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Food Hydrocolloids

Vol. 9no. 4pp.291-306, 1995

Ultrastructure of low-fat ground beef patties with added whey protein concentrate*

Salwa B.EI-Magoli, S.Larola\ and P.M.T.Hansen\,2

Department of Food Science and Technology, Faculty of Agriculture, Cairo University, Egypt and 1 Department of Food Science and Technology, The Ohio State University, Columbus, OH 43210, USA

2To whom correspondence should be addressed

Abstract

Microstructure of gels formed at trc from different mixtures of beef myofibril protein (BMP; 6.1% protein) and whey protein (WP) were studied by transmission electron microscopy (TEM). At a ratio of 30:10 (wlw) of whey protein concentrate (WPC; 79.5% protein) to BMP, WP formed

a network of aggregated clusters in which beef myofibril proteins were embedded. WP apparently acts as a filler and possibly as a cementing agent for the meat pieces. At a lower ratio of 10:30 (wi w), the WP aggregates occupied and increased the interstitial spaces between the myofibril protein and reinforced the network. The location of WP in the interstitial spaces might explain its water binding ability in beef patties formulated with WP and water. WP protected the beef myofibril protein structure during heating as less disintegration in the Z-line was observed in gels with WP

compared to the control. Low-fat (10% fat)

whey protein concentrate (WPC), cooked to three different internal temperatures (60, 70 and BO°C), were evaluated for their cooking characteristics and examined by TEM. For all levels of addition, WPC improved the cooking yield compared to a non-formulated control of 10% fat. Fat retention was also improved at the highest level of WPC addition. The increased cooking yield was shown to be caused principally by the better water retention. The textural parameters, hardness and chewiness, were not affected by WPC addition but increased with increasing cooking temperature. These temperature-induced changes were matched by marked changes to the ultrastructure of the

meat products.

ground beef patties with added 10% water and 1-4%

Introduction

The US Department of Health and Human Services (1) has issued specific nutritional guidelines to the food industry to help the public meet established dietary goals. Consumer trends toward reducing fat intake have increased the demand for leaner meat products and created opportunities for new meat product development through reformulation using effective fat substitutes (fat mimetics, fat replacers). However, maintenance of the customary meat flavor and texture (2) must remain an important consideration in any effort to reduce fat in meat products, because fat reduction will likely decrease palatability and satisfaction (3,4), especially when fat is reduced to 10% or lower (5).

* Presented as part of the conference entitled 'Food Hydrocolloids. Ohio 94', September 0-10.1994.

© Oxford University Press

Fat replacers may be protein-based, carbohydrate-based or fat-based constituents, where each category exhibits different functional properties that provide advantages as well as limitations in specific applications (6). Iota-carrageenan in combination with water was intro- duced (7) as a fat mimetic in the development of a particular formulation of low-fat beef patties which has been promoted as a commercial product (McLean De- Luxe TM) in the US since 1990. The selection was based on observations that the iota-carrageenan-water system pro- vided moisture retention and improved sensory properties of low fat « 10%) ground beef. Similarly, kappa-carra- geenan has been used to increase yield and improve texture properties of structured beef rolls with high added water content (8). With respect to protein-based fat replacement, the

