Water Holding Capacity

Water holding capacity (WHC) is the ability of food to hold its own or added water during the application of force, pressure, centrifugation, or heating.

From: Trends in Food Science & Technology , 2016

The Eating Quality of Meat—IV Water-Holding Capacity and Juiciness

Robyn D. Warner , in Lawrie´s Meat Science (Eighth Edition), 2017

Abstract

Water-holding capacity (WHC) of meat and meat products determines the visual acceptability, weight loss, and cook yield as well as sensory traits on consumption. WHC is defined, and the muscle structure and protein influences on WHC of raw and cooked muscle are described. The influence of postmortem pH fall; pale, soft, and exudative; and dark, firm, and dry; aging; electrical stimulation; vacuum packing; freezing; and thawing on WHC are explained. The changes in structure as a result of cooking and also processing are presented as well as the influence of high-pressure processing, salting pre- and postrigor, ionic strength, phosphates, and marination. Finally, methods for measuring WHC are defined, and a summary and conclusions are given.

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Functional Properties of Gum Arabic

Abdalbasit A. Mariod , in Gum Arabic, 2018

Water-holding capacity

Water-holding capacity (WHC) is the ability of the material to hold water against gravity. The range value of WHC for A. senegal gum was 65.40–65.80 (Omer, 2004). Due to the high water-holding properties of the gum, the gum imparts a smooth texture to the frozen product by inhibiting the formation of ice crystals (Omer, 2004). Kheir (2005) studied some functional properties (WHC and the emulsifying stability) of eight GA formulations, namely, handpicked selected, cleaned, sifting, kibbled 105, kibbled 107, kibbled 119, kibbled 121, and spray dried in an attempt to set standard specifications for each. She noticed that the formulations were varied between raw and processed GA of A. senegal as the influence of processing on properties of GA. The author found that WHC expressed as percentages was highly significantly different between eight GAF. The maximum WHC was recorded in the kibbled 107 (69.7%) and spray-dried (69.5%) formulations. The least WHC was recorded in kibbled 105 forms. The water solubility showed some variations among the different gum formulations, with the highest for the spray dried (98.80%) and the lowest for the sifting formulation (97.40%). However, the solubility in organic solvents (ethanol, acetone, and chloroform) had been generally very low yet with variations among the different formulations. Kheir (2005) reported that the WHC expressed as percentages was highly significantly different between eight GAF. Soibe et al. (2015) researched the impact of partial replacement of wheat with 10%–40% plantain and 1, 2, and 3% GA on composite bread quality attributes. They reported that the difference between the control and the composites was statistically significant (p < 0.05) at all levels of plantain incorporation of WHC, foaming capacity, emulsion capacity, and bulk density. GA, as used in this study, was found to improve the bread's textural qualities, as a significantly softer and more springy bread was produced.

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Gene and Protein Expression as a Tool to Explain/Predict Meat (and Fish) Quality

B. Picard , ... K. Hollung , in New Aspects of Meat Quality, 2017

3.3.3 Water-Holding Capacity

WHC is the ability of the meat to retain its own water or water added during the application of any force (Honikel and Hamm, 1994). The main myofibrillar proteins, myosin, actin, tropomyosin, and troponin, are the major muscle components able to retain water in meat. It has been shown that the postmortem events, such as the amplitude and rate of pH decline, proteolysis, and even protein oxidation, are the key factors that influence the WHC of a meat (Huff-Lonergan and Lonergan, 2005). Using a proteomic approach, Hwang (2004) showed a strong relationship between high water losses and the rate of postmortem proteolysis of pig Longissimus dorsi muscle. The author identified four proteins related to WHC: troponin T, adenylate kinase, adenosine triphosphate (ATP)-dependent proteinase SP-22 (currently listed under the name Prdx3), and the DJ-1 protein encoded by PARK7. In another study, van de Wiel and Zhang (2007) analyzed the pork muscle proteome and proposed protein markers related to the processes that may cause water drip loss. The major proteins were creatine phosphokinase type M, desmin, and an activator of transcription. Thus, samples with the highest water losses were characterized by an overabundance of creatine phosphokinase M type, inducing a rapid pH drop and alteration of the rate of muscle contraction. In addition, it was suggested that high levels of desmin observed in samples with lower WHC would increase the lateral shrinkage of myofibrils during the rigor mortis and therefore a modification of the compartmentalization of the water in muscle tissue, leading to considerable water loss. Phongpa-Ngan et al. (2011) analyzed the proteomes of chickens from two extreme groups of WHC (high vs. low) by 2DE and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). They revealed five proteins with higher abundance in the group of high WHC and one protein with higher abundance in the low-WHC group. These proteins (Table 12.2) correspond to metabolic enzymes, such as pyruvate kinase, triosephosphate isomerase, and some Hsps. Yu et al. (2009) analyzed more particularly the involvement of Hsps in the phenomenon of water loss. They tested four Hsps (αB-crystallin, Hsp27, Hsp70, and Hsp90) whose abundance measured by enzyme-linked immunosorbent assay (ELISA) in the Longissimus dorsi (LD) muscle of pigs tended to decline after the transport of animals. The authors revealed a close relationship between the decrease of the expression of Hsps and increasing water loss. Di Luca et al. (2013a,b) used 2DE DIGE to identify biomarkers of WHC meat to be ultimately used for industrial purposes. Among 44 proteins showing a modification of abundance during the postmortem period, only the abundance of Hsp70 was found to be related to WHC. Therefore, the authors suggested that Hsp70 chaperone could play a protective role against cleavage and aggregation of proteins.

