• Title/Summary/Keyword: protein solubility

Search Result 502, Processing Time 0.023 seconds

Changes in Physicochemical Properties of Rice Extrudate Due to Added Isolated Soy Protein (분리대두단백 첨가에 의한 쌀 압출성형물의 물리화학적 특성 변화)

  • Lee, Chan
    • The Korean Journal of Food And Nutrition
    • /
    • v.23 no.1
    • /
    • pp.114-117
    • /
    • 2010
  • The effects of isolated soy protein(ISP) content on the physicochemical properties of extrudates from rice flour produced by a single-screw extruder were evaluated. The integrity index(II), nitrogen solubility index(NSI), rehydration ratio(RR), and density were measured as indices of the changes of physicochemical properties of rice extrudates. Increased amounts of ISP resulted in increased II but decreased RR and density. There was no change in the NSI value. It was concluded that the addition of ISP to the raw material could be helpful in texturization of rice extrudate.

Marination and Physicochemical Characteristics of Vacuum-aged Duck Breast Meat

  • Khan, Muhammad Issa;Lee, Hyun Jung;Kim, Hyun-Joo;Young, Hae In;Lee, Haelim;Jo, Cheorun
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.29 no.11
    • /
    • pp.1639-1645
    • /
    • 2016
  • We investigated marinade absorption and physicochemical characteristics of vacuum-aged duck breasts that were halved and individually vacuum-packed for chiller aging at $4^{\circ}C$ for 14 d. One half was marinated for 0, 7, or 14 d, while the second half was used as a control. Marinade absorption, cooking loss, cooking yield, texture profile, pH, color, protein solubility, and thiobarbituric acid reactive substances (TBARS) values were evaluated, and protein sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed. Marinade absorption and pH did not vary significantly after 14 d of aging. Marination increased the pH, color ($a^*$ and $b^*$) values, and cooking yield and reduced cooking loss. TBARS values significantly increased with aging time, but were significantly reduced by marination. Myofibril and total protein solubility increased with aging and marination, while SDS-PAGE showed protein degradation. Hence, aging and marination can be used simultaneously to improve physicochemical quality and cooking yield of vacuum-aged duck breast.

Predicting In Sacco Rumen Degradation Kinetics of Raw and Dry Roasted Faba Beans (Vicia faba) and Lupin Seeds (Lupinus albus) by Laboratory Techniques

  • Yu, P.;Egan, A.R.;Leury, B.J.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.13 no.10
    • /
    • pp.1377-1387
    • /
    • 2000
  • Two laboratory techniques: (1) an in vitro method with two procedures for measuring protein degradabilities and (2) an in vitro method with three procedures for measuring protein solubility, were investigated to determine which laboratory techniques could most accurately predict the quantity of rumen protein degradation kinetics of legume seeds after dry roasting under various conditions, in terms of (1) rumen protein disappearance ($D_j$, where j=0, 2, 4, 8, 12, 24 and 48 h incubation), (2) rumen protein effective degradability (EDCP), (3) the parameters describing rumen degradation characteristics (the soluble fraction: S, the potentially degradable fraction: D, undegradable fraction: U, lag time: T0 and the degradation rate: Kd) and (4) rumen bypass protein (BCP), which were determined by the method accepted internationally at present, in sacco nylon bag technique using the standardized Dutch method. Feeds evaluated were the raw and dry roasted whole faba (Vicia faba) beans (WFB) and whole lupin (Lupinus albus) seeds (WLS), each was dry roasted under various conditions (at 110, 130 or $150^{\circ}C$ for 15, 30 or 45 min). In vitro protein degradability ($D_1$_Auf and $D_{24}$_Auf) were determined using the modified Aufr re method by enzymatic hydrolysis for 1 h and 24 h using a protease extracted from Streptomyces griseus in a borate-phosphate buffer. In vitro protein solubility ($bf_1$_S, $bf_2$_S, $bf_3$_S) was measured in a borate-phosphate buffer with three different procedures. Results from laboratory techniques (in vitro) were correlated and linearly regressed with in sacco results. Of the three procedures of in vitro protein solubility evaluated, none of them could predict in sacco results with good precision. The highest Pearson correlation coefficient ($R^2$) was less than 0.50. Of two procedures of in vitro protein degradability studied, the $D_1$_Auf values were closely correlated with in sacco parameters: Kd, EDCP and %BCP with high R' values: 0.82, 0.85 and 0.85, respectively, and closely correlated with in sacco $D_j$ at 2, 4, 8 and 12 h rumen incubation with high $R^2$ values: 0.83, 0.91, 0.93 and 0.83, respectively. The $D_{24}$_Auf values could not predict in sacco results. The highest $R^2$ value was less then 0.40. These results indicated that in vitro protein solubility measured in borate-phosphate failed to identify differences in the rate and extent of protein degradation of legume seeds after dry roasting under various conditions and thus should not be used to predict rumen degradation, particularly for heat processed feedstuffs. But in vitro protein degradability using the modified Aufr re method by enzymatic hydrolysis for 1 h or possibly an intermediate time (>1 h and <24 h) is a promising laboratory procedure to detect effectiveness of dry roasting legume seeds on rumen protein degradation characteristics and could be used as a simple laboratory method to predict the rate and extent of protein degradation in the rumen in sacco with high accuracy. The equations to predict EDCP, Kd and BCP of dry roasted legume seeds (WLS and WFB) under various conditions are as follow: For both: EDCP (%)=-1.37+1.06*$D_1$_Auf ($R^2=0.85$, p<0.01). For both: Kd (%/h)=-21.81+0.49*$D_1$_Auf ($R^2=0.82$, p<0.01). For both: %BCP=103.37-1.07*$D_1$_Auf ($R^2=0.85$, p<0.01).