292

S.B.EI-Magoli, S.Larola and P.M. T.Hansen

industry relies on the ability of various proteins, such as soy, corn and milk proteins to provide texture, mou th-feel and water-binding. Such functionality, is mainly related to the types of protein-protein interaction (9). Micro-particulated proteins have been found ideal for forming structural analogs of fat globules. Fat derives much of its functionality in foods as an emulsified, dispersed phase (10). Microparticulated fat substitutes achieve this same functionality through controlled particle size reduc- tion. The diversity of proteins with respect to their amino acid sequence, structure, and side chain modifications, present numerous possibilities for creating micro particles (11). For example, it has been reported that whey proteins (WP) can spontaneously form micro particles without any special treatment other than heating (12) and for this reason, WP has become a prototype for the micro- particulation process. Nevertheless, whey protein may be used in fat reduction schemes without microparticulation and, in this case, the functional properties of interest are related to the capacity of the protein to bind water and form heat-induced gels. This function has been described for' whey protein concen- trate (WPC) in processed meat formulations (13). When the functional properties of WPC, NFDM, and isolated soy protein were compared (14), only WPC was found to be useful in reformulation of meat emulsions. Studies on the relationship between the microstructure and gel strength, moisture and fat losses during cooking of different meat batters, have assisted the industry in improving process control and optimizing product formu- lation (9). Light microscopy techniques as well as trans- mission electron microscopy (TEM) and scanning electron microscopy (SEM) have proved useful in accurately localiz- ing the structural components within meat products (15). It has become apparent that gel formation is of particular importance to the textural quality of processed meats. Globular proteins form two types of gels, depending on how much charge is carried on the native protein. Fine- stranded gels are formed when repulsion is large while a network of colloidal particles is formed when the repulsion is minimum, such as when the isoelectric point is approached (16). However, the microstructure and physical properties of whey protein gels are sensitive to pH, concentration, the amount of salt addition and heating conditions (17). The relation between structure and func- tion is of importance in studying the basic gelation phenomena as well as for practical aspects of food system stability (9). The objective of this work has been to study the ultrastructural characteristics of composite whey protein concentrate and beef myofibril proteins in a model system and in real meat systems as a step towards understanding the factors responsible for the final characteristics of low-fat ground beef patties, formulated with WPC. Particular attention has been given to a study of the effect of internal cooking temperature on the ultrastructure of formulated low-fat ground beef with added WPC and water.

Materials and methods

Gel preparation

Beef myofibril protein (BMP) was extracted at 0-4°C from freshly ground, round beef (10% fat), using a pH 7.1 buffer of 0.1 mol/drrr' potassium chloride, 0.05 mol/dm' potassium phosphate and 0.005 mol/dm' sodium-EDTA buffer (18). The ground beef (100 g) was homogenized in a Waring blender with 500 ml of the buffer for one min. Connective tissue was removed by filtration of the homogenate through

cheesecloth. The filtrate was centrifuged at 600 g for 15 min at 0-4°C. The supernatant was discarded and the pellets resuspended in buffer and again centrifuged. This treat- ment was continued until the discarded supernatant was clear. The resulting BMP pellets were collected and used as such. Analysis of a separate preparation showed 8.7% total solids and 6.1 % protein. Whey protein concentrate (WPC) was obtained from New Zealand Milk Products (N.America), Inc. (San Francisco, CA) (Alacen 878: 79.5% protein, 4.5% ash, 4.2% moisture, 4.6% fat and 6% lactose). Solutions were prepared by adding 10, 15,20,30 and 40%g WPC and 0.5% encapsulated salt (Morton Salt Inc., Chicago, IL) to -50 g of water and adjusting the final weight to 100 g with water. These WPC concentrations all contained 0.5% salt and corresponded to WP concentrations of approximately 8, 12, 16, 24 and 32%. The ash content varied from 0.45 to 1.84%. Combined solutions of BMP and WPC were prepared as follows. (a) 10:30 ratio: 1 g BMP + 3 g WPC +

0.05 g salt + 5.95 g water; (b) 20:20 ratio: 2 g BMP + 2 g

WPC + 0.05 g salt + 5.95 g water; (c) 30:10 ratio: 3 g BMP + 1 g WPC + 0.05 g salt + 5.95 g water. The estimated protein contents of the combined solutions were 24, 17 and 10% for a, b, and c respectively.

For gel preparation, 5 ml from each sample were placed

in glass tubes, stoppered at one end, and heated at 71°C for

10.5 min in a water bath. This time and temperature were

chosen to match the actual cooking time and temperature of beef patties in the present study and was sufficient to

induce gelation in all of the samples. After heating, the tubes were cooled to room temperature, and the gels were removed from the tubes, cut into 1 em cubes and placed immediately in the fixative (4% glutaraldehyde in 0.1 moll drn' phosphate buffer pH 6.8), for TEM.

Formulation of low-fat ground beef patties

The patties were formulated using coarsely ground beef (10% fat), 10% water, 0.5% encapsulated salt and four different concentrations of WPC (1, 2, 3 and 4%). WPC was first hydrated with the required amount of water to be added to the meat, by mixing for 15 min using an electrical stir plate. The resulting thick liquid slurry was kept overnight at 4°C, before it was added with the salt to the meat and mixed thoroughly. The mixture was ground in succession with 9.5 and 4.8 mm plates using a Hobart

 

Meat-whey protein ultrastructure

293

mixer. For

comparison , a control was included of lean beef

Transmission electron microscopy

(10% fat) , with only 0.5 % salt and no water added.

