• Title/Summary/Keyword: denaturation

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Study on the Quality Improvement of Sardine Surimi (정어리 냉동고기풀의 품질개선에 관한 연구)

  • Oh, Kwang-Soo;Moon, Soo-Kyung;Lee, Eung-Ho;Kim, Bok-Gyu
    • Korean Journal of Food Science and Technology
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    • v.25 no.4
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    • pp.327-333
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    • 1993
  • The processing conditions and quality of sardine surimi were examined: Raw sardine meat was separated, washed in 0.2% $NaHCO_3$ and 0.15% NaCl solution, and then dewatered by centrifuge. The dewatered sardine meat was chopped, mixed with 20% emulsion curd (soybean protein : water : refined sardine oil=1:5:2.6), 4% sorbitol, 4% sucrose, 0.2% polyphosphate and 0.1% sodium erythorbate by stone mortar. The mixed sardine meat was frozen with contact freezer, packed in carton box and then stored at $-25{\pm}2^{\circ}C$. The moisture, crude protein and lipid contents of the sardine surimi product was 73.3%, 15.0% and 6.9%, respectively. Fatty acid composition of product consisted of 28.8% of saturates, 24.3% of monoenes and 47.7% of polyenes and the major fatty acids were 16:0, 20:5, 18:1, 22:6 and 16:1. The results of changes in POV, TBA value, fatty acids, texture and sensory score of products during frozen storage showed that lipid oxidation and freeze denaturation of product could be retarded, and flavor enhanced by addition 20% emulsion curd and 0.1% sodium erythorbate. In an attempt to apply sardine surimi in producing surimi-based product, it was concluded that pollack surimi could be substituted with sardine surimi up to 40% without showing any significant changes in texture and taste of surimi-based product.

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Influence of Thermal Oscillation on Quality of Frozen Foods Stored in Domestic Refrigerator (가정용 냉장고의 제상 주기와 온도 변화가 저장 식품의 품질에 미치는 영향)

  • Kang, Gil-Jin;Auh, Joong-Hyuck;Kim, Myo-Jeong;Cho, Kwang-Yeun;Choi, Young-Hoon;Jung, Dong-Sun;Kook, Seung-Uk;Park, Kwan-Hwa
    • Korean Journal of Food Science and Technology
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    • v.28 no.4
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    • pp.624-631
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    • 1996
  • Effect of fluctuation range and intervals of defrosting temperature on quality of frozen foods stored in a domestic refrigerator equipped with an automatic defrost system was evaluated. As defrost system was operated, temperatures of domestic refrigerators were elevated from $-18^{\circ}C\;to\;-5^{\circ}C\;and\;-15^{\circ}C$, and fluctuation intervals were l6 hrs and 30 hrs, respectively. Quality deterioration such as protein denaturation, vitamin loss, exudate production and changes in appearance of frozen foods was minimized by reducing temperature oscillation during storage. Considerable effects of thermal oscillation on ice crystal sizes were observed for frozen beef tissue and ice cream. TTI (time temperature indicator) system also proved that the temperature control of defrost system in domestic refrigerator can improve the quality of foods during storage.

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Processing Optimization and Physicochemical Characteristics of Collagen from Scales of Yellowfin Tuna (Thunnus albacares)

