The Wine Proteins: Origin, Characteristics and Functionality Andrea Curioni

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The wine proteins: origin, characteristics and functionality

Andrea Curioni
Dipartimento di Biotecnologie Agrarie
Centro interdipartimentale per la Ricerca in Viticoltura ed Enologia (CIRVE)

Università di Padova

1

The CIRVE campus in Conegliano

2

Protein Structure / Functionality

Aminoacid sequence

Protein

Size Charge

Protein structure

Hydrophobicity

Proprieties

Functionality

Environment

pH

Detectable

Solvent

effects

Ionic strength Temperature Etc.

3

Proteins in wine

Implications in wine

Hazing of white wines (negative)

–“Mouthfeel” and aroma –Foam volume and stability

The wine proteins

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Protein Haze in wine

Serious quality defect Prevention: Protein removal by bentonite treatments

Bottled wine
Precipitation

  • Flocculation
  • Coagulation

Bentonite

Other methods?

several drawbacks: Loss of aroma

Knowledge is needed

Cost Waste …..

The wine proteins

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Wine Proteins: Origin

Where do the wine proteins came from?

The wine proteins

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Wine Proteins: Origin

• The wine proteins derive from

Grape (mainly):

involved in wine hazing

 Microorganisms

The wine proteins

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Grape Proteins

• Accumulate after veraison

– with sugars

Low quantity

– ≈ hundreds mg/Kg

heterogeneous

- > 300 components

Few main components

Pocock et al. (2000) JAFC 48, 1637

The wine proteins

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The Grape Proteins similar in all the varieties

Sarry et al., 2004 Proteomics, 4, 201

pH

The wine proteins

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Grape Proteins: Identification by MS

PR-proteins

Sarry et al., 2004 Proteomics, 4, 201

10

The wine proteins

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Grape Proteins: the main components

Pathogenesis related (PR)-Proteins

THAUMATIN-LIKE PROTEINS (TLP, PR 5)

• ≈ 24 kDa

CHITINASES (PR 3)

• ≈ 30 kDa

– Osmotins – Beta-(1,3)-glucanases

The wine proteins

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Thaumatin-like Proteins (TLP)

• Antifungal activity • Expressed mainly in the berry • Several types

– main: VvTL1 (constitutive) – minor : VvTL2 (less present in healthy grapes), .

• Tattersall, et al. (1997). Plant Physiology 114, 759; Pocock et al. (2000)

• No sweet taste

• Peng, et al. (1997) J. Agric. Food Chem., 45, 4639

The wine proteins

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Chitinases

• Up to 13 isoforms (4 basic and 9 acidic) Derckel et al.(1996), Plant Sci. 119, 31 • Chitinolitic activity

• Main: class IV chitinase Robinson et al., 1997 Plant Physiol. 114, 771

Catalytic domain

CHITIN- BINDING DOMAIN

The wine proteins

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Chitinases

reduced

Chitinase activity

Chitinolytic activity detection after SDS-PAGE of

grape berries (1), wine (2) and pomegranate fruit

(3) proteins under (A)–(C) reducing and (D)–(F) nonreducing conditions. Gels contained (A), (D) 0.01, (B), (E) 0.05, and (C), (F) 0.10% glycol chitin. In (D)–(E), the arrowheads indicate the chitinase isoform retarded in the presence of glycol chitin.

Vincenzi and Curioni (2005) Electrophoresis, 26, 60

Not reduced

 Chitinase is active in wine  Chitinase can bind chitin

Percent chitin in the gel

  • 0.01 %
  • 0.05 %
  • 0.10 %

14

PR-Proteins

Pathogen defense

  • 1. Inducibility by
  • 2. Resistance

. pathogens
. acidic pH

. solvents
. abiotic stress
. proteolysis

Grape: only in part
PR-Proteins are
Constitutive

.Stable

The wine proteins

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What happens to the grape proteins during winemaking?

The wine proteins

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Proteins and winemaking

Proteins (but not PR-P)

1. Juice extraction

•Denaturation (acidic pH) •Degradation (proteases) •Precipitation (tannins)

Low pH

only PR-proteins

Grape Proteases

resist

2. Fermentation

Yeast Proteases

WINE

Alcohol

The wine proteins

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Proteins in wine: Quantity

Low concentration

10 – 250 mg/L

Large variability

(reported: < 1 mg/L - > 1 g/L).

Are proteins quantified correctly?

The wine proteins

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Quantification by the Smith assay of the protein recovered by the KDS method from different Prosecco and Manzoni Bianco wine samples. Data are expressed in BSA equivalents.

Vincenzi et al., AJEV 2005

N

°

Protein concentration wine
(mg/L) ± SD

123456789

Proseccoa Proseccoa Proseccoa Proseccoa Proseccoa Proseccoa Proseccoa Proseccoa Proseccoa
14.9 ± 1.9 15.5 ± 1.5 19.7 ± 0.5 15.7 ± 1.6 20.0 ± 0.5 14.2 ± 0.7 12.2 ± 2.6 14.1 ± 1.7 16.9 ± 1.3 14.7 ± 1.8
121.5 ± 2.9
30.5 ± 3.6 30.5 ± 3.6 26.5 ± 1.9
176.1 ± 9.3
328.0 ± 40.5
10 Proseccoa 11 Proseccob 12 Incrocio Manzoni 6.0.13a 13 Incrocio Manzoni 6.0.13a 14 Incrocio Manzoni 6.0.13a 15 Incrocio Manzoni 6.0.13a

A

Commercial bottled wines;

b

wine samples taken before bentonite fining.

