. With sulfate in the medium chitinases formed visible haze immediately when heat was applied, whereas TL-proteins aggregated during cooling but not into particles large enough to be visible to the naked eye. The data show that the aggregation mechanisms of TL-proteins and chitinases are different and are influenced by the ionic strength and ionic content of the model wine. Under the conditions used in this study, chitinases were more prone to precipitate and form haze than TL-proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Marangon</LastName><ForeName>Matteo</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>The Australian Wine Research Institute, P.O. 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