UTILIZATION OF MINCED SUCKER FLESH

UTILIZATION OF MINCED SUCKER FLESH

A. A. DAWOOD’, J. F. PRICE and A. E. REYNOLDS, JR.’

Dept. of Food Science and Human Nutrition Michigan State University

East Lansing, MI 48824

Accepted for Publication July 12, 1982 Received for Publication July 16,1982

ABSTRACT

Freshwater suckers (Catostamidae family) were obtained from Lake Huron to study the possibility of developing new products utilizing its f lesh and the influences of additives on the functionality of sucker muscle proteins. Results showed that sodium chloride increased protein solubility, but also decreased swelling, gel forming and pH. In comparison, sodium tripolyphosphate increased protein solubility, pH, swelling and gel formation. Fish sausages and canned products showed low binding characteristics. However, adding corn meal and soy protein in combination with sodium chloride and sodium tripolyphosphate improved their water holding capacity, texture and cook yield. I t was concluded that sodium tripolyphosphate, corn meal and f a t should be used in manufacturing minced sucker products.

INTRODUCTION

Baker (1978) stated that about 80-90% of the fish resources from the great Lakes are wasted. So called “trash” fish considered pollutants, are routinely thrown back by fishermen. Those species can be used as raw materials for new fish products.

The role of muscle proteins in functional performance can be speci- fied more precisely by dividing these into three major classes on the basis of their solubility to myofibrillar, sarcoplasmic and stroma proteins (Go11 et al. 1974). Myofibrillar proteins are essential for water binding, gel formation and emulsification characteristics in comminuted sausages (Briskey and Fukazawa, 1971; Go11 et al. 1974). Water

‘Abdelbary A. Dawood, Food Science Department, College of Agriculture, El-Minya University, El

‘A. E. Reynolds, Jr., Extension Food Science Dept., Cooperative Extension Service, U . of Georgia, Minya, Egypt

Athens, GA 30602

49

50 A. A. DAWOOD ET AL.

soluble proteins have relatively minor effect on water binding, gel forming ability and emulsifying capacity compared to myofibrillar proteins (Hamm, 1960; Schut and Brouwer, 1974). Stroma proteins have poor water and fat binding ability. However, they are useful in reduction of the cost of finished products (Kramlich, 1971; Saffle, 1968). The role of fish proteins has been described as being similar to that of red meat proteins (Learson et af. 1971).

Protein extractability and solubility are useful parameters for determining the quantity of proteins available for binding and emulsification (Saffle, 1968). Ionic strength, pH and freezing influence the extractability of muscle proteins. Solubility of fish muscle protein is reported to be minimal in the pH range 5.5-6.0 but increases on both the acidic and basic sides of this range. Frozen meat has been shown to be less stable than fresh meat i n sausage-type emulsions (Morrison et al. 1971). Poulter and Lawrie (1977) found that protein solubility decreased more rapidly during storage at -8" C than during storage a t -30" C. About 7040% of myosin from cod flesh became nonextractable a t a rate similar to the extractability of myofibrillar protein during storage of this species a t -14 O C (Connell, 1962). Observations in this laboratory indicate tha t minced muscle tissue from the sucker species was extremely susceptible to freeze damage which was associated with a soft texture in cooked product.

Rigor mortis involves a type of aggregation of muscle protein in situ, characterized by the disorganization of tissue and loss of ATP from myofibrils. These changes may prevent the distribution of proteins into solution when salt solutions are used (Dixon and Webb, 1961). According to Asghar and Yeates (1974), the effect of rigor mortis on protein solubility apparently disappeared with the addition of phosphate and appropriate conditions of ionic strength, pH and temperature during muscle protein extraction.

Swelling and gel-forming measurements were negatively correlated with water loss (Hermansson and Akesson, 1975a). According to Her- mansson (1972), swelling i s strongly dependent on pH and ionic strength. Nakayama and Sato (1971b) found that myosin fractions have major effects on gel formation. Tong et al. (1975) reported that alkaline extractions (pH 11) of squid protein concentrations were more effective than protein extracted by 4% salt in forming gels.

