• Title/Summary/Keyword: 탈지반응

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Stability of the Fat Ingredients of Deep Fried Instant Noodles, Biscuits, and Cookies (라면, 비스킷, 및 쿠키속의 유지성분(油脂成分)의 안전성(安定性)에 관한 연구(硏究))

  • Hu, Tae-Ryun;Kim, Dong-Hoon
    • Korean Journal of Food Science and Technology
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    • v.6 no.1
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    • pp.24-29
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    • 1974
  • Deep fried instant noodles, biscuits, and cookies were prepared, using the same beef tallow as their fat ingredient. In addition to wheat flour and beef tallow, the common and major ingredients, the deep fried instant noodle contained 1.5% salt before frying, the biscuits 20.0% sucrose and 10.0% nonfat milk solid before baking, and the cookies 20.0% sucrose before baking. The three products and a portion of beef tallow, which was to be used as control, were stored in an incubator at $47.0{\pm}1.5^{\circ}C$. The peroxide value and the free fatty acid value of the control and the extracted fat were determined regularly during the storage period. The fat incorporated in the biscuits exhibited far greater stability to rancidity development than that of the control with regard to both peroxide value and free fatty acid value development. However, the fat incorporated in the deep fried instant noodles and the cookies showed much poorer stability than that of the control. Factors like a deep frying process and/or the presence of a significant amount of salt in the deep fried instant noodles appeared to promote the rancidity development of the fat incorporated in the product. On the other hand, Maillard type browning reaction products in the biscuits seemed to retard effectively the rancidity development of the fat incorporated in the product.

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Studies on the Production of Cellulase by Trichoderma sp. SO-571 and the Enzyme Treatment for Cellulosic Fabrics. (Trichoderma sp. SO-571에 의한 Cellulase 생산 및 섬유가공 처리에 관한 연구)

  • Oh, Sung-Hoon;Kim, Moo-Sung;So, Sung;Seo, Hyung-Ju
    • Microbiology and Biotechnology Letters
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    • v.31 no.1
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    • pp.42-45
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    • 2003
  • A Trichoderma sp. SO-571 producing cellulase was isolated from soil, and a pilot-scale cultivation and separation of cellulase were conducted. The cellulase activity was about 14.5 unit/ml after 112 hr of cultivation in a 301 fermenter containing 3.0% cellulose, 4.0% soybean powder, 3.0% wheat bran, 0.5% ($NH_4$)$_2$$SO_4$0.2% urea, 1.0% CSL, 0.5% $KH_2$PO$_4$, and 0.2% Tween 80. The cellulase was purified over 4.6 folds in three steps with 47.86% yield. The optimum pH of cellulase was pH 5.0 and optimum temperature was $60^{\circ}C$. To investigate the effect of the cellulase-treated cellulosic fabric, the weight loss was compared. The weight loss of denim treated with cellulase from Trichoderma sp.SO-571 was 2.9% and that with Celluclast 1.5L was 2.2%. In tencel treatement with enzyme, cellulase showed 0.7% higer weight loss than that with Celluclast 1.5L.

An Enzyme-Linked Immunosorbent Assay for Detection of Milk proteins in Food (우유단백질의 분석을 위한 효소면역측정법)

  • Shon, Dong-Hwa;Kim, Hyun-Jung;Bae, Gun-Won;Kim, Soon-Mi
    • Korean Journal of Food Science and Technology
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    • v.32 no.3
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    • pp.564-569
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    • 2000
  • An enzyme-linked immunosorbent assay(ELISA) was developed for the detection of milk proteins in processed foods. The ${\alpha}_{s1}-casein({\alpha}_{s1}-CN)$, a heat stable major milk protein, was immunized into rabbits to produce specific antibodies. When competitive indirect ELISA(ciELISA) using $anti-{\alpha}_{s1}-CN$ antibodies was established, its detection limit was $0.1\;{\mu}g/mL$. The reactivities of the specific antibodies toward ${\alpha}_{s1}-CN$, skim milk, ${\beta}-CN$ and whey protein isolate(WPI) were 100, 37, 0.14 and 0.04%, respectively, as determined by ciELISA. However $anti-{\alpha}_{s1}-CN$ antibodies did not have any reactivity to other milk proteins such as ${\beta}-lactoglobulin,\;{\alpha}-lactalbumin$, bovine serum albumin, and isolated soy protein. When sandwich ELISA was established, its detection limit was $0.01\;{\mu}g/mL$ which was 10 times more sensitive than that of ciELISA. In the spike test which was performed by adding 1-10% of whole CN to market milk, mean assay recovery as determined by sandwich ELISA was 94.8%(CV, 8.2%). Food stuffs and dairy products were assayed by sandwich ELISA to show 29, 0.13, 0.25, and 6.9% of whole CN in skim milk powder, WPI, semi-solid yoghurt, and processed cheese, respectively.