  • Han, Yuna;Ahn, Ju-Ryun;Woo, Jin-Wook;Jung, Cheol-Kyun;Cho, Sueng-Mock;Lee, Yang-Bong;Kim, Seon-Bong
    • Fisheries and Aquatic Sciences
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    • v.13 no.2
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    • pp.102-111
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    • 2010
  • This study was conducted to investigate the optimal conditions of collagen extraction from scales of yellowfin tuna (Thunnus albacares) using surface response methodology. Four independent variables of NaOH concentration and pretreatment fime in alkali pretreatment and enzyme concentration and treatment time in enzyme hydrolysis were used to predict a model equation for the collagen yield. The determinant coefficient ($R^2$) for the equation was 0.906. The values of the independent variables for the maximum yield were 0.32 N NaOH, 16.38 h alkali pretreatment time, 0.18% enzyme concentration, and 31.02 h enzyme treatment time. In the physicochemical properties of tuna scale collagen, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of tuna scale collagen showed the same migration distances as that of calf skin collagen. The amide A, I, II, and III regions of tuna scale collagen in Fourier transform infrared measurements were shown in the peaks of 3,414 $cm^{-1}$, 1,645 $cm^{-1}$, 1,553 $cm^{-1}$, and 1,247 $cm^{-1}$, respectively. The amount of imino acids in tuna scale collagen was 18.97% and the collagen denaturation temperature was $33^{\circ}C$. The collagen solubility as a function of NaCl concentration decreased to 4% NaCl (w/v) and the collagen solubility as a function of pH was high at pH 2-4 and sharply decreased from pH 4 to pH 7. Viscosity of the collagen solution decreased continuously until $30^{\circ}C$ and this decreasing rate slowed in the temperature range of $35-50^{\circ}C$.

Cryoprotective Effect and Mechanism of Corn Starch Enzyme Hydrolysates on Fish Protein 1. Cryoprotective Effect of Corn Starch Enzyme Hydrolysates on Fish Protein (전분가수분해물의 어육단백질 동결변성 방지효과 및 작용기구 1. 옥수수전분가수분해물의 어육단백질에 대한 동결변성 방지효과)

  • LEE Kang-Ho;JUNG Byung-Chun;HONG Byung-Il
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.31 no.6
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    • pp.823-828
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    • 1998
  • The objective of this study is to investigate cryoprotective effects of corn starch enzyme hydrolysates of nonsweet and low-calories on denaturation of frozen fish protein. The cryoprotective effects of were examined in Alaska pollack actomyosin solution by changes in SDS-PAGE pattern, solubility, and $Ca^{2+}$-ATPase activity. When samples stored for 0 and 30 days were compared on SDS-PAGE patterns, severe changes in all bands were shown on the control sample regardless of storage temperature, especially in myosin heavy chain (MHC). Not much difference no appeared the electrophoretic pattern in case of the samples containing sucrose at any storage temperature during 30 days of storage. The cryoprotective effect of the hydrolysates were markedly dependant on storage temperature and no MHC band was found in the samples stored at $-5^{\circ}C$. The SDS-PAGE patterns of sample stored at $-20^{\circ}C$, however, completely maintained after 30 days or storage. When the samples were stored at $-5^{\circ}C$, the solubility of the sample containing sucrose was retained at $90\%$ after 30 days of storage, whereas dramatically decreased in other samples. The samples including sucrose, D.E. 10, 15, and 20 revealed $90\%$ in solubility when stored at $-20^{\circ}C$. The tendency of remaining $Ca^{2+}$-ATPase activity was almost shown the same as that of solubility.

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Exploration of optimal Lactobacillus plantarum strains for curdling milk for yogurt and evaluation of physicochemical and sensory properties (호상 요구르트에 적합한 Lactobacillus plantarum strains 탐색 및 요구르트의 이화학적 및 관능 특성)

  • Jeong, Seong-Yeop;Lee, Yong Hyen;Kang, Suna;Shin, Bae Keun;Park, Sunmin
    • Korean Journal of Food Science and Technology
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    • v.48 no.6
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    • pp.548-554
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    • 2016
  • Since some strains of kimchi lactobacilli can curdle milk, they can be used for making yogurt. However, the best Lactobacillus plantarum strains for curdling milk for yogurt are still unknown. In this study, we determined the best L. plantarum strains for curdling milk, and the physicochemical properties of yogurts made using different L. plantarum strains were examined. Three strains of L. plantarum useful for curdling milk were identified (YD2, YD9, YD12). The number of lactobacilli was lower in yogurts made with L. plantarum than in those made with control, and among the L. plantarum strains tested, YD12 had the highest bacterial counts. However, the microbial count reached $6.3{\times}10^8CFU/mL$ after 24-h fermentation in all yogurts. The pH of the yogurts decreased after 12-h fermentation, while the acidity increased. The low pH and high acidity decreased the viscosity in all the three types of yogurts, because the acids disturbed gel formation due to protein denaturation. Sensory evaluation revealed that the YD12 group showed a high percentage of completion similar to the control group. YD2 and YD9 showed a high sourness value and low sweetness value, whereas YD12 yielded optimal values for all the organoleptic characteristics. Therefore, YD12 would be a high quality bacterial strain for use as a yogurt starter culture.