Sherman (1961) reported that pH, time, temperature, additive concentration and the ability of alkaline phosphates to split the bond between myosin and actin are factors influencing water binding capacity. Hamm (1975) indicated that water holding capacity (WHC) and swelling (sw), myosin and actin interaction changes, and solubili- zation of myofibrillar proteins are the main factors affecting rheo-

UTILIZATION O F MINCED SUCKER FLESH 51

logical properties of minced meat. Lee and Toledo (1976) indicated that amount of time spent in com-

minution, addition of NaCl or NaCl and tripolyphosphates, effect of mechanical deboning, cooking temperature and type of heating medium used are the factors affecting texture characteristics of fish sausages.

Soy protein isolate is a widely used additive in sausage batters and it has properties similar to those of meat proteins (Brown, 1972). The addition of SPI to a variety of foods supplies desirable functional properties, such as emulsifiability, ability to absorb fat, moisture ret- ention and thickening and foaming ability (Wolf, 1970).

The aim of this study was to investigate the effect of added salt, sodium tripolyphosphate and soy protein isolate at various levels on the functional properties of frozen minced sucker and to study the possibility of developing new products utlizing its flesh.

MATERIALS AND METHODS

Fish Freshwater sucker from Lake Huron (Saginaw Bay) were obtained

for study in July of 1978. The fish were a mix of redhorse (Moxostornu anisururn) and white (Cutostornus cornrnersoni) suckers. They were transported in ice to the Meat Laboratory a t Michigan State Univer- sity where they were processed. Fish were headed, gutted, rinsed under running cold water, split lengthwise, and passed through a Bibun mechanical deboning machine (Type SDX 13, Bibun Co., Fukeyama Hiroshima, Japan) equipped with a 5 mm hole size drum.

The sucker flesh was then vacuum packaged in 2.3 and 9.k kg lots in Cryovac (polyvinylidene chloride) bags which were blast frozen and stored at-29" C. The frozen fish was thawed in a 3" C cooler as needed.

Processing Procedures Smoked fish sausages. All ingredients presented in Table 1 except

hydrogenated vegetable oil were mixed a t medium speed for 8 mins. in a Kitchen Aid Food preparer (Model A-200, Hobart Mfg. Co., Troy, OH) with a paddle attachment. Hydroganted vegetable oil (Mazola, corn oil) was added and the mixture blended a t low speed for 7 minutes more. The fish pastes was stuffed into collagen casings (Brechteen, Box 71 1, Mt. Clemens, MI) 35mm in diameter which were then linked.

Sausages were cooked in a n Elek-Trol Laboratory Smokehouse

52 A. A. DAWOOD E T AL.

Table 1. Design and formulation of smoked fish sausage treatments

_____

Treatment Treatment and Formulations'

A

B C D

E

97% Mechanically deboned frozen fish (MDFF), 2% sodium chloride (NaCI), No hydrogenated vegetable oil (HVO). 88% MDFF, 3% NaCl and 8% HVO 84% MDFF, 3% NaCI, 4% soy protein isolate (SPI) and 8% HVO 84% MDFF, 3% NaCl, 4% white corn meal and 8% HVO 60% MDFF, 3% NaCl, 4% SPI, 4% white corn meal and 8% HVO

I In all formulations (A, B, C, D, E) the following additives and spices are present: 0.45% sodium tripolyphosphate. 0.1% monosodium glutamate,0.05% sodium aacorbate,0.5%condensed smoke,and the spices.

(Drying Systems Inc., Chicago, IL) until the internal temperature reached 82" C, using a 6-112 hr. stepwise cooking cycle(40" C-88" C and 22-40% RH).

