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Development of a product which simulates abalone texture from Alaska Pollock (Theragra chalcogramma) SurimiChang, Seong Ook 26 August 1988 (has links)
The objective of these studies was to develop an
analog from surimi that would resemble abalone.
Preliminary studies involved the standardization of batter
preparation conditions, such as pH adjustment, optimum
moisture content and batter mixing time. The texture of a
gelled analog prepared with different protein adjuncts
egg white, gluten and bovine serum albumin) was compared
with cooked abalone for hardness, elasticity, and
cohesiveness by a trained sensory evaluation panel and by
instrumental methods.
Serial levels of sodium carbonate were used to adjust
the pH of the sol from pH 6.75 to 7.73. As the pH value
rose, the textural strength of kamaboko correspondingly
increased. The 0.1% level of sodium carbonate was
determined suitable for further use.
The moisture level in kamaboko caused significant
variations in hardness (P<0.001) and cohesiveness (P<0.001). At the lowest level of moisture tested,
73.24%, gel hardness was greatest (l27N/g); with a 5%
increase in moisture, the gel hardness was lower (52N/g).
Sol mixing time (solubilization of myofibrillar
proteins) was a very important factor to significantly
affect gel texture for properties of hardness (P<0.00l),
elasticity (P=0.002) and cohesiveness (P<0.001). To
produce a strong, elastic and cohesive gel, 30 minutes
mixing was required.
In serial concentrations (O to 4%), egg white,
gluten, and bovine serum albumin, were evaluated for
enhancement of textural parameters in order to produce an
imitation abalone product. The addition of either egg
white or gluten at the two percent level resulted in the
greatest hardness and most cohesive gels (P<0.001). Two
percent added bovine serum albumin significantly improved
gel hardness and elasticity (P=0.003 and P=0.0149,
respectively).
A shredded gel containing one of three protein
adjuncts was effective in varying the final gel texture
when incorporated with a surimi-based carrier. In overall
parameters, the trained sensory evaluation panel judged
the analog gel containing bovine serum albumin texturized
chunks (at a 70:30 ratio to carrier) closest to cooked
abalone. The instrumental measurements of textural
parameters were slightly less discriminating than the
trained sensory panel. / Graduation date: 1989
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Development of a restructured seafood product from squid (Loligo Opalescens)Berntsen, Steven Eldon 28 July 1987 (has links)
The influence of protein adjuncts and variations in pH on the
cook-cool loss, moisture content, and texture of squid gels was
investigated. Break force (P [greater than or equal to] .025), deformation to break (P [greater than or equal to] .01)
and cook-cool loss (P [greater than or equal to] .001) decreased as the pH of squid gels was
adjusted from 6.4 to 8.3 with sodium carbonate. The moisture
content of gels increased (P [greater than or equal to] .01) as the pH was elevated. Break
force (P [greater than or equal to] .001) and deformation distance to break (P [greater than or equal to] .005) were
inversely correlated to gel moisture content.
Protein adjuncts (2%) had a significant effect on cook-cool
loss, break force and moisture content (P [greater than or equal to] .001, .026, and .018,
respectively) of squid gels. Egg white produced an improved
water-holding capacity over soy protein isolate and sodium
caseinate. The mean cook-cool loss from gels containing egg white
was 5.29 + 0.66% which was significantly (P=.05) lower than that
of gels containing soy protein isolate (12.41 + 0.17%), no
protein adjunct (16.65 + 3.82%) and sodium caseinate (19.75 +
2.42%). Gels containing sodium caseinate had a significantly (p [greater than or equal to] .05) lower moisture content and higher cook-cool loss (P=.05)
than gels containing egg white or soy protein isolate.
The break force of gels containing sodium caseinate could not
be measured because the gels possessed little fracturability when
compressed. The break-force of gels containing soy protein
isolate or egg white were equal (P=.05), but each was less (P=.05)
than observed for control gels.
Holding minced squid gel sols at 4°C for 4 and 24 hours
before forming and heat-setting into gels, had a significant
effect on the force required to break gels (P [greater than or equal to] .001) and
expressible moisture (P [greater than or equal to] .006). Control squid gels and gels
containing soy protein isolate that were formed after holding for
24 hours required a lower force (P=.05) to break gels than similar
gels formed after holding for 4 hours. Holding time did not alter
(P [greater than or equal to] .05) moisture content, cook-cool loss or deformation at break.
Reduced gel strengths observed for gels held for 24 hours prior to
heat-setting was related to protease activity, loss of reactive
sulfhydryl functions and/or cold temperature setting.
