Effect of mechanical denaturation on surface free energy of protein powders

Mohammad, Mohammad Amin; Grimsey, Ian M.; Forbes, Robert T.; Blagbrough, Ian S.; Conway, Barbara R.

doi:10.1016/j.colsurfb.2016.07.010

Cited by 12 publications

(2 citation statements)

References 43 publications

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“…In a ball mill, high-energy collisions exert intensive shear forces on a dry or wet sample, which often result in partial or even complete protein denaturation and which may cause protein molecule degradation, thereby potentially affecting its solubility (Mohammad et al, 2016). Liu et al (2021) subjected commercial gluten powder to a ball milling step for 0-40 min at 400 rpm.…”

Section: Ball Millingmentioning

confidence: 99%

Relevance of the air–water interfacial and foaming properties of (modified) wheat proteins for food systems

Janssen

Monterde

Wouters

2023

Comp Rev Food Sci Food Safe

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A shift from animal protein-to plant protein-based foods is crucial in transitioning toward a more sustainable global food system. Among food products typically stabilized by animal proteins, food foams represent a major category. Wheat proteins are ubiquitous and structurally diverse, which offers opportunities for exploiting them for food foam and air-water interface stabilization. Notably, they are often classified into those that are soluble in aqueous systems (albumins and globulins) and those that are not (gliadins and glutenins). However, gliadins are at least to an extent water extractable and thus surface active. We here provide a comprehensive overview of studies investigating the air-water interfacial and foaming properties of the different wheat protein fractions. Characteristics in model systems are related to the functional role that wheat proteins play in gas cell stabilization in existing wheat-based foods (bread dough, cake batter, and beer foam). Still, to further extend the applicability of wheat proteins, and particularly the poorly soluble glutenins, to other food foams, their modification is required. Different physical, (bio)chemical, and other modification strategies that have been utilized to alter the solubility and therefore the air-water interfacial and foaming properties of the gluten protein fraction are critically reviewed.Such approaches may open up new opportunities for the application of (modified) gluten proteins in other food products, such as plant-based meringues, whippable drinks, or ice cream. In each section, important knowledge gaps are highlighted and perspectives for research efforts that could lead to the rational design of wheat protein systems with enhanced functionality and overall an increased applicability in food industry are proposed.

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Section: Ball Millingmentioning

confidence: 99%

Relevance of the air–water interfacial and foaming properties of (modified) wheat proteins for food systems

Janssen

Monterde

Wouters

2023

Comp Rev Food Sci Food Safe

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“…In recent years, there has been a considerable interest in the use of denatured globular proteins as excipients in pharmaceutical formulations with improved emulsion stability and targeted delivery of active pharmaceutical ingredients. 45 For this purpose, milling would be a perfect solution for fast denaturation and modification of protein conformation eliminating the need for solvents.…”

Section: Effect Of Milling On Conformationalmentioning

confidence: 99%

Mechanochemically Induced Controlled Glycation of Lysozyme and Its Effect on Enzymatic Activity and Conformational Changes

Xing

Yaylayan

2019

J. Agric. Food Chem.

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Protein glycation through heating of a mixture of protein and reducing sugars is one of the most commonly used methods of protein modification; however, in most cases, this approach can lead to uncontrolled glycation. The hypothesis that mechanical energy supplied through ball milling can induce glycation of proteins was tested using a well-characterized enzyme lysozyme. The Q-TOF/MS analysis of the milled samples has indicated that the milling of sugar−protein mixtures in stainless steel jars for 30 min and at a frequency of 30 Hz generated mainly monoglycated proteins even with the highly reactive ribose. Increasing the sugar concentration or the milling time did not influence the overall yield or generate more glycoforms. Enzymatic activity measurements, FTIR, and fluorescence spectroscopic studies have indicated that milling of lysozyme alone leads to a significant loss in enzymatic activity and structural integrity in contrast to milling in the presence of sugars.

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Towards Controlling the Reactivity of Enzymes in Mechanochemistry: Inert Surfaces Protect β‐Glucosidase Activity During Ball Milling

et al. 2019

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The activity of b-glucosidases-the enzymes responsible for the final step in the enzymatic conversion of cellulose to glucose-can be maintained and manipulatedu nder mechanochemicalc onditions in the absence of bulk solvent, either through an unexpected stabilization effect of inert surfaces, or by alteringt he enzymatice quilibrium. The reported results illustrateu nique aspects of mechanoenzymatic reactions that are not observable in conventionala queous solutions. They also represent the first reported strategies to enhance activity and favor either direction of the reactionu nder mechanochemicalconditions.Celluloseist he most abundant biopolymer on Earth [1] and central to many strategies for developing renewable and sustainable alternatives to fossil resources for the production of fuels and chemicals. [2] The deployment of lignocellulosic biomass as ar enewable feedstocki sh indered by its recalcitrantn ature,i ncluding its poor solubility and low reactivity. [3] Additionally,c ellulose in lignocellulosic material is intricately mixed with the biopolymers hemicellulose andl ignin, [4] impeding its accessibility and separation, and requiring the use of harsh and wasteful conditions for biomass saccharification. [5] Whereas cellulosic materials in nature are degraded by mixtures of cellulase enzymes (exoglucanases, endoglucanases, b-glucosidases, etc.) secreted by microorganisms, the use of such enzymes in cellulose-based industries requires initial harsh physical and chemical pretreatment of the cellulosicm aterial, fore xample, with sulfuric acid. [6] Furthermore, since b-glucosidases (BGs)-enzymes responsible for cleavage of the b-(1-4)-glucosed imer (cellobiose)i nto glucose( Scheme 1)-are often limiting in cellulase mixtures, incomplete depolymerization is ac ommon problem. [7] Recently,w er eported that cellulases can catalyze the efficient hydrolysis of both microcrystalline cellulose (MCC) and raw lignocellulosic biomassd irectly into glucose without chemicalp retreatment. [8] This was made possible by am echanochemistry-based process termedr eactive aging (RAging), which consists of alternating cycles of brief mechanochemical activation by milling in the presence of am inute amount of water,f ollowed by aging [9] of the resulting moist powder at a mild temperature (45-55 8C). The volume of water used in RAging is significantly lower than in conventionals olutions or slurries, with the liquid-to-solidr atio (h) [10] below 1 mLmg À1 , consistentw ith liquid-assisted grinding (LAG) mechanochemical conditions. [11] By using near-stoichiometric amounts of water,t his solvent-free environment better mimics the conditions for whichc ellulases have been naturally selected for,a chieving af ast, efficient, and clean hydrolysis of crystalline cellulose or native biomass.F urthermore, RAging avoids the energy consumption associated with continuous heatinga nd stirring of large volumes of aqueous suspensions used in conventional processes and affords the highest glucose concentration reportedt od ate for...

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Effect of mechanical denaturation on surface free energy of protein powders

Cited by 12 publications

References 43 publications

Relevance of the air–water interfacial and foaming properties of (modified) wheat proteins for food systems

Relevance of the air–water interfacial and foaming properties of (modified) wheat proteins for food systems

Mechanochemically Induced Controlled Glycation of Lysozyme and Its Effect on Enzymatic Activity and Conformational Changes

Towards Controlling the Reactivity of Enzymes in Mechanochemistry: Inert Surfaces Protect β‐Glucosidase Activity During Ball Milling

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