Canned minced fish. The following ingredients were mixed in the same manner described earlier for sausages (Table 2). The fish paste was then placed into size 21 1 * 304, C-enamel coated cans (American

Table 2. Design and formulation of canned minced fish treatments

Treatment Treatment and Formulations'

A

B

C D

86.5% mechanically deboned frozen fish (MDFF) 82.5% MDFF, 4% soy protein isolate (SPI) 82.5% MDFF, 4% white corn meal

78.5% MDFF, 4% SPI, 4% white corn meal

IIn all formulationn (A. B. C, D) the following additives and spices are present: 4% beef tripe, 8% hydrogenated vegetable oil, 1% sodium chloride, 0.45% sodium tripolyphosphate.0.3OW white pepper powder, 0.15% onion powder, 0.15% garlic powder, 0.30% paprika pepper powder and 0.05% ground ginger

Can Company, Greenwich, CT). The filled cans were baked in a dry air oven for 30 mins. a t 167°F (75°C) then cans were closed using a n automatic closing machine (Canning Devices Inc., Manitowoc, WI). The sealed cans were processed in a still retort (Food Machinery Corp., Sprague-Sells Division, Hoopeston, IL) at 250" F (121" C) for 75 minutes. The processed cans were immediately cooled in water until the

UTILIZATION OF MINCED SUCKER FLESH 53

temperature a t the center of the cans was reduced to approximately 100" F.

Chemical and Physical Measurements

Total extractable protein, salt souluble proteins, and water soluble proteins as well as non-protein nitrogen were extracted by a modification of the method described by Trautman (1964). All total soluble protein fractions were compared using a modification of the sodium dodecylsulphate (SDS) polyacrylamide gel electrophoresis technique described by Weber and Osborne (1969). Gel formation was determined using the least concentration endpoint (LCE) method reported by Trautman (1966b). Percent swelling was determined according to the method reported by Wierbicki et al. (1963).

The pH of total extracted proteins was measured with a pH meter (Beckman, Model 35600 Digital pH meter), using a glass electrode.

The difference in weight of the stuffed product before and after smokehouse cooking was calculated as percent cooking loss.

Baking loss was calculated by the weight difference of filled cans before and after baking. Results are presented as percent baking loss.

Water holding capacity of the cooked fish flesh was determined using the centrifuge technique of Bremner (1974). The water holding capacity calculated according to the following formula.

Water holding capacity = 100 X weight of meat residue

10 g of sample

The texture of both products, measured as shear force, was determined on the Instron Universal Testing Machine(Mode1 TTB, Instron Corp., Canton, MA). The edible casing and firm surface layer were removed in order that only the resistance to shear of the internal mass was measured. The products were sheared using a compression load cell of the 1 to 50 kg range. A shear cell was attached to the upper moving fixture. Drive speed and chart speed adjusted a t 20 cm/minute and 5 cmlminute, respectively. The resistance force met by the cell was expressed as kg-f per cm length of fish product of a standard diameter (see below).

RESULTS AND DISCUSSION

Effects of Additives on Solubility

The value of measurements of protein solubility in various salt solutions lies in the functional role of proteins in processing high


quality products. The data (Table 3) indicated tha t total extracted protein increased significantly when NaCl was added. The largest average value was noted when 3.0% NaCl was used in the extraction, and the minimum protein solubility of minced frozen fish was noted a t 0% NaC1. Salt soluble protein (SSP) extracted from frozen minced fish also increased as NaCl concentration increased, with the largest

Table 3. Effects of adding sodium chloride and sodium tripolyphosphate on the amount of total extracted protein from frozen mechanically deboned fish (% total extracted protein = mg extracted protein/100 mg toal protein)

% Sodium Chloride

Sodium 0 .o 3.0 3.6 Meanb tripol yphosphate

w W Total Extracted Protein ~ ~~ ~

0.000 13.67" 67.40 62.17 47.63 0.225 15.20 54.70 54.8 1 41.57 0.450 47.84 58.80 61.11 55.91 Mean' 25.48 60.30 59.36

aStandard error for each cell mean (N = 12) is 0.07 'Standard error for each row or column mean (N = 36) is 0.04

Table 4. Effects of adding sodium chloride and sodium tripolyphosphate on the amount of salt soluble protein extracted from frozen mechanically deboned fish (% salt soluble protein - mg salt soluble protein/100 mg total extracted protein)