Effect of NaCl, Phosphate and pH on the Functional Properties of a Mixed System of Pork Myofibrillar and Plasma Proteins (소금, 인산염, pH가 돼지 혈장단백질과 근원섬유단백질 혼합물의 기능적 특성에 미치는 영향)

  • Kim, Cheon-Jei;Han, Eui-Su
    • Korean Journal of Food Science and Technology
    • /
    • v.23 no.4
    • /
    • pp.428-432
    • /
    • 1991
  • This study was carried out to investigate the effect of NaCl, pH and phosphate on the functional properties of a mixed system of plasma protein and myofibrillar proteins. The solubility of plasma protein, myofibrillar protein and the mixture (plasma+myofibrillar protein) increased according to the increase of NaCl concentration ($0{\sim}4%$) and pH $pH4{\sim}8$). The solubility, emulsifying activity and capacity of the mixture were lower than those of plasma protein, whereas higher than those of myofibrillar protein. The gel strength of the mixture and myofibrillar protein showed a significant increase when NaCl concentration was increased from 2 to 3%. The gel strength of myofibrillar protein increased about four times when 0.3% polyphosphate added to the sample containing 2% NaCl, whereas the moisture loss of the mixture and myofibrillar protein decreased significantly. The gel strength of plasma protein, myofibrillar protein and the mixture increased slightly at $3{\sim}5%$ protein concentration, whereas the gel strength of those increased significantly as the protein concentration increased from 5 to 9%.

  • PDF

Effects of Phosphorylation and Acetylation on Functional Properties and Structure of Soy Protein (인산화와 초산화가 대두단백질의 기능특성과 구조에 미치는 영향)

  • Kim, Nam-Soo;Kwon, Dae-Young;Nam, Young-Jung
    • Korean Journal of Food Science and Technology
    • /
    • v.20 no.5
    • /
    • pp.625-630
    • /
    • 1988
  • Phosphorylation of soy protein by sodium trimetaphosphate and acetylation of soy protein by acetic anhydride were performed. Then, the functional properties of modified soy proteins were compared with that of unmodified soy protein. Isolated soy protein prepared from defatted soybean flake had protein content of 92.7% as moisture-free basis. The phosphorylated soy protein showed higher solubility, foaming properties, and water holding capacity than unmodified soy protein. Acetylation of soy protein increased emulsification activity and foaming properties greatly, whereas decreased the solubility at pH 8.0. Isoelectric pHs of phosphorylated and acetylated soy protein were shifted to acidic regions(pH 3.0 and pH 4.0) from pH 5.0, which was the isoelectric pH of unmodified soy protein. Soy protein seems to be aggregated during phosphorylation and acetylation procedure, judging form Sepharose CL-4B gel filtration profiles. The modified soy proteins showed increased mobilities to anode direction in disc-gel electrophoresis.

  • PDF

Economic Evaluation of Two Imported Soybean Meals and Two Dietary Protein Levels for Broilers (육계에 대한 두 종류의 수입대두박과 두 가지의 단백질 수준의 경제성 비교)

  • 박홍석;이봉덕
    • Korean Journal of Poultry Science
    • /
    • v.25 no.2
    • /
    • pp.91-98
    • /
    • 1998
  • In order to compare economics of soybean meals (SBMS) imported from Brazil and the U.S., a feeding trial was conducted with 480 commercial broiler chicks (Abor Acres strain) for 38 days. The Brazilian SBM was brownish in color and the protein solubility in 0.2 % KOH solution was 63. 4 %. The U.S. SBM, on the other hand, was a dehulled SBM, and uniform in color (light yellow) and particle size. The protein solubility value of the latter was 76.6 %. Two dietary protein levels (19 % and 21 %) were used for each source of SBM (2x2 factorial). Chicks fed diets containing the U.S. SBM grew significantly faster (P<0.05) and utilized feed more efficiently than chicks fed diets containing Brazilian SBM. Chicks fed diets containing 21 % CP showed better growth performance and profitability than those fed the 19 % CP diets. The price of the U.S. SBM was higher but the feed cost per unit gain was lower than the Brazilian SBM. Results suggest that there are over-cooked SBMs being traded on the Korean rnarket, and attention should be given to not only the price but also the quality of SBMs.