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EMULSIFIERS | Phosphates as Meat Emulsion Stabilizers

L. Knipe , in Encyclopedia of Food Sciences and Nutrition (Second Edition), 2003

Water-Holding Capacity of Meat Emulsions

The water-holding capacity of meat could be compared to the action of a sponge and is important to meat processing in that as proteins are able to hold more water they become more soluble. The water-holding capacity of meat is at a minimum at the isoelectric point (pI) of meat proteins. At this point, equal positive and negative charges on the protein molecules result in a maximum number of bonds between peptide chains and a net charge equal to zero. The pI of meat (where water-holding capacity is at a minimum) is in the pH range of 5.0–5.4, which is also the ultimate pH of meat or the pH of meat after it has gone through rigor mortis.

The water-holding capacity of meat is greatly affected by pH. Increasing or decreasing the pH on either side of the pI will result in an increased water-holding capacity by creating a charge imbalance. A charge imbalance is a predominance of either positive or negative charges which will result in a repulsion of the charged protein groups of the same (positive or negative) charge. This repulsion results in increased capacity for water retention and could be compared to the repulsive effect of like charges on two magnets.

An increase in predominance of negative protein charges, due to the addition of phosphates, may also cause better distribution of fat particles in emulsified products. The better fat particle distribution may prevent the clumping of fat particles that occurs during overchopping and which results in an unstable emulsion.

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REFRIGERATION AND FREEZING TECHNOLOGY | Freezing and Product Quality

K. Rosenvold , in Encyclopedia of Meat Sciences (Second Edition), 2014

Appearance

The water-holding capacity of thawed meat is dependent on the rate at which the meat was frozen. The effect of freezing rate on water-holding capacity (measured as centrifuge drip) measured over a wide range of local freezing times is shown in Figure 1. The highest water-holding capacity is obtained with very short freezing times, whereas the lowest is obtained with freezing times of approximately 17–20   min, which coincides with a single ice crystal inside the muscle fibers. Beyond freezing times of 20   min, the water-holding capacity improves again until it plateaus at freezing times more than 30   min, beyond which no further improvement in water-holding capacity is achieved.

Figure 1. Changes in exudates from thawed meat in relation to the characteristic freezing time. The exudate was obtained by centrifugation.

 Reproduced from Mascheroni, R.H., Añón, M.C., Calvelo, A., 1980–81. Basis for a method of characterization for quick frozen beef. Meat Science 5, 457–472.

A slow freezing rate results in the formation of relatively large ice crystals, which create tissue damage. Temperature fluctuations during frozen storage often result in recrystallization, which influences subsequent thaw-drip losses. Thawing inevitably produces drip, particularly from cut muscle surfaces. However, some uptake of this drip occurs when thawed meat is held at refrigeration temperatures and most of the drip would ultimately be lost during cooking, primarily through evaporation, if it had not already been lost during thawing.

Freezing induces alterations in optical properties and hence a change in meat color when the frozen meat is thawed. Previously frozen thawed meat has been found to exhibit a slower rate of blooming than meat that had not been frozen, because the mitochondrial respiratory enzyme still remains active. Thus, previously frozen meat appears darker in color than nonfrozen meat. Frozen and thawed meat is also likely to be more susceptible to myoglobin oxidation, resulting in a faster conversion into metmyoglobin and hence shorter color display life compared with chilled meat. In addition, the longer the meat is stored frozen, the shorter its color stability is after thawing. Recent studies have found that aging meat before freezing can provide equivalent color and better lipid oxidation stability compared with aged nonfrozen meat. This indicates that aging meat for a certain limited period before freezing can allow oxygenation conditions similar to aged nonfrozen meat, improving meat color and color stability of the frozen/thawed meat.