96 Sodium Chloride

Sodium 0.0 3 .O 3.6 Meanb tripol yphosphate

% W Salt Soluble Protein

0.000 0.00 47.65 51.47 33.04 0.225 8.17" 57.02 54.84 40 .O 1 0.450 52.17 47.75 55.59 51.83 Meanb 20.1 1 50.80 53.96

aStandard error for each cell mean (N = 6) is 0.08 'Standard error for each row or column mean (N = 13) is 0.05

increase obtained between 0.0% and 3.0% NaCl (Table4). Adding NaCl decreased the percent of extracted water soluble protein (WSP) in the total extracted protein (Figure 1). This effect was expected, since SSP content increased as NaCl concentration increased (Table 4). The


4 0 1

0- 0 1 2 3 4

Percent Sod ium Chloride FIG. 1. EFFECT OF SODIUM CHLORIDE IN VARYING CONCENTRATIONS ON THE RATIO BETWEEN THE AMOUNTS OF SALT SOLUBLE PROTEIN AND WATER SOLUBLE PROTEIN

EXTRACTED FROM FROZEN MINCED FISH 0-0 Total Extracted protein, ~ - salt soluble protein and X - - - X water soluble protein

average percentages of nonprotein nitrogen (NPN) decreased slightly as NaCl concentration increased (Table 5), the larger effect occurring in the absence of phosphate.

Protein solubility was low in low ionic strength solutions. The lower extractability of protein at lower ionic strengths was attributed to the presence of strong associations between myofibrillar proteins. Sodium tripolyphosphate (STP) concentration of 0.225% and 0.45% were not strong enough to spread protein filaments apart a t low ionic strength. However, 0.45% STP raised the pH to 7.8, which was more favorable for extraction of fish muscle proteins as indicated by the sharp increase in the percent extractability of fish protein (Figure 2). In samples without NaC1, no SSP was extracted unless STP was present. The data suggest

56 A. A. DAWOOD ET AI,.

Table 5. Effects of adding sodium chloride and sodium tripolyphosphate on the soluble nonprotein nitrogen of frozen mechanically deboned fish (% nonprotein nitrogen = mg nonprotein nitrogen/100 rng total protein “N X 6.26”)

YO Sodium Chloride

Sodium 0 .o 3 .O 3.6 Meanh tripolyphosphate

w YO Nonprotein Nitrogen

0.000 7.77“ 6.11 5.15 6.34 0.225 6.07 6.07 6.06 6.07 0.450 5.75 5.60 5.61 5.65 Meanb 6.53 5.93 5.61

‘Standard error for each cell mean ( N = 12) is 0.01 ’Standard error for each row or column mean ( N = 36) is 0.005

PERCENT TRIPOLY PHOSPHATES FIG 2 EFFECTS OFSODIUM CHLORIDE ANDSODIIJM TKIPOLYPHOSPHATE. IN VARYING CONCENTRATIONS AND COMBINATIONS. ON THE SALT-SOLUBLE PROTEIN FRACTION

EXTRACTED FROM FROZEN MECHANICALLY DEBONED FISH 0-0 0 0% NaCI. . . 3.0% NaCl and X - - - X 3.6% NaCl


tha t adding STP sharply increased the extractability of SSP in the absence of NaCl (Figure 2). However, the addition of STP in the presence of 3.0% NaCl had slight adverse effect on the extractability of SSP.

WSP was lowest at the 0.45% level of STP(Tab1e 6). Once again, this effect was expected, since the amount of SSP increased as STP increased.

Table 6. Effects of adding sodium chloride and sodium tripolyphosphate on the amount of water soluble protein extracted from frozen mechanically deboned fish (% water soluble protein = mg water soluble protein/100 mg total extracted protein)

% Sodium Chloride

Sodium 0.00 3.00 3.60 Meanh tripolyphosphate

w W Water Soluble Protein

0.000 99.21 36.68 35.13 57.00 0.225 88.91 46.11 50.51 61.84 0.450 44.26 37.41 43.78 41.82 Mean’ 77.46 40.07 43.14

‘Standard error for each cell mean (N = 6) is 0.08 hStandard error for each row or column mean (N = 18) is 0.04

Myosin heavy chain (MHC) did not solublilize in samples containing only 0.225% STP and in the absence of NaCl or STP (Table 7). These data indicated that MHC is not soluble at low ionic strength. However 0.45% STP solubilized myosin. The effect of the latter concentration of STP may be due to the high pH (7.8) of the extraction solution. As NaCl increased, MHC total area increased in samples containing no STP. In general, adding either NaCl or STP increased the solubility of MHC.

