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Citation = BULLETIN OF THE FACULTY OF FISHERIES HOKKAIDO UNIVERSITY,36(4): 258-266
Issue Date 1985-12
Doc URL http://hdl.handle.net/2115/23896
Type bulletin
File Information 36(4)_P258-266.pdf
Hokkaido University Collection of Scholarly and Academic Papers : HUSCAP
https://eprints.lib.hokudai.ac.jp/dspace/about.en.jsp
36(4)258-266. 1985
2
-fI~*
Quality Control of Gel-forming Ability in Manufacturing
Kamaboko" 2
A quality of salted meat paste and
its deterioration during preservation
Akihiko HASHIMOTO* Shin-ichiro NISHIMOTOandNoboru KATOH**
Abstract
It is well known from experience thaadeterioration of the gel-forming ability in manufacturing kamaboko..was caused by using such salted meat ps*"'..hahadbeen ground to higher temperauresor that had been preserved for long time in a refrigerator.
In this respechepr
: 2.
1
Theragrachalcogramma 8A
76%pH 7.2 4% 4%0.2%
(K4)8-
12%) } pH
Hobar (2kg)
8.C20.C 30.C 3% 8-20
8.C 30( 48mm)
90.C20
-RMT-1300 lX12mm( 16.)
11mm2)
(g)
20.C 7-10
6-11.C 5.10.15. 20.C 02 6 12
24(8M-G90)
(3.8cmX1.5 cm) 35.C 60 90.C 20
3)
(Mf) CaATPase
35g Mf (0.1M KCI 40 mM Borate buffer pH 7.0) Mf
Biuret 5g MfMf
CaATPase (EC3613) 5 mM CaCI2 50 mM KCI 25 mM Tris-malea (pH7.0)
lmMATP 25.C
5g (molPi/min5g of pas)
0.4g 1% 8D88M
1%21OmM buffer(pH 7.2) 15ml ~. 9.10) Weber
and Osborn 11) 0.1% 8D8 5%
Coomassiebrilliant blue-R
Dual-wavelengthTLC 8canner C8-910
lXIX3mm
24
12.13) 1%
Awd
Fhd
q
36(4).1985.
5-250
C T.ble1 8-20
305
5-150
C
200
C
30oC 14)
200
C
Table1 5-80
C
5-20o
C
24h
Fig.l
(Mf) Ca-ATPase
MfCa-ATPase
20oC 2h 30%
150
C 200
C
70-85% Table 1
(200
C) Mf
150
C WC
50
C 1
50%
Table 1. Gel-forming ability of the saledmeatp groundovarious temperures.Frozen surimi of Alaska poll kCspecialA grade) was crushed inopieces and chopped with 3% NaCl for 8-20 min aroomtempera of80 200 and 30
o
C using a Hobart silencuer. The salted meat p teshaving various temperatures in the range of 5-25
0
C thus obtained were stuffed into casings after 30min and cooked a900Cfor 20min. The evaluation of the gelexturewas performed by auhors'methodCRef. 2).
mTeemat pperaasttue re of CC)
Jelly strength Cg)
Depth of depression (cm)
Ge(l gs-trceHn17 gth
5 900 0.94 423
10 930 0.95 442
15 1080 1.02 551
20 760 0.51 194
25 450 0.39 88
260-
5 I 10 I 15 I 20
Pres vationtemperature (C)
tilapi 24 h
~
24 h
Fig. 1. Effect of preservation time and tem
perature on the quality of the saldmeat paseof Alaska pollk.The salted meat paste (5-8"C) was
obtained by grinding the surimi with
3% NaCl for about 10 min and preser-ved at 5 10 15 20 and 25"C for 2 6 12 and 24 h. After the presevaionthe meat pastes were comminuted to make them homogeneous stuffed into casings and cooked at 35"C for 60 min followed by 90"C for 20 min. The jelly srengthof kamaboko was asses-
sed using a rheolometer (Ref. 1 and 2) The myofibrils w quantiativelyprepared from 5 g ofhemeat paste just before cooking and the
myofibrillar Ca-ATPaseotalactivity was estimated (Ref. 1 and 3). In this
figure jelly strength of meat p teand myofibrillar Ca-ATPaseotalactivity
were expressed as the relative values ; the estimated values for 100% ~.ere
1820:t 50 g and 1128molPijmin5 g of paserespectively
white croaker
5
2.
100
50
100
50
()
(N
)K22o-ovow0U
CO
{nU)pgh--0020
-261
Fig. 2. Effect of preserv iontime and tem
peraureon the qualiyof the salted
mea p of white croaker and tilapia.
The experimental method and condi-tion were same as in Fig. 1 except that
hesalted meat pew usedfrom white croaker and tilapia and preser-
vation time was fixed for 24 h
2 h
6h
12 h
24 h
:
5 Preservat ion
5
5
50
nunu
AU
(R
)
(
HU)
OE03
8EomcZb-o-
[email protected]
-a
0
100
0
100
50
50
100
50
()
2000 ~ 10
E
>-300
2
36(4).1985.
;;j:!