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Recent advances in the application of high pressure technology to processed meat products

Y. Ikeuchi , in Processed Meats, 2011

24.2.1 WHC

WHC is defined as the ability of meat to retain its water when external force such as heating, pressing or grinding are applied. Much of the water in meat exists in myofibrils by capillary action, and about 5% of water binds to the hydrophilic groups of amino acids in muscle proteins. Thawing and heating cause the decrease of WHC accompanied by some increase in the exudative meat juice (meat pigments, amino acids, nucleotides, etc.) into the meat surface (drip loss) and the deterioration of meat quality such as texture, flavor or appearance. When pork meat is subjected to high pressure of 100   MPa, the drip loss increases because the myofibrils shorten. An increase in pressure from 200 to 300   MPa reduces the drip loss, thereby contributing to an increase in free water content in meat (Okamoto and Suzuki, 2002). This may be because the space that is able to maintain water increases via the partial destruction of structure of myofibrils, probably because of depolymerization of actin filaments. The application of high pressure to meat also leads to release of divalent cations that bind to myofibrillar proteins due to the electrostatic effect, preventing the formation of salt bridges among myofibrils. As a result, increased moisture retention in meat is achieved by muscle fiber expansion (swelling) caused by enhanced electrostatic repulsions. The drip loss increased again with a further rise in pressure to 400   MPa, indicating the severe denaturation of myofibrillar proteins.

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Packaging of retort-processed seafood, meat and poultry

J. Bindu , ... T.K.S. Gopal , in Advances in Meat, Poultry and Seafood Packaging, 2012

Water-holding capacity

The water-holding capacity of cans can be determined as per IS: 6093 (1970). Two holes of 3–4   mm diameter are drilled about 5   cm apart as close as possible to the countersink, from the inside surface outwards on a can end. This is attached by double seaming on the other end of the can body. The can is then weighed to the nearest 1   g and filled with water at 27°C, employing a narrow water jet through one of the holes. Surplus water on the outside of the can is removed using a blotting paper and the filled can is weighed to the nearest 1   g. The difference between the weights is noted and to this 0.45% of the value is added. This represents the capacity in millilitres.

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Developments in Our Understanding of Water-Holding Capacity

Brian Bowker , in Poultry Quality Evaluation, 2017

4.2.4 Other Methods

Aspects of WHC related to moisture-enhancement and freezing-thawing are also commonly reported in poultry meat. Salt-induced water uptake measurements are used to assess the ability of fresh poultry meat to hold added salt water, which is an indicator of the potential ability of the meat to pick up and retain marinade in moisture-enhanced products. For this assay, cold salt brine (usually 0.6   M NaCl) is mixed with chopped meat, and then held at refrigerated temperatures for a set time before centrifuging and pouring off unbound liquid (Wardlaw et al., 1973). The addition of salt causes the myofibrils within the muscle cells to swell laterally and take up water (Offer and Trinick, 1983). Oftentimes the swollen meat pellet that remains after the salt-induced water uptake assay is heated in a water bath and then reweighed as a measure of cooking loss. The amount of fluid (or purge) that is expressed from meat upon thawing from a frozen state (i.e., thaw loss) is also used as an indicator of WHC in poultry. Thaw loss measurements, however, are highly variable and can be influenced by freezing and thawing rates and prefreezing moisture losses from the meat. Most of the accepted methods for measuring WHC in fresh poultry are both time-consuming and destructive to the samples. With varying levels of success, advanced technologies such as visible and near infrared spectroscopy (Prieto et al., 2009; Samuel et al., 2011; Bowker et al., 2014a; Hawkins et al., 2014), Raman spectroscopy (Herrero, 2008; Phongpa-Ngan et al., 2014), dielectric spectroscopy (Zhuang et al., 2007; Samuel et al., 2012), hyperspectral imaging (Elmasry et al., 2012), and nuclear magnetic resonance (NMR) relaxometry (Bertram et al., 2002a; Bertram and Ersen, 2004; Huang et al., 2014) have been investigated as rapid, nondestructive methods for predicting WHC.

