Addition of Carrageenan at Different Stages of Winemaking for White Wine Protein Stabilization

2013 ◽  
Vol 61 (26) ◽  
pp. 6516-6524 ◽  
Author(s):  
Matteo Marangon ◽  
Vanessa J. Stockdale ◽  
Peter Munro ◽  
Timra Trethewey ◽  
Alex Schulkin ◽  
...  
Keyword(s):  
White Wine ◽  
Protein Stabilization

Assessment of Potential Effects of Common Fining Agents Used for White Wine Protein Stabilization

2012 ◽  
Vol 63 (4) ◽  
pp. 574-578 ◽  
Author(s):  
Ricardo Chagas ◽  
Sara Monteiro ◽  
Ricardo Boavida Ferreira
Keyword(s):  
White Wine ◽  
Protein Stabilization ◽  
Fining Agents

White Wine Continuous Protein Stabilization by Packed Column

2004 ◽  
Vol 52 (6) ◽  
pp. 1558-1563 ◽  
Author(s):  
Vesselina Pashova ◽  
Carme Güell ◽  
Francisco López
Keyword(s):  
Packed Column ◽  
White Wine ◽  
Protein Stabilization

scholarly journals Papain Covalently Immobilized on Chitosan–Clay Nanocomposite Films: Application in Synthetic and Real White Wine

Nanomaterials ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1622
Author(s):  
Ilaria Benucci ◽  
Claudio Lombardelli ◽  
Ilaria Cacciotti ◽  
Marco Esti
Keyword(s):  
Young Modulus ◽  
White Wine ◽  
Nanocomposite Materials ◽  
Covalent Immobilization ◽  
Protein Stabilization ◽  
Nanocomposite Films ◽  
Mechanical Resistance ◽  
Mechanical And Thermal Properties ◽  
Fixed Amount ◽  
Food Grade

Increasing attention has been recently paid to the development of nanocomposite materials for food application as new tool to enhance the mechanical and thermal properties of polymers. In this study, novel chitosan–clay nanocomposite films were produced as carriers for the covalent immobilization of papain, by using a fixed amount of chitosan (1% w/v) and a food-grade activated montmorillonite (Optigel, OPT) or a high-purity unmodified montmorillonite (SMP), in four different weight percentages with respect to chitosan (i.e., 20, 30, 50, 70% w/w). Both nanoclays (OPT and SMP) improved the mechanical properties of the obtained nanocomposites, and the OPT films showed the highest Young modulus and mechanical resistance (σmax). The nanocomposites were used as carriers for the covalent immobilization of papain, which was preliminarily characterized in model wine towards a synthetic substrate, showing the highest efficiency in the release of the reaction product when it was bound on OPT-30 and OPT-50 films. Finally, the latter biocatalyst (papain on OPT-50 film) was applied for the protein stabilization of two different unfined white wines, and it efficiently reduced both the haze potential and the protein content.

Preparation and Characterization of β-glucosidase Films for Stabilization and Handling in Dry Configurations

2020 ◽  
Vol 21 (8) ◽  
pp. 741-747
Author(s):  
Liguang Zhang ◽  
Yanan Shen ◽  
Wenjing Lu ◽  
Lengqiu Guo ◽  
Min Xiang ◽  
...  
Keyword(s):  
Tensile Strength ◽  
Protein Function ◽  
Protein Stabilization ◽  
Functional Protein ◽  
Elongation At Break ◽  
Gelatin Films ◽  
The Stability ◽  
And Function ◽  
General Method

Background: Although the stability of proteins is of significance to maintain protein function for therapeutical applications, this remains a challenge. Herein, a general method of preserving protein stability and function was developed using gelatin films. Method: Enzymes immobilized onto films composed of gelatin and Ethylene Glycol (EG) were developed to study their ability to stabilize proteins. As a model functional protein, β-glucosidase was selected. The tensile properties, microstructure, and crystallization behavior of the gelatin films were assessed. Result: Our results indicated that film configurations can preserve the activity of β-glucosidase under rigorous conditions (75% relative humidity and 37°C for 47 days). In both control films and films containing 1.8 % β-glucosidase, tensile strength increased with increased EG content, whilst the elongation at break increased initially, then decreased over time. The presence of β-glucosidase had a negligible influence on tensile strength and elongation at break. Scanning electron-microscopy (SEM) revealed that with increasing EG content or decreasing enzyme concentrations, a denser microstructure was observed. Conclusion: In conclusion, the dry film is a promising candidate to maintain protein stabilization and handling. The configuration is convenient and cheap, and thus applicable to protein storage and transportation processes in the future.

Protein Solvent Interaction: Transition of Protein-solvent Interaction Concept from Basic Research into Solvent Manipulation of Chromatography

2018 ◽  
Vol 20 (1) ◽  
pp. 34-39 ◽  
Author(s):  
Tsutomu Arakawa ◽  
Yoshiko Kita
Keyword(s):  
Column Chromatography ◽  
Rapid Development ◽  
Academic Research ◽  
Basic Research ◽  
Protein Stabilization ◽  
Special Issue ◽  
Solvent Interaction ◽  
Protein Formulations ◽  
Solvent Additive ◽  
Downstream Processes

Previously, we have reviewed in this journal (Arakawa, T., Kita, Y., Curr. Protein Pept. Sci., 15, 608-620, 2014) the interaction of arginine with proteins and various applications of this solvent additive in the area of protein formulations and downstream processes. In this special issue, we expand the concept of protein-solvent interaction into the analysis of the effects of solvent additives on various column chromatography, including mixed-mode chromatography. Earlier in our research, we have studied the interactions of such a variety of solvent additives as sugars, salts, amino acids, polymers and organic solvents with a variety of proteins, which resulted in mechanistic understanding on their protein stabilization and precipitation effects, the latter known as Hofmeister series. While such a study was then a pure academic research, rapid development of genetic engineering technologies and resultant biotechnologies made it a valuable knowledge in fully utilizing solvent additives in manipulation of protein solution, including column chromatography.

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