Quarter pound , (114

g) patties were shaped using a

Initially , l-cm cubes from gels and meat patties

were fixed

household hamburger mold (Burger press, US Pat 0191367) , and quick frozen in liquid nitrogen. Each patty was wrapped separately using pol yethylene cling film, and

every four patties were then sealed in 'Zip-Lock' pouches

cooked to three internal temperatures (60, 71 and 80°C) on

for -1 h in 4% glutaraldehyde in 0.1 mol/drrr' phosphate

buffer (pH 6.8). One millimeter cubes were then cut from each sample and placed in fresh fixative overnight at 4°C. Samples were rinsed three times in 0.1 mol/dm" phosphate

and stored at -18°C until further analysis.

buffer, for 45 min , post fixed at room

temperature in 1%

The patties were thawed at 4°C, overnight , and were

osmium tetroxide in buffer for 90 min; then rinsed three more times in buffer over a 90 min period and dehydrated

an

electric household grill heated to 150°C and using

in graded ethanol series (50, 70,80,95, and 100%), where

variations upon a standard protocol (3 min, 2 min and 15 s

each step involved two changes over 15 min. The samples

on

each side). The actual cooking time varied between lO-

were placed in propylene oxide over a 15 min period and

II

minutes, depending upon the desired end-point tem-

then embedded in Spurr-resin and polymerized in a vacuum

perature. Temperatures were monitored using a hypo- dermic probe-type thermocouple (Model HVP-2-21-1-V2- TG-48-0ST-M Omega, Stanford, CT) connected to a data

oven overnight at 60°C (22). Sections (70-80 nm) , were stained with uranyl acetate followed by Reynold's lead citrate, and examined by a Phillips C-12 Electron Micro-

logger recorder (21X Micrologger, Campbell Scientific

scope at 60 KV.

Inc

., Logan , UT) and linked to a computer (Laser

3865X/25).

Moi sture was determined by weight loss after 12-18 h drying in a conventional oven at 105°C (20). The fat content was determined using the Babcock method (21) , after slight

modification for meat use . Four to five grams of the sample were placed in cream bottles with 9 ml water. A quantity of 17.5 ml sulfuric acid was then added at room temperature

to dissol ve the meat.

followed the standard Babcock method. Texture profile

analysis (TPA) was conducted after cooking and cooling to

room

three different locations) each to 75% of their height , for two cycle s using a Universal T A-XTI Texture Analyzer

(Texture Technologies Corp., Scarsdale, NY) equipped with a 1/2 inch flat surface plunger. The machine was programmed for a 50 kg load cell and cross head speed of 200 mm/min. Hardness and chewiness were obtained using the available computer software . Uncorrected cooking yield was determined relative to the me at content :

temperature . Two whole patties were compressed (at

The rem ainder of the procedure

Cook ing yield (%) = Cooked weight Weight of raw meat

Cooking yield , corrected for the addition of WPC , was calculated as above by subtracting from the cooked weight ,

the weight of the added WPC. Shrinkage and fat retention

values were calculated according to (2,19) as follows :

Fat retention (%) =

Cooked weight x percent fat in cooked patties x 100

Raw weight x percent fat in raw patties

Shrinkage (%) = (Raw width - (Raw length -

cooked width) + cooked length)