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Chemical deterioration and physical instability of dairy products

G. Mortensen , ... H.J. Andersen , in Chemical Deterioration and Physical Instability of Food and Beverages, 2010

24.8.1 Case study: syneresis in fermented dairy products

The water-holding capacity in acidified milk gels like yoghurt is mainly determined by the microstructure of the protein network. If the water binding is not sufficient, whey will be expelled on the surface of the product during storage. The mechanisms causing syneresis in fermented dairy products have been studied extensively, and a number of different experimental techniques have been applied in order to quantify the extent of syneresis. Tellier et al. (1993) studied milk coagulation and syneresis, and Harwalkar and Kalab (1983) were among the first to develop a method for quantifying the extent of syneresis. Additionally, a number of research groups have focused on the connections between rheological properties of yoghurt and syneresis (Guinee et al., 1995; Schkoda, 1999).

Figure 24.4 shows the viscosity profile measured from top to bottom of a freshly produced yoghurt (black line) and the viscosity profile of the same yoghurt after two weeks of storage at 5   °C (grey line) using Brookfield Viscosimetry. Figure 24.4 illustrates that even though the viscosities at different positions in the freshly produced product are similar, there is a large difference in viscosity between the top and the bottom of the two-week-old sample. It is also evident that the average viscosity of the stored sample is higher than that of the fresh sample. It is possible to quantify the extent of syneresis from such curves by relating the reduction in viscosity in the top of the container to the average viscosity of the fresh sample. For further details, please refer to Andersen et al. (2003). Quantification of syneresis in yoghurt by the Brookfield approach is, in our view, an improvement over the more conventional measurement methods, weighing the amount of whey that can be removed with a pipette, where large measurement errors often present a serious problem.

Fig. 24.4. Brookfield viscosity profiles of freshly produced yoghurt (black line) and yoghurt stored for 14   days (grey line).

Syneresis may also be studied using various microscopic techniques. In recent years, the most popular technique has been confocal laser scanning microscopy (CLSM), which, compared with electron microscopy, has the advantage of a much gentler sample preparation and thereby better reflects the properties of the protein network. The combination of CLSM and image analysis enables prediction of the extent of syneresis. Figure 24.5 illustrates this approach. Twenty yoghurt samples were produced according to a full factorial experimental design (varying both processing parameters and the composition of the samples). Confocal micrographs of the protein structure of the freshly produced samples were subjected to image analysis, and the resulting data were related to the extent of syneresis after two weeks by multivariate data analysis (PLS). This illustrates the link between the micro-structure of the freshly produced product and the extent of syneresis after storage. The combination of microstructural information, a precise measure for syneresis and multivariate data analysis constitute a powerful tool that enables identification of the optimal combination of product composition and processing conditions. Thereby, the water-holding capacity may be optimised in order to prevent syneresis in fermented dairy products.

Fig. 24.5. Predicted versus measured syneresis in yoghurts (based on Brookfield viscosity profiles). Please refer to Andersen et al. (2003) for an explanation of measurements units.

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CHEMICAL AND PHYSICAL CHARACTERISTICS OF MEAT | Water-Holding Capacity

M.S. Brewer , in Encyclopedia of Meat Sciences (Second Edition), 2014

Effect of pH

The pH of minimum WHC of the principle muscle proteins is 5.4–5.5, which coincides with their isoelectric points. The minimum WHC of meat occurs approximately at pH 5.0, which corresponds to the isoelectric point of actomyosin (Figure 6). Salt-soluble proteins are completely soluble above pH 5.9 but are 95% insoluble below pH 4.9 with peak solubility occurring between 5.7 and 6.0. When water is added to muscle tissue, between pH 5.1 and 4.4, swelling occurs across and along the muscle fiber axis. Increases in muscle fiber diameter were much more important to total muscle swelling than increases in sarcomere length. The pH is inversely correlated with fiber diameter (r=-0.76) but much less so with sarcomere length (r=-0.39). As pH approaches 4.0, muscles containing predominantly white fibers continue to swell, whereas those containing predominantly red fibers shrink. This behavior has been explained by differences in buffering capacity as predominantly red fiber muscles have lower buffering capacity than white fiber muscles under acidic conditions. Maximum precipitation of sarcoplasmic proteins occurs between pH 4.8 and 5.2 regardless of temperature, however, at 37   °C and above, high pH no longer protects these proteins. The pH-induced precipitation of sarcoplasmic protein onto myofibrillar proteins decreases WHC as well as other quality characteristics of meat.

Figure 6. Effect of pH on WHC.

Efforts to increase WHC in meat have centered on maintaining or increasing pH during the postmortem period. Injection of adrenaline before slaughter to reduce intracellular glycogen content at slaughter such that postmortem anaerobic glycolysis to lactic acid is limited does produce meat with high postmortem pH and high WHC. Addition of pH-increasing agents such as high molecular weight phosphates and sodium bicarbonate also increase postmortem pH and WHC to some degree.

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