Effect of Heating Rates on the Thermal Denaturation of Pork Loin Muscle (가열속도가 돈육 등심 근육의 열변성에 미치는 영향)

  • Kim, Cheon-Jei;Song, Min-Seok;Lee, Chang-Hyun;Lee, Eui-Soo;Cho, Jin-Kook;Choi, Do-Young
    • Korean Journal of Food Science and Technology
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    • v.31 no.3
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    • pp.678-681
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    • 1999
  • The objective of this study was to evaluate the effect of different heating rates on the thermal properties of pork loin muscle by DSC. Pork loin muscle was subjected to programmed heating at the following heating rate: 5, 10, 20, 30 and $40^{\circ}C/min$. Peaks were progressively shifted to right side as the heating rate was increased. $T_0$ was $50.39^{\circ}C$ at $5^{\circ}C/min$ and it was increased to $57.45^{\circ}C$ at $40^{\circ}C/min$ (p<0.05). Total enthalpy was 3.52 J/g at $5^{\circ}C/min$ and total enthalpy was increased to 3.60, 4.14, 4.54 and 4.61 J/g by degrees at heating rate 10, 20, 30 and $40^{\circ}C/min$ respectively.

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The Effect of Freezing Rates on the Physico-Chemical Changes of Beef during Frozen Storage at $-20^{\circ}C$ (동결속도에 따른 쇠고기의 냉동저장중 이화학적 변화)

  • Kim, Young-Ho;Yang, Seung-Yong;Lee, Moo-Ha
    • Korean Journal of Food Science and Technology
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    • v.20 no.3
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    • pp.447-452
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    • 1988
  • In order to study effect of freezing rates on the quality changes such as pH, TBA value, free fatty acids and protein extractability, cylindrical chopped beef logs with 10cm of diameter and 10cm of height were frozen at three freezing rates(0.97cm/hr, 2.05cm/hr, 3.71cm/hr)using air blast freezer. Physicochemical changes of frozen meat were investigated during forzen storage at $-20^{\circ}C$ for 16weeks. Results on pH change showed $0.1{\sim}0.2unit$ increase at the 16th week of the frozen storage and the change was smaller with the increasing freezing rates. Free fatty acids content and TBA value also were increased during forzen storage, but they were minimal at 3.71cm/hr freezing rate. Correlation coefficient between TBA value and free fatty acids content were highly significant(r=0.804). After 16weeks of storage, extractibilities of salt soluble protein were decreased by 17.7%, 6.1% and 1.6% at freezing rates of 0.97, 2.05 and 3.71cm/hr, respectively. On the other hand, extractabilities of water soluble protein were decreased by 26.0%, 21.2% and 18.5%, respectively. The effect of freezing rates on the protein extractability appeared to be greater in salt soluble protein than in water soluble protein, but freezing denaturation was more rapid in water soluble protein.

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Rapid Detection for Shiga Toxin Type 1 (Stxl) by Using Two-Step Ultra-Rapid Real-Time (URRT) PCR (초고속 이단계 PCR에 의한 Shiga 독소 타입 1의 신속 검출법)