Raw width + Raw length

x

100

Results and discussion

Whey protein concentrate gel

Transmision electron micro scopy of WPC gels (Figures 1 and 2) showed a distribution of aggregated protein clusters separated by irregularly shaped void spaces, which have also been previously recognized (23-25). The void space s in the network represent the compartments of water which was removed during specimen preparation with the graded alcohol series (26). The dimensions and extent of void spaces are an indication of the water retained by the system. At higher magnification (Figure IB), the clusters of the aggregated proteins were seen to be connected by fine threads, forming a distinct network. The presence of an extended protein network explains the role of WP when used as a water binder in the meat system. According to Langton and Hermansson (16), TEM of a network of WPC gel (12%) at pH 7.5 revealed loosely packed aggregates, interconnected by thin threads. In the present study, the void spaces and crevices diminished and the structure became more compact and dense as the concentration of WPC increased (Figure 2A and B) . The relatively compact structure of heat induced WP gels has been explained (16) to be related to the pre sence of immunoglobulins (up to 11% in WPC) that have an isoelectric point at a relatively high pH (6-8) and might precipitate and , thus , contribute to a more dense structure of WP gels. The whe y protein started to form a gel at a concentration of 15% WPC , corresponding to 12% WP. As the WPC concentration increased , the micrographs (Figure 10 and 2A) showed embedded globular structures, resembling holes or entrapped gas bubbles and varying in diameter between 0.1 and 0.5 urn. At high magnification (Figure 2C; 112500x), a substructure was revealed, which may be surface active protein surrounding gas bubbles. These

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Meat-whey protein ultrastructure

297

particles were not detected in gels at 15% level (Figure 1A and B). Gels of WP, formed at 30-40% WPC (24-32% protein) were white in color with a highly rubbery texture. Such texture (27) may arise from the intermolecular S-S bond resulting from an interchange reactions of SH/S-S reported to occur at pH 7.5 over a broad concentration range. TEM micrographs of these gels (Figure 2B) showed aggregated globular particles with many rough edges. This structure was not apparent in gels containing 15% Wl'C, These gels were less rubbery, almost transparent and showed more of

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lB).

The results confirm that WP is capable of forming more than one type of gel, depending on its concentration and the condition of the system. Such observations have been reported (25) for heat induced gels formed at 8-15% in the pH range of 7-8. It may be noted that the temperature of heating and pH used in the current study for gel prep- aration were chosen to correspond to the cooking con- ditions for the meat system. Addition of salt (0.5%), did not affect the gel structure of WP in this study. Sodium ions (0.25 mol/drrr') are reported

to improve the water holding capacity of WP gels (9). This concentration is equivalent to 1.5% NaCl and thus, considerably higher than the salt level used in this study. It

is possible that some of the variations in gel structure were

due to differences in ash levels of the WPC dispersions.

BMP gels

Immediately upon extraction BMP formed a delicate soft gel. When heated at 71°C for 10.5 min in the buffer (pH 7.1) the protein sample coagulated and formed a more fibrous, thread-like structure. TEM micrographs of BMP before and after heating are shown in Figure 3 (A, B, C and

D).

Before heating BMP showed a typical structure of myofibril proteins with sarcomere length of -2 urn. The Z- disks, A-Bands, I-bands and M-lines were identifiable at both high and low magnifications (Figure 3A and B). Heating of the BMP resulted in fragmentation of the Z- disks with the loss of structure due to the coagulation of the filaments. The structure of the myofibrils became more amorphous and a pronounced shrinkage occurred (Figure 3C and D). The Z-disks became diffused, thickened and disrupted. These changes are typical of those previously reported (28-30) for the effects of heating on myofibril proteins.

Combined gels (WP/BMP)

The distinct morphological differences between gels from the two proteins may be used as a basis for further comparison of the combined systems. The granular aggre- gates of the WP are seen to persist within the complex gels. Thus, the ultrastructure of combined gels, containing WPC/

BMP in the ratios 30:10, 20:20 and 10:30, with estimated total protein content of 24, 17 and 10% respectively, showed that the relative amounts of the proteins had a determining effect on their distribution in the system (Figure 4). At a ratio of 30:10 WPCIBMP, the WP appeared as a continuous network embedding the BMP and water (Figure 4A and B). It is possible that at this concentration WP may act as a filler or as a cementing agent. At the 20:20 ratio (Figure 4C and D), both WP and BMP were distributed on an equal basis, with the WP occupying the intracellular and some of the intercellular spaces. The effect of heating (71°C for 10.5 min) on the shrinkage and disintegration of BMP was less pronounced in the presence of WPC, compared with the control (Figure 3C and D) suggesting a protective action of WPC on the BMP, and possibly explaining its role in decreasing shrinkage when used in real meat systems. Both the BMP fibrous network and small WP globular aggregates were visible at the ratio of 10:30 (WPC/BMP), with the WP clearly located in the interstitial spaces (Figure 4E and F), holding the filaments together and reinforcing the original network of the myofibril proteins. At high magnification (Figure 4F), WP aggregates were evenly embedded within the BMP gel matrix. The type of gel formed seemed similar to the 'coupled network' gel form (31,32) possibly formed from a two-phase separated net- work. Thus, WP might gel within the interstitial spaces of the already formed BMP gel network. The creation of this type of gel could have an impact on the tenderness and juiciness of a meat product containing Wf'C. In a low-fat meat system, the meat tends to be tough and dry. Toughness is mainly due to drying and coagulation of myofibrillar proteins, originating from the loss of water of hydration surrounding thick and thin filaments. If this water of hydration could be retained by the WP gelling within the interstitial spaces between the myofilaments, the meat tenderness is likely to improve.