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Physico-ecological Studies on Korean Seed-mustard I. Effects of Varieties and Seeding Date on the Variation of Agronomic Traits (한국산 개자(Brassica juncea)의 재배학적 특성연구 I. 수집품종의 특성 및 파종기 차이에 따른 주요형질의 변이)

  • 이종일;이상래;최형국;권병선
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.30 no.2
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    • pp.146-153
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    • 1985
  • To investigate the possibility of improvement of seed mustard varieties, these experiments were conducted at Muan in Chonranamdo for three years with five local seed mustard varieties and seeding dates. Local varieties collected from Seoul, Cheju and introduced from Japan showed earlier bolting date while Yungsanpo and Suweon varieties bolted later and Suweon variety exhibited the latest maturity. Suweon variety had the shortest plant height with higher number of grains per pod. Seoul and Yungsanpo varieties had more total branch numbers than others. There was no varietal difference in grain weight, pod length and one liter weight. Grain yield per 10a was highest in Seoul variety by 247.5kg. Late seeding date delayed the bolting and flowering date while plant height, total branch numbers, pod numbers per ear and grain number per pod were decreased. The magnitude of varietal response to seeding date was varied greatly with traits. Grain weights per liter, 1,000 grain weight, pod lengths, oil contents, and fatty acid compositions were not affected by the different seeding dates.

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Hydrolysis of Lactose in Milk by Microencapsulated ${\beta}-Galactosidase$ (Microencapsulated ${\beta}-Galactosidase$에 의한 우유 유당의 가수 분해)

  • Baik, Ok-Ryun;Uy, Ro-Sa;Byun, Si-Myung
    • Korean Journal of Food Science and Technology
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    • v.12 no.1
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    • pp.45-52
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    • 1980
  • The nylon (poly 6, 10) microcapsules containing ${\beta}-galactosidase$ were obtained by the interfacial polymerization of 1, 6-diaminohexane and sebacoyl chloride with ${\beta}-galactosidase$ from Escherichia coli. They were generally spherical and had a mean diameter of $80{\mu}$ with 45 % of the activity recovery. In particular, there was no transport hamper of lactose through the membrane of microcapsules. The characteristics of the microencapsulated enzyme were similar to those of soluble enzyme optimal pHs, $7.0{\sim}7.2$ for the soluble and $7.3{\sim}7.5$ for the microencapsulated ; optimal temperatures, $50^{\circ}C$ for both ; apparent $K_m,\;3.33{\times}10^{-4}(on ONPG),$ $2.86{\times}10^{-3}$ M(on lactose) for the soluble and $5.28{\times}10^{-4}$ (on ONPG), $4.25{\times}10^{-3}$ M (on lactose) for the microencapsulated ; activation energies, 8.94 for the soluble and 9.78 Kcal/mole for the microencapsulated enzyme. Using this microencapsulated ${\beta}-galactosidase$, hydrolyses of lactose and milk lactose were carried out and 80 % of 5 % lactose solution and 70 % of lactose in skim milk were hydrolyzed in 40 hr at $27^{\circ}C$. The reusability and operational stability showed that the remaining activity was 50 % of the original activity after 5 runs and 120 hr of total operating time at $27^{\circ}C$.