  • PDF

Preparation and Characterization of the Hydrolyzed Protein from Shaving Scraps of Leather Waste Containing Chromium by the Combination Treatment with Alkaline Inducing Agent and Alkaline Proteolytic Enzyme (Alkaline Inducing Agent 및 Alkaline Proteolytic Enzyme 혼용처리에 의한 Shaving Scraps 가수분해 단백질의 제조 및 특성)

  • Kim, Won-Ju;Cho, Ju-Sik;Lee, Hong-Jae;Heo, Jong-Soo
    • Journal of the Korea Organic Resources Recycling Association
    • /
    • v.6 no.1
    • /
    • pp.1-12
    • /
    • 1998
  • To examine the possibility of protein recycling of shaving scraps containing chromium generated from manufacturing process of leather, the optimum hydrolysis conditions and the withdrawal methods of low molecular weight protein for using the liquid fertilizer sources by investigation of solubilities of hydrolyzed protein, inorganic nutrients contents and molecular weight distributions of hydrolyzed protein from shaving scraps treated with mixed alkaline inducing agents and mixed alkaline proteolytic enzymes including MgO were investigated. In hydrolysis of shaving scraps treated with mixed alkaline inducing agents, the solubility of shaving scraps were clearly different with 65~85% according to the sorts of the inducing agents, and the degree of hydrolysis was high in the order of NaOH, $Ca(OH)_2$ and KOH. The average molecular weights of withdrawal hydrolyzed protein were 10, 40 and 80 KD treated with NaOH, $Ca(OH)_2$ and KOH, respectively. And the chromium contents was about 15 ppm. In hydrolysis of shaving scraps treated with mixed alkaline proteolytic enzymes, the bility of shaving scraps were high in the order of alcalase, esperase and savinase. In c of treating 0.5% alcalase, the low molecular weight of hydrolyzed protein could be withdrawn. The solubility of the hydrolyzed protein was about 85%, the average molecular weight of the protein was below 1 KD and chrome content of the protein was below 10 ppm.

  • PDF

Production of White Zein Using Aqueous Ethanol (물-에탄올 혼합액을 이용한 백색 제인의 생산)

  • Kim, Kang Sung
    • Korean journal of food and cookery science
    • /
    • v.29 no.6
    • /
    • pp.647-652
    • /
    • 2013
  • Solubility profiles of zein and carotenoid in aqueous ethanol were studied. Zein showed minimum turbidity at the aqueous ethanol concentration of 87-92%, indicating least aggregations between protein molecules. Solubilities of zein and carotenoid increased linearly with the content of yellow zein up to 20% in the aqueous ethanol range of 60-95% tested. At room temperature of $20^{\circ}C$, zein showed maximum solubility in broad ethanol concentration ranges of 60-95%, while that for carotenoid was somewhat narrower with ethanol concentration range of 85-95%. However, at incubation temperature of $-20^{\circ}C$, solubilities of both carotenoid and zein were lowered, with dramatic reduction being exhibited at aqueous ethanol concentration of 60% for both compounds, while substantial reduction in solubility was shown at 95% ethanol by zein only. Zein was practically insoluble in absolute ethanol, regardless of temperature range tested, while carotenoid remained largely soluble, though there was pronounced decrease in solubility at the subfreezing temperature.

Acetylation of Fist Protein form Alaska Pollack (명태 근육단백질의 아세틸화에 따른 기능성의 변화)

  • 홍정화;최진호;변대석
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.19 no.3
    • /
    • pp.219-223
    • /
    • 1990
  • Myofibrillar protein from Alaska pollack was modified with acetic anhydride at pH 7.5 and $25^{\circ}C$ and changes in functional properties as affected by the degree of modification were determined. Acetylation of myofibrillar protein resulted in protein with unique functional properties dependent upon the degree of acetylation. By selecting appropriate degree of modification it was possible to control protein solubility heat coagulability calcium precipitability foaming and emulsion capa-city.

  • PDF

Technical Functional Properties of Water- and Salt-soluble Proteins Extracted from Edible Insects

  • Kim, Tae-Kyung;Yong, Hae In;Jeong, Chang Hee;Han, Sung Gu;Kim, Young-Boong;Paik, Hyun-Dong;Choi, Yun-Sang
    • Food Science of Animal Resources
    • /
    • v.39 no.4
    • /
    • pp.643-654
    • /
    • 2019
  • The amino acid composition, protein quality, and protein functionality of protein solution extracted from three edible insect species were investigated. We used 0.02% ascorbic acid and 0.58 M saline solution to extract water-soluble and salt-soluble proteins from the three insect species. Extracted protein solutions of Tenebrio molitor (TM), Allomyrina dichotoma (AD), and Protaetia brevitarsis seulensis (PB) were divided into six groups, according to species and solubility: WTM, WAD, WPB (water-soluble), and STM, SAD, and SPB (salt-soluble). Defatted TM had the highest protein content, but its protein solubility was the lowest, for both water and saline solutions. Amino acid composition differed by edible insect species and buffer type; SPB had the highest protein quality, followed by WPB. PB had a higher pH than the other species. Color values also differed among species. SPB had abundant high molecular weight proteins, compared with other treatments; and also had the highest foaming capacity, foam stability, and emulsifying capacity. In conclusion, PB is a good source of functional protein compared with the other studied species. Additionally, protein extraction using saline solution is promising as a useful method for improving edible insect protein functionality.