Effects of Additive on pH, Swelling and Gel Formations

It is interesting to note changes in pH caused by adding NaCl and STP, since protein solubility, swelling, gel formation and WHC in fish muscle are affected by pH (Table 8). As NaCl was increased, the pH of frozen deboned fish decreased. As STP increased, pH also increased. Adding STP to meat increased its pH, which in turn increased the negative charge on myofibrillar proteins. There were no remarkable changes in pH caused by adding soy protein isolate to frozen minced fish.


Table 7. Effects of adding sodium chloride and sodium tripolyphosphate of Myosin Heavy Chain of frozen mechanically deboned fish

W Sodium Chloride

0.0 3.0 3.6 Mean'

Myosin Heavy Chain (MHC) total peak area measured by scanning MHC from 20 ng total extracted protein sample

expressed a s millivolte scanner output coded by multiplying W Sodium Tripolyphosphate by 10"

0.000 - 0.74 1 .oo 0.58 0.225 - 2.14 1.14 1.09 0.450 2.59" 1.85 1.45 1.96 Mean' 0.86 1.57 1.19

'Standard error for each cell mean (N = 9) is 269 millivolts 'Standard error for each row or column mean (N = 27) is 155

Table 8. Effects of adding sodium chloride and sodium tripolyphosphate on pH of frozen mechanically deboned fish

W Sodium Chloride

0.0 3 .O 3.6 Meanb % Sodium

trip01 yphosphate pH Readings

0 .ooo 6.86" 6.20 6.14 6.40 0.225 7.27 6.41 6.38 6.69 0.450 7.80 6.61 6.67 7.05 Mead 7.31 6.43 6.40

'Standard error for each cell mean (N = 6) is 0.002 'Standard error for each row or column mean (N = 18) is 0.001

The data on swelling (Table 9) shows as NaCl increased, swelling decreased. Schults et al. reported similar results, stating that meat swelling decreased with the addition of 36% NaC1. The decrease in swelling was attributed to the exchange of Mg" and K' by Na'. As amounts of STP blended with frozen minced fish increased, swelling also increased. Swelling is due to the ability of inorganic phosphate to split actomyosin into its component proteins actin and myosin, result- ing in the uptake of water. Swelling of fish muscle increased as SPI increased due to the tendency of this protein to absorb HzO.

Gel forming ability has been measured at Least Concentration End- point (LCE). LCE is the minimum protein concentration required to form a gel. The LCE of total extracted protein for gelation increased as the concentration of NaCl increased (Table 10). These poor gelation


Table 9. Effects of adding soy protein isolate on percent swelling of frozen mechanically deboned fish

W Sodium Chloride

0.0 3.0 3.6 Meanb % soy

Protein Isolate 96 Swelling

0.0 72.19" 49.65 42.50 54.78 2.0 73.48 54.42 52.63 60.18 4.0 88.67 70.62 63.54 74.38

"Standard error for each cell mean (N = 12) is 1.10 'Standard error for each row or column mean (N = 36) is 0.63

Table 10. Effects of adding sodium chloride and sodium tripolyphosphate on the least concentration endpoint of frozen mechanically deboned fish extracted protein

% Sodium Chloride

0.0 3 .O 3.6 Meanb % Sodium

Tripolyphosphate Least Concentration Endpoint for Stable Gel

0.000 1.41" 4.36 5.62 3.40 0.225 1.40 5.53 6.87 4.60 0.450 1.22 7.75 7.31 5.43 Meanb 1.34 5.88 6.60

"Standard error for each cell mean (N = 12) is 0.11 'Standard error for each row or column mean (N = 36) is 0.06

properties in samples containing NaCl were probably related to high ionic strength and possibly lower pH in these samples. The LCE was decreased by adding 0.45% STP only in samples containing no NaC1. Soy protein isolate slightly improved formation of gel in samples of frozen minced fish.