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Studies on the Immobilization of ${\beta}-Galactosidase$ from Bacillus subtilis (Bacillus subtilis ${\beta}-Galactosidase$의 고정화에 관한 연구)

  • Jang, Gi;Kim, Chang-Ryoul;Lee, Yong-Kyu
    • Korean Journal of Food Science and Technology
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    • v.22 no.4
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    • pp.426-433
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    • 1990
  • The conditions for immobilization of the partially purified ${\beta}-galactosidase$ form Bacillus subtilis HP4 and the properties of the immobilized enzyme have been investigated. The crude enzyme precipitated with cold acetone was purified about 68-fold through DEAE-cellulose and sephadex G-100 chromatography and its recovery was 19.9% The optimal conditions for Immobilization of enzyme were obtained in 2%(w/v) sodium alginate, 15%(v/v) enzyme solution and 2%(w/v) calcium chloride, and also the optimal stirring thme was 2 hours on the above conditions. The optimum temperature and pH values for immobilized enzyme were $55^{\circ}C$ and 6.5, respectively. Its residual activity was show 25% after heat treatment for an hour at $65^{\circ}C$, and found its high stability in pH 6.0 to 8.0. The enzyme activity was not affected b)· EDTA, 2-mercaptoethanol, KCN, protective agents, and other methal ions except Hg ion and Cu ion. The $K_m\;and\;V_{max}$ values of the immobilized enzyme on ONPG were $1.82{\times}10^{-2}M\;and\;3.57{\times}10^{-8}mole/min$, whereas those on lactose were $2.94{\times}10^{-2}M\;and\;1.68{\times}10^{-7} mole/min$, respectively. The remained enzyme activity for the immobilized enzyme was 95%t of original activity after storage of 40 days at $4^{\circ}C$, and when reused for 5 times was 81%. When skim milk(4.8% lactose) and 5% lactose solution were reacted with the immobilized enzyme(250 units/g) of lactose were 51% and 43%, respectively.

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Isolation and Characterization of Acid Protease Produced by Staphylococcus sp. CB2-3 from Digestive Organ of Harmonia axyridis (무당벌레 소화기관으로부터 산성 단백질 분해효소를 생산하는 Staphylococcus sp. CB2-3의 분리 및 특성)

  • Kim, Se-Jong;Whang, Kyung-Sook
    • Korean Journal of Microbiology
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    • v.47 no.3
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    • pp.255-262
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    • 2011
  • Six protein-degrading bacteria were isolated from digestive organ of Harmonia axyridis. These isolates were categorized as Staphylococcus sciuri subsp. sciuri (3 strains), Bacillus subtilis (1 strain), and Bacillus thuringiensis (2 strains) by 16S rRNA gene sequence analysis. The Staphylococcus sp. CB2-3 was selected as a protease-producing bacterium which showed the highest protease activity of 58.5 U/ml at the pH 5.0 medium. The optimal pH and temperature of protease activity were pH 5.0 and $40^{\circ}C$, respectively. This acid protease had a relatively high stability of 80% between $30-50^{\circ}C$ at broad temperature range. The opimal medium compositions of carbon, nitrogen and mineral source for cell growth and protease activity were investigated. When sorbitol (0.5%) was used as carbon source, enzyme activity was increased about 2 times than that of the basal medium. When skim milk (0.5%) was used as nitrogen source, activity was increased about 2.5 times than that of the control. Cell growth and enzyme activity were increased by mineral source such as KCl, $K_2HPO_4$, $FeSO_4$, but was completely inhibited by divalent ions such as $Co^{2+}$, $Zn^{2+}$, $Mn^{2+}$, $Cu^{2+}$.

