A Novel Method for the Quantification of White Wine Mannoproteins by a Competitive Indirect Enzyme-Linked Lectin Sorbent Assay (CI-ELLSA)

Autor: Simone Vincenzi, Matteo Marangon, Alberto De Iseppi, Mara Vegro, Andrea Curioni, Giovanna Lomolino
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Pharmaceutical Science
01 natural sciences
Lees
Article
Analytical Chemistry
lcsh:QD241-441
0404 agricultural biotechnology
lcsh:Organic chemistry
Yeasts
Drug Discovery
Physical and Theoretical Chemistry
wine
Enzyme Assays
Winemaking
mannoproteins
Wine
Membrane Glycoproteins
Chromatography
beta-Fructofuranosidase
biology
Chemistry
010401 analytical chemistry
Organic Chemistry
digestive
oral
and skin physiology
Lectin
food and beverages
04 agricultural and veterinary sciences
wine
mannoproteins
competitive indirect enzyme-linked lectin sorbent assay (CI ELLSA)
method
quantification
yeast invertase
040401 food science
Yeast
quantification
0104 chemical sciences
Chemistry (miscellaneous)
Concanavalin A
White Wine
biology.protein
method
Molecular Medicine
competitive indirect enzyme-linked lectin sorbent assay (CI ELLSA)
Fermentation
yeast invertase
competitive indirect enzyme-linked lectin sorbent assay (CI-ELLSA)
Zdroj: Molecules, Vol 23, Iss 12, p 3070 (2018)
Molecules
Volume 23
Issue 12
ISSN: 1420-3049
Popis: Mannoproteins (MPs) are cell wall proteoglycans released in wine by yeast during fermentation and ageing on lees, a procedure used for the production of several wines to enrich them in these components with consequences from both a technological and sensory point of view. Given the significance that wine MPs have for wine quality, winemakers would welcome a simple and accurate method for their quantification, as this would allow them to have a better control of this aspect at different winemaking stages. This study develops and validates a novel, simple and accurate method for MPs quantification in white wines based on a competitive indirect enzyme-linked lectin sorbent assay (CI-ELLSA), using the highly mannosylated yeast invertase as the standard. The method utilizes the lectin concanavalin A (ConA) as the immobilized ligand for MPs, and peroxidase, an enzyme rich in mannose, as the competitor for ConA. After addition of the peroxidase substrate, the intensity of the signal produced by the activity of this enzyme (absorbance at 450 nm) is inversely proportional to the amount of mannosylated proteins in the sample. Results have been validated on several wine styles including still, sparkling and sweet wines.
Databáze: OpenAIRE
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