Further Processing of Minced Frozen Fish From this basic knowledge of the functionality of sucker proteins, it

was decided to utilize the frozen mincd sucker in two different products: (1) sausage type and (2) canned minced products. The addition of 3.0% NaC1,0.45% STP and 4% SPI were adequate for the sausage formulation. However, samples containing 0.45% STP without NaCl had 50% of its total protein content solubilized and the highest solubility of MHC occurred with that treatment. Those samples also had the


highest pH and swelling and the best gel forming ability. Therefore, it was decided to use the same blend of minced fish in a canned product with the addition of 1.0% NaCl to improve product taste. Since4% SPI did not improve the functional properties of fish products imparted a soy flavor to the finished product, 4% corn meal w a s substituted in product formulations.

The addition of fat was needed since sucker flesh contained only about 2% fat, and fat is needed to improve succulence and acceptability of products.

Fish sausages showed low binding characteristics. Sausages in treatment A shrank more when heated to 82" C internal temperature for 30 min. than any of the other sausages and shriveled or had poor physical structure and shape, whereas the others appeared normal. The data (Table 11) indicated that adding corn meal, SPI and hydrogenated vegetable oil (HVO) with NaCl and STP improved the WHC, texture and cook yield of the sausages.

Canned minced frozen sucker also showed low binding characteristics. Again the treatment A group shrank more than the other treatments. When the finished products had been processed at 121" C for 75 min., all but those subject to treatment A showed relatively firm structure with few air pockets.

Treatment A showed approximately 80% WHC. Further improve- ment in WHC was obtained by adding SPI and/or corn meal (treatment A vs B, C and D) (Table 12). The greatest WHC (98.79%) was obtained by using 4% SPI and 4% cornmeal in combination with the other ingredients. The canned fish product made according to treatment A was soft and mushy and difficult to slice. Firmness with the addition of 4% SPI (treatment B), 4% cornmeal (treatment C) and a combination of the two (treatment D).

In conclusion, results showed that sodium chloride increased protein solubility, but also decreased swelling, gel forming and pH. In comparison, sodium tripolyphosphate increased protein solubility, pH, swelling and gel formation. Fish sausages and canned products showed low binding characteristics. However, adding cornmeal and soy protein in combination with sodium chloride and sodium tripolyphosphate improved their water holding capacity, texture and cook yield. I t was concluded that sodium tripolyphosphate, cornmeal and fat should be used in manufacturing minced sucker products.

Tab

le 1

1. A

vera

ge p

erce

ntag

es*

and

stan

dard

dev

iati

ons

of c

ooki

ng loss, w

ater

hol

ding

cap

acit

y an

d sh

ear

forc

e (k

g-fl

3.0 c

m

sect

iona

l 0) o

f sm

oked

fish s

ausa

ges

Tre

atm

ents

A

B

C

D

E 23

.20b

rg f 0.

14

21.1

5Ceg

f 1.77

22

.43'

"f

1.34

18

.83"

cd f 1

.64

Coo

king

los

s %

(N

= 2

) 34

.65 f 0.

49

Wat

er h

oldi

ng

capa

city

%

83.1

0 f 1

.62

90.2

0" f 1

.47

93.0

0* f I .

20

98.0

4' f 0.

95

99.5

3df

0.17

N

= 8

) Sh

ear

forc

e 0.

94 f 0

.06

0.80

" f 0.

09

I .03

bC f 0.

05

I .03

"' f 0.

05

1 .52

d f 0.

10

N=

12)

*Ave

rage

per

cent

age

in t

he s

ame

row

not

fol

low

ed b

y th

e sa

me

supe

rscr

ipt

are

sign

ific

antl

y di

ffer

ent (

P <

0.05

)

A =

29;

NaC

l B

= N

aCI.

8% h

ydro

gena

ted

vege

tabl

e oi

l (H

VO

) C

= N

aCI.

8% H

VO

. 4%

soy

pro

tein

Iso

late

(SP1

) D

= N

oCI.

8% H

VO

. 45

corn

mea

l E

= N

aCI.