Preparation of Cheese-like Product Using Soybean Milk (대두유(大豆乳)를 이용(利用)한 치즈 유사제품(類似製品)의 제조(製造)에 관한 연구(硏究))

  • Yu, Ju-Hyun;Shin, Won-Cheol;Pyun, Yu-Ryang;Yang, Ryung
    • Korean Journal of Food Science and Technology
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    • v.10 no.2
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    • pp.231-236
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    • 1978
  • It has been investigated that preparation of cheese-like product from defatted soybean milk and changes during 6 weeks' ripening. Obtained results were as follows: 1. Defatted soybean milk was fermented at $37^{\circ}C$ for 4 hours with Streptococcus lactis YUFE L-4 without addition of any other carbon sources. 2. Optimum concentration of coagulant such as $MgCl_2{\cdot}6H_2O$ and $CaCl_2$ were 0.0125M and 0.0375M, respectively. 3. Coagulating time for 30 minutes was sufficient to make curd. 4. Optimal reaction temperature for coagulating were $50^{\circ}C$. 5. After 6 weeks' ripening, moisture content was approximately $62{\sim}63%$. Water and 10%-TCA soluble nitrogen contents of soybean cheese with Asp. saitoi protease were higher than those of Mucor rennet. Water soluble nitrogen content of Asp. saitoi protease cheese was 50.5% and 10%-TCA soluble nitrogen was 27.5%.

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Nutritional Value of Dried Paddy Grasshopper, Oxya chinensis formosana (벼메뚜기 단백질(蛋白質)의 영양가(營養價)에 관한 연구)

  • Kim, Tae-Soo;Lee, Jong-Ho;Choi, Byeong-Dae;Ryu, Hong-Soo
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.16 no.2
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    • pp.98-104
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    • 1987
  • Studies were carried out to determined the optimal conditions of processing and changes in trypsin indigestible substrate(TIS) and in vitro protein digestibility of paddy grasshopper(Oxya chinensis formosana) under various drying conditions. The multienzyme assy and amino acid compositions were used to predict the quality changes of dried products. The in vitro protein digestidility of defatted products were higher than that of sun and hot air dried products. This results indicated that heat processing is decreased the digestibility, but is increased the TIS contents of dried samples. Amino acid composition of the products was comparable to the ANRC casein scoring pattern. The protein was espeoially low in the amount of lysine, tryptophan and methionine, but high in the quantity of aspartic acid, glutamic acid and arginine indicating that it could be a difference of the dry processing. C-PER and DC-PER were 2.65 and 2.44, respectively, in the defatted and freeze dried products and 2.49 and 2.30, respectively, in hot air dried products. From the these results, it could be confirmed that defatted and freeze dried products might be utilized with feed or foodstuff, unless the toxic substances were no longer detectable.

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Angiotensin Converting Enzyme Inhibitory Activity in Enzymatic Hydrolysates of Anchovy Muscle Protein (멸치육 효소 가수분해물의 Angiotensin 전환효소 저해작용)

  • LEE Tae-Gee;PARK Young-Beom;PARK Douck-Choun;YEUM Dong-Min;KIM In-Soo;GU Yeun-Suk;PARK Young-Ho;KIM Seon-Bong
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.31 no.6
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    • pp.875-881
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    • 1998
  • To develop functional food material with angiotensin converting enzyme (ACE) inhibitory peptides, muscle protein of anchovy, Engraulis japonica was hydrolyzed during 48 hrs by digestive pretenses such as pepsin, trypsin, $\alpha$-chymotrypsin, and commercial proteases such as papain, bromelain, complex enzyme, Elavourzyme, Novozym, Neutrase, Protamex and Alcalase. The only $50\%$ ethanol soluble hydrolysates were tested for inhibitory activity against ACE and yield of $50\%$ ethanol soluble peptide-nitrogen ($ESPN_{50}$). ACE inhibition effects and yield of $ESPN_{50}$ occurred as hydrolysis time increased to 8 hrs, Among those pretenses tested, hydrolysates by Alcalase and $\alpha$-chymohypsin had greater ACE inhibitory activity (80 and $74\%$, reipectively) with eletated levels of $ESPN_{50}$ (48 and 58 mg/ml, respectively), while Protamex hydrolysates had greater ACE inhibitory activities ($73\%$) with reduced levels of $ESPN_{50}$ (7.2mg/ml) than others. Amino acid compositions of $50\%$ ethanol solubles obtained from those hydrolysates were rich in glutamic acid, aspartic acid, cysteine and leucine.

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