16 Incrocio Manzoni 6.0.13b

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Grape/Juice vs Wine

Grape
WWiniene

Marangon et al. (2009) JAFC, 57, 4415

The wine proteins

2D-PAGE of wine proteins (cv. Manzoni Bianco) (Polesani, 2004, unpublished).

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Wine Proteins: Preparative Purification

1. Cation exchange chromatography

(SCX) for Chardonnay wine .

2. Hydrophobic interaction chromatography

(HIC, Phenyl Sepharose)

SDS-PAGE bands used for MS identification

SDS-PAGE and RP-HPLC profile of purified proteins

Gazzola et al., unpublished

21

Identification by Nano LC-MS/MS

band

C 1-2 C 4

  • sequence
  • protein

PREDICTED: Vitis vinifera class IV chitinase (CHI4D), mRNA

Class IV chitinase [Vitis vinifera]

LOC100232841, PREDICTED: Vitis vinifera VVTL1 (LOC100232841), mRNA

VVTL1 [Vitis vinifera]

LOC100256970, PREDICTED: Vitis vinifera hypothetical protein LOC100256970 (LOC100256970), mRNA
C 6-7 α

Vacuolar invertase 1, [Vitis Vinifera].

LOC100256970, PREDICTED: Vitis vinifera hypothetical protein LOC100256970 (LOC100256970), mRNA
C 6-7 β

Vacuolar invertase 1, [Vitis vinifera].

PREDICTED: Vitis vinifera thaumatin-like protein (TL3), mRNA
C 6-7 γ

Thaumatin-like protein [Vitis vinifera]

D 1-2-3- LOC100232841, PREDICTED: Vitis vinifera VVTL1

VVTL1 [Vitis vinifera].

  • 4
  • (LOC100232841), mRNA

  • E 1-2-3
  • Lipid transfer protein isoform 1 [Vitis vinifera]

Lipid Transfer Protein 1 [Vitis vinifera]. VVTL1 [Vitis vinifera].

LOC100232841, PREDICTED: Vitis vinifera VVTL1 (LOC100232841), mRNA
H 4 I 1
LOC100232841, PREDICTED: Vitis vinifera VVTL1 (LOC100232841), mRNA

VVTL1 [Vitis vinifera].

22

Gazzola et al.2011, unpublished

How do the wine protein behave to form haze?

The wine proteins

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Proteins and Haze formation

• 1. Protein denaturation

– Limiting step

• 2. Interactions (?) • 3. Insoluble particles

formation (invisible)
• 4. Aggregation

Visible HAZE

The wine proteins

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Proteins and Haze formation

1. Wine Protein denaturation

Can be reversible

Temperature (!)

– Other factors (?)

The wine proteins

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Thermal stability of wine proteins

Chitinase
TLP

Repeated DSC scans of chitinase from Sauvignon blanc showing a melt

temperature of 55 °C, no reversibility

of thermal unfolding

Repeated DSC scans of thaumatin-like

protein from Semillon showing a melt

temperature of 61 °C and some reversibility of thermal unfolding.

Falconer et al.; J. Agric. Food Chem.  2010, 58, 975.

Copyright © 2009 American Chemical Society

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Haze formation at 30°C

Effect of incubation at 30°C for 22 h on the

protein composition of wine.
(A) PAGE of proteins from Sauvignon blanc wine after 22 h at 30 °C. The wine was centrifuged and the obtained pellet washed with model wine. Proteins from 100 μL for control (before heating, C) and supernatant (after heating, S) and from 500 μL

Chitinase

of pellet (after heating, P) were loaded per

lane.

TLP

(B) Reverse phase (C8) HPLC chromatograms of unheated Sauvignon blanc wine (C) and

supernatant after 22 h at 30 °C (S).

Chitinase is more sensitive than LTP

Marangon et al; J. Agric. Food Chem.  2011, 59, 733-740.

Copyright © 2010 American Chemical Society

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Chitinases and haze

Wine Treatment with Chitin specific interaction with the chitin

binding domain of Chitinases

Proteins: - 29%
Haze : - 80%

(Bentonite: -90%)
(Bentonite: -100%)

Chitinase is strongly involved in wine hazing

Vincenzi et al. (2005) Am. J. Enol. Vitic. 6:3:246

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Proteins and Haze formation

The wine proteins do not form haze in model wine, but only in real wines!

  • model
  • real

2. interactions with other compounds

• the “factor(s) X”

– Sulfate – Tannins

The wine proteins

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Proteins and Haze formation

Sulfate

(Pocock et al. JAFC 2007,   55, 1799; Marangon et al. JAFC 2011,   59, 73)

SO4 > HPO4 > acetate- > Cl- > NO3

2-

  • 2 -
  • -

Hofmeister series:

• Remove water

• Promote Hydrophobic interactions

Model wine

Effect of increasing sulfate

concentration on the haze produced by heating wine proteins (150 mg/L) in model wine.

Effect of protein concentration and composition on haze

30

formed in model wine.

The wine proteins

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