A restructured seafood product was fabricated from mantle and
tentacle muscle of squid (Loligo opalescens). Whole squid yielded
37.5 + 1.4% edible mantle and 15.3 + 1.0% tentacle meat; a total
yield of 52.2 + 2.4% based upon round weight. A restructured
product fabricated from heat-set fibers (60%) and squid sol (40%) yielded 33.4 + 1.0% based upon round weight. A consumer
preference panel found no (P [less than or equal to] .05) differences in the product
containing different protein adjuncts and judged the product to
be, at least, slightly desirable (score of 6.0 on a 9 point scale). Firmness was the only sensory attribute that a trained
panel found to be influenced (P [greater than or equal to] .05) by the incorporation of
protein adjuncts. The product containing sodium caseinate was
judged to be less firm (P=.05) than products incorporating either
egg white or soy protein isolate. Trained panel scores for
firmness were consistent with measurements for break force. / Graduation date: 1988
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Resource combination and product-mix in Oregon seafood processingChong, Kee-Chai 09 June 1978 (has links)
Graduation date: 1979
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A simulation study of the dynamic behavior of a Newfoundland seasonal fish processing operation /Boone, Aldwin Hayward, 1950- January 1978 (has links)
Thesis (M.Eng.) -- Memorial University of Newfoundland. / Typescript. Bibliography : leaves 213-216. Also available online.
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Concentration of anserine and carnosine in surimi wash water and their antioxidant activityKaur, Jasvinder 07 July 1999 (has links)
Anserine and carnosine are water-soluble dipeptides that have antioxidant
properties and are found in the skeletal muscle of mammals and fishes. These
dipeptides are removed through the washing process in surimi production. The
objective of this research was to determine the concentration of anserine and
carnosine in surimi wash water (SWW) at all stages of surimi processing, and
undertake preliminary methods to remove and concentrate the two dipeptides and
study the effect of surimi wash water extract on color. Wash water samples were
collected from a local surimi plant. The samples were treated by the following
methods: centrifugaion, heat-treatment at 60, 80 and 100°C and filtration using
different ultrafiltration (UF) membranes. The concentrations of the protein and
the two dipeptides were analyzed using Lowry and high performance liquid
chromatography with a fluorescent detector, respectively. Iron content was
determined in SWW samples using atomic absorption spectrometry and
colorimetry. Effect of SWW extract and other antioxidants on the color of fresh-farmed salmon were studied using color parameters-hue angle, chroma and
lightness. Results showed that there was a trend: content of protein and dipeptides
(anserine and carnosine) in SWW (raw) was higher in the first two stages of
surimi processing. In the second set of experiment, where different heat
treatments were used, it was found that the proteins and dipeptides showed similar
trends. Additionally, 80°C followed by 100°C treatment were effective in
removal of proteins and recovery of dipeptides. Among UF treatments, 1K
molecular weight cut-off membrane was the most effective in recovery of
dipeptides. Iron was less than 1 ppm in all SWW samples. Color measurement of
fresh farmed salmon patties revealed that treatments of SWW extract (1%) in
addition to other food antioxidants such as butylated hydroxy toluene and
camosine (1%), mamtained salmon color until day 5. Therefore, SWW extract
at lower concentrations may have an economical and potential use as a food
antioxidant. / Graduation date: 2000
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Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditionsKim, Young S. 13 December 2002 (has links)
Protein solubility of Pacific whiting muscle with isoelectric point at pH 5.5 was
significantly affected by pH. The highest breaking force was measured from fish
proteins treated at pH 11, while high deformation values were obtained at pH 2 and
11. Texture of gels made using the conventional method were quite inferior to gels
made using fish proteins treated at pH 2 or 11, while color of conventional gels was
significantly better than the other treatments. SDS-PAGE revealed that fish proteins
were highly denatured during acid or alkali treatment. High cathepsin B-like
activity was detected from acid-aided fish proteins. Strong cathepsin L-like activity
was found in fish proteins treated at pH 10.5, which corresponded with the lower
breaking force and deformation obtained from those samples. Disulfide bonds contributed to high texture value in fish proteins treated at pH 11.
Physicochemical characteristics of sarcoplasmic proteins (SP) from rockfish
and their interaction with Alaska pollock surimi (myofibrillar proteins) were
investigated. Solubility of SP was significantly suppressed at acidic pH (2-4) plus
high salt concentration (0.5 M NaCl). This was also supported by SDS-PAGE
results (extensively degraded SP). DSC results revealed SP gave three endothermic
transitions. The least amount ofproteins was lost when treated at pH 2 or 3 followed
by precipitation at pH 5.5. SP did not enhance the gelation properties of myofibrillar
proteins, but positively contributed to gelation with myofibrillar proteins when
compared to sucrose. Myofibrillar proteins were primary components contributing
to heat-induced gelation.
Salt effect on acid- or alkali-treated surimi gel was investigated. Good gels
were obtained without salt using acid- and alkali-treated fish proteins. Their texture
properties decreased as NaCl content increased, unlike conventional surimi gels.
Consequently, NaCl did not solubilize myofibrillar proteins once the fish proteins
were treated by acid or alkali. Solubility was apparently not a key factor for the
texture properties of acid- or alkali-treated surimi. Transglutaminase-mediated
setting reaction was partially inactivated during acid or alkaline treatment.
Acid-treated surimi gel gave the best color properties. / Graduation date: 2003
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Utilization of fish processing by-products for nutritional formulation of fish feedMaghaydah, Sofyan. January 2003 (has links) (PDF)
Thesis--PlanA (M.S.)--University of Wisconsin--Stout, 2003. / Includes bibliographical references.