Low-fat ground beef patties (TEM)

Specimens for TEM of the control low-fat ground beef patties, cooked at three internal temperatures were collected from the interior of the sample where end-point temperatures were monitored. The micrographs revealed pronounced changes in the myofibril patterns starting at 71°C and continuing at 80°C. The uncooked patties showed well defined, closely packed and well-preserved structures of myofibril with a sarcomere length of -2 urn. The 1- band, A-band, H-zone and M-lines were clearly identifi- able. Shrinkage and coagulation of the thick-band (the A- band) began at 60°C and increased significantly with the increase in cooking temperature (Figure 5A, B, C and D). At 80°C wider endomysial spaces between the myofibrils were evident indicating more shrinkage. Maximum shrink- age of the endomysial connective tissue at 70°C has been previously reported (28).

298

S.B.EI-Magoli, S.Larola and P.M. T.Hansen

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s. B. EI-Magoli, S. Larola and P. M. T. Hansen

Marked disintegration in the myofibril occurred at 71DC; however, banding patterns remained visible, with some of the Z-lines and H-zones still intact. At 80 DC the filamentous structural integrity was almost gone and the myofibril showed granulation. The granular material formed at a higher cooking temperature (90 DC) may be related to the partial precipitation of sarcoplasmic proteins from fluids that collect beneath the sarcolemma during fiber shrinkage

(29).

The raw meat samples containing 2 and 4% WPC (Figures 6 and 7) showed the same well-preserved pattern of the myofibril structure as in the control sample (Figure 5A). The structural unit of the myofibril, the sarcomere, was neatly organized, showing the refined distribution of the A-band, l-band, Z-lines and M-lines. The TEM of the low-fat ground beef patties with 2 and 4% WPC, showed that the cooking temperature had far more impact on meat structure than the presence of WPC. However, the structure of myofibrillar proteins seemed to be less affected by heat in the presence of WPC at the 2 and 4% levels used than without WPC (Figures 5,6 and 7). The myofilaments had shrunk less and have retained their Z- lines, particularly at the 4% level. This observation suggests that WP might form a weak gel, even when the samples are heated to an internal temperature of 60 D C. To reach this

point, the outer areas of the patties will obviously attain higher temperatures with more complete gelation of WP and stronger retention of the water around the myofila- ments, thereby decreasing the shrinkage. Overall, increasing cooking temperatures resulted in a progression from a compact structure of the myofibrils at

(Figure 6A and B) to a separation of the strands at

71DC and finally more granulation at 80 D C (Figure 6C and 0). WP was not detected between the myofilament at the lower cooking temperatures at the 2% WPC level; how- ever, some of the WP aggregates were present in the interstitial spaces between the myofibrils at the highest cooking temperatures and at the 4% WPC level (Figure 7C and 0). These findings support the perceived role of WP as a water binder in the meat system, and may explain the higher cooking yield and the lower shrinkage of the low-fat ground beef patties with 4% WPC (Table 1). Micrographs of samples containing 2% WPC (Figure 60) and cooked at 80 DC, showed a network structure of myofibrils that seemed connected by delicate threads resembling the WP strands in the gel system (Figure 2B) and differed in structure from the control without WP. However, more amorphous and granulated surfaces due to protein coagulation were apparent at this cooking tempera- ture than at 60 or 71DC and were also accompanied by a