  • Kim, Il-Wook;Kang, Min-Hee;Kwon, Soon-Hwan;Cho, Seung-Hak;Yoon, Byoung-Su
    • Korean Journal of Microbiology
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    • v.44 no.3
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    • pp.203-211
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    • 2008
  • Rapid detection-method for Shiga toxin type 1 that was produced from Shiga toxin-producing Escherichia coli (STEC) was developed by two-step ultra-rapid real-time (URRT) PCR. The specific primers were deduced from 80 bp stable region of stx type 1 (stxl) gene among various informations of STEC strains. URRT PCR is a microchip-based real-time PCR using 6 ${\mu}l$ of reaction volume with extremely short denaturation step and annealing/extension step (1 sec, 3 sec, respectively) in each cycle of PCR. Using the stx1-specific URRT PCR, 35 cycled PCR were finished in time of 6 min and 38 see, also measured 7 min and 28 see including melting temperature (Tm) analysis. The detection-limit of stxl-specific URRT-PCR was estimated until 3 colony forming units / PCR with products with stable Tm at $81.42{\pm}0.34^{\circ}C$. In the applications to various STEC strains and contaminated genomic DNAs, stx1-specific URRT-PCR were tested and shown that it would be expected an useful method for the rapid detection of stx1-coded STEC strains.

Screening for raw material of modified gelatin in marine animal skins caught in coastal offshore water in Korea (수식 어류껍질 젤라틴의 원료로서 연근해산 수산물껍질의 검색)

  • Cho, Soon-Yeong;Kim, Jin-Soo
    • Applied Biological Chemistry
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    • v.39 no.2
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    • pp.134-139
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    • 1996
  • In order to effectively utilize marine animal skin wastes in marine processing manufacture, conger eel skin, file fish skin and arrow squid skin as raw material of edible gelatin were screened. Conger eel skin was the highest in the collagen content, followed by Ole fish skin and arrow squid skin, in the order named. In the fish skins, the soluble and insoluble collagens occupied $67.4%{\sim}72.3%\;and\;27.7{\sim}32.6%$, respectively, and in the arrow squid skin, 30.4ft and 69.6ft, respectively. No difference in the amino acid composition between soluble and insoluble collagens was detected. Collagen from the marine animal skin catched in coasted and offshore water in Korea consisted ${\alpha}$ chain and ${\beta}$ chain, and ${\alpha}$ chain were hetero type. The sum of proline and hydroxyproline contents in conger eel skin collagen was higher than that in the other skin collagens, while was lower than that pork skin collagen. Conger eel skin collagen exhibited a higher denaturation temperature in solution and a higher degree of proline hydroxylation, compared with skin collagen of the respective species. The physical properties such as gel strength, melting point and gelling point of conger eel skin gelatin were superior to those of file fish skin and arrow squid skin gelatins.

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Studies on Preservation of Concentrated Milk by Freeze - Flow Process (Freeze - Flow Process 를 이용한 농축우유의 저장에 관한 연구)

  • Lee, Young-Chun;Shin, Dong-Bin
    • Korean Journal of Food Science and Technology
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    • v.17 no.6
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    • pp.500-505
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    • 1985
  • A method to store concentrated milk in the liquid state at $-15^{\circ}C$ was developed, and quality changes during storage of milk were evaluated. Combined cryoprotectants (CCP) suitable for storing concentrated milk in the liquid state at $-15^{\circ}C$ were consisted of 17.74% sucrose, 8.87% glucose, 8.87% fructose, 2% glycerol, 0.25% sodium hexametaphosphate, 0.25% NaCl and 0.02% ascorbic acid. The amount of CCP to be added to concentrated milk to depress freezing point to $-15^{\circ}C$ was 38% by weight. Gelation due to protein denaturation was the most serious quality change during storage, which adversely affected appearance and utilization of the stored product. Gelation was observed after 3 weeks storage in the control, but it was not in milk with CCP throughout 18 weeks storage. Amount of protein precipitated increased in the control during storage, whereas there was no protein precipitated in milk with CCP. Surface color and peroxide value of the control and treatment did not change significantly during storage, and there were no marked differences between the control and treatment. These results indicated that quality of concentrated milk could be preserved, without gelation, by storing milk with CCP in the -liquid state at the frozen storage temperature. Besides, energy required for freezing preservation of milk could be significantly reduced by elimination of phase changes for freezing and thawing, and the stored product could be continuously processed for the final products without long waiting time for thawing.

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