O 2 3 4 5
Preservation time ( h )
Fig. 3. Effect of amounts of NaCl added on the quality ofhesalted meat paste of Alaska pollack during pr ervationThe surimi was ground wih2 3 4 and 5% NaCl for 7-15 min and pre-ved at 15"C. At appropriate iner-valshemeat pasew commmuedagain and used forhepreparionof kamaboko andheevaluation of jelly srength. Compared tohechange of gel-forming abiliyfor this saledmeat pethat for surimi (no salt added) was quoted from previous paper (Ref. 2). Amounts of NaCl added to the surimi were as follows ;
(e) 2% (0) 3% ()4% ()5% and ()0%.
15.16)
(Fig.2) 20"C 24h
C-ATPase 50%85%
(100%)
Mf
1)
lO"C 24h 70% MfCa-ATPase
90% 20%50%
0 2 3 45%
15"C Fig.3
2%5%2
5% 20 MfCATPase
17) B'8) Mf
Mf
15"C
0-8h Fig.4
()
8h
4tc.o 2000g
500g 1/4
262
: 2.
20
!! 1000
p1.-a .
. .
3 . a 2 .
100 o 2 4 6 8
Preationtime (h)
- setting IyrZZZZl1I cooking(90OC.20 n)ftersettir
E comminutirndcooking (90C.20n)after ttir
::::.1 re-comminutirndcookir (35C.1h+90C.20min)after setting
Fig. 4. Effect of the re-comminution for
preserved saledmeat paseon the
gel-forming ability.
Salted meat p (3%NaCI) of Alas
ka pollack was preserved 150C. At an interval of 2 h a portion of it was
taken out and cooked soon or cooked afercomminuting iagain. The jelly
strength of kamaboko thus obtained was ass sedusing a rheolometer (Ref
1 and 2). As a comparison the evalu- ionof jelly strength for the ravmeat paste d uring preservation was also
made
40%
8h 350
C 60
()
8h Mf
Mf
10)Fig. 4
SDS- Mf
Fig.5
Mf (HC/A)
8h
350
C 60
2
150
C
()
()
Fig.4 8h
Fig.6(B)(D)
(A) (C)
(AC)
(BD)
263-
36(4). 1985
1.57 11
1.86/1 ( HC I A )
o h
4 h
~
HC
~t
1.06/1
h 8
O
0.3
coDO
0.87 11 0.1
O @
Fig.5. SDS-polyacrylamide gel electrophoreogramsofhesalted meat paste during preservation and i densitogramsA portion of the preserved sal ted me p teof Alaska pollack obtained in the experiment shown in Fig. 4 dissolvedin 1% SDS 8M urea 1% 2-mercapethanolld10 mM phosphate buer(pH 7.2). 15-20g prolnw applied0
SDS-polyacrylamide gel (5%) ac rdinghemethod of Weber and Osborne (Ref 10). Preserv iontime of salted meat p teat 150C is entered onhisgure.8 hIShesample th the vedmeat pa.ste 15Cfor 8 h v COffiffiInUedandhenpreserved a35'Cfor 1 h. Abbreviations used are; HC myosinheavy chain A =
actin SDS=sodium dodecyl sulfate. Numerals below polyacrylamide gels in figure expheratio of area underhepeak of densiogramcorrespondingoHC and A (HCjA)
(D)t
co qL
2
Fig. 6. Micrographs ofissueslice of kamaboko prepared fromhere-comminuted salted meat p afrpreservatIOn
Kamaboko samples obtained inheexperimenshownin Fig. 4 were used in this udy. Bar=0.1 mm (A) fresh me p wascooked at 90Cfor 20
(B) preserved meat p 15Cfor 8 h was comminuted again and cooked s neasA
(C) fresh meat p wascooked 35Cfor 1 h followed by 90Cfor 20 min (D) preserved meap teat 15Cfor 8 h " comminutedagain and cooked same
C
L
Mf!J '/
() Mf!J'/Mf Ca-ATP e
3) SDS
Mf
10l
-265
36(4).1985.
1) (1985). l
. 36 139-146 2) (1983)
. 49 1429-1436 3) (1985).
. 51 847-853 4) (1985).6() p. 487-490.
.
5) (1981) () 1 p.66-80.
.6) Tanikawa E. (1971). Mrine Prod. tsin Japn. p. 340-372 Koseisha-Koseikaku Tokyo. 7) (1979)..
45 1027-1032 8) Gornall A.G. BardiVillC.S. and David M.M. (1949). Deerminationof serum proinsby
means of the biuret reaion. J. biol. Chem. 177 751-766. 9) (1976). SDS
. 42 1169-1176 10) (1985)
. 51 1559-1565. 11) Weber K. and Osborn M. (1969). The reliability of molecuar weigherminaionsby
dodecyl sulphate-polyacrylamide gel electrophoresis. J. biol. Chem. 244 4406-4412. 12) (1977). P 47-91 P 135-161.
13) (1967) P 131-158.14) (1984)
. 50 2103-2108. 15) (1982). Ca-ATPase.
48 671-684 16) H himoA. and Arai K. (1984). Temperature dependence of Mg-ATPase activity and its
Ca-sensitivity of fish myofibrils. Bull. Jpn. Soc. Sci. Fish. 50 853-864. 17) (1983) Ca-ATPase
. 49 237-243. 18) (1984).B 50
635-643
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