60 DC

Table 1

Cooking characteristics of low-fat ground beef patties (10% fat) with added whey protein concentrate, salt and water

WPC

Internal

Cooking yield

Fat

Shrinkage

Texture profile analysis

(%)

temperature

retention

(%)

eC)

(g/100 g meat)

Corrected for (g/lOO g meat)

WPC

(%)

Hardness

Chewiness

Control

60

77.6

77.6

66.1

10.5

2.79

1.22

(0%)

71

70.8

70.8

68.4

12.2

3.99

1.71

80

68.2

68.2

61.9

10.4

4.47

1.78

60

83.6

8.25

50.1

11.7

3.06

1.78

1.00

71

76.4

75.3

53.8

13.0

3.13

1.03

80

74.6

73.5

55.9

13.6

4.53

1.75

60

86.3

84.0

59.7

5.9

2.28

0.97

2.00

71

84.9

82.6

57.5

10.0

4.20

1.82

80

78.9

76.6

68.7

10.8

4.33

1.82

60

91.7

88.2

72.7

8.2

2.93

0.97

3.00

71

86.2

82.8

80.1

11.1

3.71

1.64

80

78.9

79.3

73.9

9.1

4.66

2.08

60

95.9

91.2

73.7

6.1

2.46

1.09

4.00

71

85.2

80.5

69.2

8.6

3.87

1.48

80

85.9

81.2

69.9

7.4

3.55

1.65

Standard error

±1.76

±1.76

±4.26

±1.04

±0.43

±0.33

All measurements are means of duplicate analyses. Standard error values were determined from the mean square values from analysis of variance.

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304

S. B.EI- Magali. S. Laraia and P. M. T. Hansen

complete loss of the M-line . At 80 aC, WP will form a more ru bbery and elastic ge l, which might the n support the concept of it working as an agent for cementing the meat pieces. Water absorption and gelation phenomena are important for the stability of ground or minced meat products (33) . However, the TEM micrographs of the meat system (Figure 8A and B) showed that WP may playa role as an emulsifying agent when added to a meat system. The fat globules were covered by the WP, with some of the WP aggregates extending into the system, indicating an associ- ation of protein aggregates with the fat globules. It has been observed that glo bules covered with adsorbed protein molecules may be immobilized by direct reticulation between membrane-forming protein mo lecules and bu lk phase protein (34). Fat membranes are likely to be ruptured during the preparation of beef patties and upon cooking, the fat will tend to form pools rather than retaining separate globular structures. The micrographs in Figure 8 are selected fields from low-fat ground beef patties formulated with 4% WPC and cooked at 71°C showing areas where fat is prominent. Figure 8C shows a fat pool surrounded by protein, assumed to be WP . Such fat pools were observed during examination under the microscope in all cooked samples, with and without WPC. However, separate fat globules were only detected in samples with 4% Wl'C .

Cooking characteristics of low-fat gro un d beef patt ies

The control in these studies was a 10% beef patty with no

water and only salt

formulated with 10% added water, salt and different WPC

added . The treatment samples were

levels. The results for cooking yields(Tables 1 and 2) show that WPC addition is an effective means for retaining the added water, because the yields gradually increased over the control for each leve l of WPC addition . As might be expected, yield decreased significantly as the inte rna l cooking temperature was raised. However , increases in yield due to WPC addition and losses due to heating were independent of each other as shown by the lack of significance of the interaction term . Some improvements in cooking yield ma y be expected from the additional solids provided by WPC; however, corrected yields still showed substantial gains in cooked weight over the controls which must be ascribed to better water or fat retention, or both . Cooking yield has been reported to improve by reducing the fat content of meat patties to 20% (35,36). In other studies (4,5, 37) cooking yields did not diffe r much when the fat levels were below 20% . Fat retention was significantly improved (Tables 1 and 2) at the 3 and 4% WPC addition but not at the lower levels of addition. In fact, at the 1% WPC addition , fat retention was adversely affected compared with the non-formulated control. We speculate that the addition of WP to the formulated beef patties might result in em ulsification of some of the fat which is then better retained in the WP gel. This explanation would be consistent with the microstruc- ture observed in Figure 8. Another possible reason for the observed differences in fat retention for different levels of WPC may re late to the failure of WP to gel firmly at the lower levels of addition . The greater loss in cooking yield, at these concentrations, implies some loss of the added liquid, which might carry associated fat, and thus explain, why more fat is lost from the product formulated with 1% WPC than from the non-formulated control.