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Solubility and structure of fish myofibrillar proteins as affected by processing parametersLin, Tein Min, 1964- 07 March 1996 (has links)
The results of SDS-PAGE and densitometry indicated that a significant amount
of myofibrillar proteins was lost during surimi processing. Microfiltration (MF) was
utilized to recover insoluble particulate. The MF-recovered proteins showed highly
functional properties in gel hardness, cohesiveness, color, and water retention ability. The
soluble proteins concentrated by ultrafiltration (UF) possessed dark colors and strong
odors. However, the use of UF demonstrated the possibility of recycling water in
leaching systems.
To reduce the loss of myofibrillar proteins during processing, the factors causing
solubilization of myofibrillar proteins were investigated. Myosin and actin were highly
soluble when their ionic strengths were substantially reduced. Salt concentrations of
0.25%, 0.5%, and 1.0% NaCl reduced the solubility of myosin and actin but did not
remove sarcoplasmic proteins effectively. At 2.0% NaCl, severe loss of myosin, actin,
α-tropomyosin, β-tropomyosin, and troponin-T was observed. At low water/meat ratio
(2:1) with increased washing cycles and washing time, more sarcoplasmic proteins per unit of water were removed without a noticeable loss of myosin or actin. Myosin heavy
chain (MHC) content, water retention ability, and whiteness of the washed mince were
comparable to that at high water/meat ratio (4:1). Prolonged storage and elevated
temperatures caused a severe proteolysis of myofibrillar proteins. The degraded proteins
had higher solubility than their native myofibrillar proteins. MHC and actin degradation
both showed a good correlation to protein solubility.
The relationship between conformational changes and solubility of myofibrillar
proteins was investigated using myosin as a model system. The results showed that
adding salt or shifting pH from the isoelectric point of myosin caused an increased
surface hydrophobicity and a decreased helix structure. A slightly increased sulfhydryl
content was also observed. These conformational changes resulted in an increased
solubility. At high salt concentration (>1.0 M), myosin regained its helix structure with
a concomitant loss of solubility. The salting out effect was probably due to the dominant
hydrophobic interaction among nonpolar amino acids residues. / Graduation date: 1996 / Best scan available. Original is a black and white photocopy.
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Recovery and utilization of catheptic proteases from surimi wash waterDeWitt, Christina A. Mireles 20 January 2000 (has links)
Graduation date: 2000
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Surimi wash water treatment by chitosan-alginate complexes : effect of molecular weight and degree of deacetylation of chitosan and nutritional evaluation of solids recovered by the treatmentWibowo, Singgih 11 November 2003 (has links)
Soluble surimi wash water (SWW) proteins could be recovered using
chitosan (Chi) complexed with alginate (Chi-Alg) generating co-products for feed
formulations. Chi with a degree of deacetylation (DD) of 84% complexed with Alg
at a mixing ratio (MR) of 0.2 was used to study Chi-Alg concentration and
treatment time protein recovery effects. Insoluble SWW solids were removed by
centrifugation and the supernatant was then adjusted to pH 6. Flocculation at 20��C
using Chi-Alg at 20, 40, 100 and 150 mg/L SWW was aided by 5 mm agitation and
holding for 30 mm, 1h and 24h. Concentration had an effect between low (20 and
40 mg/L) and high (100 and 150 mg/L) levels. Time had an effect between 30 min
and 1h but not between 1 and 24 h. Turbidity reduction was affected only by
concentration. 100 mg Chi-Alg/L SWW for 1 h achieved 83% protein adsorption
and 97% turbidity reduction while lower concentrations yielding higher adsorption
required longer times. Fourier Transform Infrared (FTIR) analysis of untreated and
Chi-Alg treated SWW solids confirmed protein adsorption. Amide band areas
normalized against a common 3005-2880 cm����� region confirmed the high protein
recovery by 100 mg Chi-Alg/L SWW. Six Chi samples differing in molecular
weight (MW) and degree of deacetylation (DD) were tested to recover soluble
SWW solids using 20, 40, and 100 mg Chi-Alg/L SWW (0.2 MR, 1h). High (94%,
93%) and low (75%) DD chitosan had lower protein adsorption (73-75%) when
compared to the intermediate (84%) DD chitosan (74-83%). Intermediate DD and
high MW Chi seemed to perform better; however, SY-1000 with 94% DD did not
follow this trend (79-86% protein adsorption, 85-92% turbidity reduction).
Insoluble SWW (P1) and soluble solids (P2) recovered using 150 mg Chi-
Alg/L SWW contained 61.4 and 73.1% protein, respectively. Rat diets formulated
with 10% protein substitution by P1 and 10% and 15% by P2 had acceptability and
protein efficiency ratios (PER) as high as the casein control with no deleterious
effects. Rat diets with 100% P2 protein substitution showed higher PER and net
protein ratio than the casein control with no deleterious effects. Protein recovered
from SWW using Chi-Alg has the potential to be used in commercial feed
formulations. / Graduation date: 2004
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