8%

HV

O. 4%

SPI.

4%

cor

n m

eal

3 m

U

In311 sa

usag

es(A

. 8. C

. Dan

d E

)the

loll

owin

gadd

itiv

esan

d sp

ices

are p

rese

nt: -

0.45

"i.s

odiu

m

trip

olyp

hosp

hate

.O.O

~mon

osod

ium

glut

amat

e.O

.O5C

/cso

dium

asco

rbat

e.

0.Sr

; co

nden

sed

smok

e. a

nd m

ixed

spi

ces.

Tab

le 1

2. A

vera

ge p

erce

ntag

es'

and

stan

dard

dev

iati

ons o

f bak

ing

loss

, wat

er h

oldi

ng ca

paci

ty a

nd sh

ear

forc

e of c

anne

d m

ince

d fi

sh

Tre

at m

ents

l A

B

c

D

?

?

Bak

ing

loss

o/i

(N

= 2

) 0.

73' f 0.

05

0.69

h' f 0.

01

0.41

" 5~

0.0

0 0.

33" f 0.

09

Wat

er h

oldi

ng

capa

city

7;

(N =

8)

tr *

79.2

4" k

1.2

7 92

.24h

f I

.00

95.3

3' f 0.

73

98.7

9"*

0.21

s 0

0.31

' * 0

.02

0.41

" f 0

.02

0

Shea

r fo

rce

(N =

12)

0.

18" f 0.

12

0.29

' + 0

.01

Kg-

Ti I

.8 c

m c

ross

ecti

on

U

H

>

*Avc

r;ig

c p

ercc

nta

gc

in I

he b

ame

row

no

t Io

llo

wcd

hy

thc

sam

e .iu

psrs

crip

l ar

e si

gnif

ican

tly

dif

lcre

nl (

IJ<

0 05

1

A =

Xh

S<:i

mec

han

ical

ly d

ehon

cd I

rwe

n Ii

sh (

MII

FF

) I3

= X

?.S'

i, M

DI-

F. 4

?+

soy

pro

lein

iso

lil~

c

C =

X?

5'7

MII

FF

. 4r4

co

rn m

eal

I) =

7X.5

<7 M

DF

F. 4

% s

oy p

rofr

ln s

o la

ic. 4

Q c

orn

mea

l

In a

11 I

tc;l

tmcn

t\

(A,

R. C

. [I

) th

e fo

llo

win

g a

dd

itiv

es a

nd

spi

ces

are

pres

ent

4(:6

he

Kf

lrip

e. X

?i

hydr

ogen

ated

veg

etah

lc o

il.

ICt

sod

ium

ch

lori

de.

0 4

SS

sod

ium

lr

ipol

ypho

spha

te.

0.30

wh

ile

pepp

er p

owde

r. (1

.159

; o

nio

n p

ow

der

. 0.1

5% g

arlic

po

wd

er. 0

30%

pap

rika

pep

per

po

wd

er a

nd

O.O

5'!i

gro

un

d g

ing

er

r


REFERENCES

ASGHAR, A. and N. T. M. YEATES. 1974. Systematic procedure for the fractionation of muscle protein with particular reference to biochemical evaluation of meat quality. Agr. Biol. Chem 38(10): 1851-1858.

BAKER, R. C. 1978. New products of poultry and fish. In “Proceedings of the Meat Industry Research Conference” Amer. Meat Inst. Found. 1600 Wilson Blvd., Arlington, VA.

BREMNER, H. A. 1977. Storage trails on the mechanically separated flesh of three Australian mid-water fish species. 1. Analytical test. Food Technol- ogy in Australia. 29(3):89.

BRISKEY, E. J. and T. FUKAZAWA. 1971. Myofibrillar proteins of skeletal muscle. Adv. in Food Res. 19:279.

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ACKNOWLEDGEMENTS

The work reported herein was supported in part by the National Fisheries Institute, Washington, D. C. and the National College Sea Grant Program.

Appreciation is also extended to Ms. Cherine LeBlanc who served as laboratory technician in support of the Sea Grant project.

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UTILIZATION OF MINCED SUCKER FLESH