Table 2

Analysis of variance of cooking characteristics. Single degree of freedo m comparisons between treatments and temperatures

(40)

Comparisons

Cooking yield

Fat

Shrinkage

Texture profile analysis

(%)

retention

(%)

 

(g/IOO g meat)

Corrected for WPC (g/IOO g meat)

(%)

Hardness

Chewiness

 

Significance levels (P <)

 

Between treatments (WPC)

(1%)

(1%)

(1%)

(1%)

(NS)

(NS)

4

versus 3, 2, 1% WPC and control

1%

1%

5%

1%

NS

NS

3

versus 2, 1% WPC and control

1%

1%

1%

NS

NS

NS

2

versus

1% WPC and control

1%

1%

NS

1%

NS

NS

1% WPC versus control

1%

1%

1%

NS

NS

NS

Between internal temperatures (T)

(1%)

(1%)

(NS)

(5%)

(1%)

(NS)

60

versus

71 and 80 aC

1%

1%

NS

1%

1%

5%

71

versus

80 aC

5%

5%

NS

NS

NS

NS

Interaction (WPC x T)

NS

NS

NS

NS

Significance levels in paren theses are from two-way ANOVA ; others are from single degree of freedom comparisons of the same treatments. NS, not significant (P > 5%).

Meat-whey protein ultrastructure

305

Cooking temperature did not influence fat retention within the temperature range studied. Therefore , the overall losses in cooking yield observed for increasing temperatures are principall y due to loss of water. In other reports, cooking to well-done versus medium doneness (77 and 71"C) have been found to increase cooking losses (38). There is evidence in the present study that fat retention is improved when fat has been partially emulsified by WP. Higher fat retention in low-fat meat systems has been reported (39). These authors concluded that the denser protein matrix of low-fat ground beef prevents fat migration , reducing the possibility of encounter and expansion among fat pools. Significant changes in shrinkage values due to WPC addition and cooking temperature were observed. Gener- ally, WPC addition> 1% reduced the degree of shrinkage , while increasing the internal end-point temperature > 60°C increased shrinkage . The micrographs in Figures 5, 6 and 7

show features which correlate to

No significant differences due to added WPC occurred for the textural profile traits , hardness, and chewiness, indicating that such addition doe s not markedl y affect these textural characteristics of meat. However, hardness in- creased significantly as the final internal temperature was raised above 60°C. This result is understandable, since at 60°C (rare to medium) less coagulation in both myofibril proteins and endomysial connective tissue will occur. This

effect is evident in the ultrastructure micrographs (Figures 5, 6, and 7), where changes to the myofibril become more

pronounced at 71 and 80°C

increase in chewiness (P > 0.05) was observed as the cooking temperature was raised above 60°C which would be

consistent with the increase in hardness .

these observations .

(medium to well-done) . Some

Conclusion

TEM was used to show the role of WPC as a functional agent for formulating a low-fat ground beef system with improved cooking yield and fat retention . Such improve- ments may generally be related to improvements in perceived moistness and juiciness. The observations are consistent with whey protein acting as a water binder, cementing agent and an emulsifying agent. Results suggested that the addition of a solution fo WPC can enhance the cooking characteristics of low-fat ground beef patties , depending on the concentration used. An addition of 10 parts of water, 4 parts of WPC and 0.5 parts of encapsulated salt to low-fat ground beef, produced im- proved cooking yield, better fat retention and less shrink- age compared to other concentrations tested.

Acknowledgements

Appreciation is expressed to Kathleen S.Wolken of the OSU Microscopy and Imaging Facility for assistance with the electron microscopy and to Dr H.W.Ockerman for helpful advice. S.B.E.-M. acknowledges with thanks a

grant awarded to her by the Fulbright Commission . Journal Article No. 142-94. Salaries and research support provided by state and federal funds appropriated to the Ohio Agricultural Research and Development Center and The Ohio State University.

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Received on October 17, 1994, accepted on May 5, 1995