• Title/Summary/Keyword: protein fraction

Search Result 1,169, Processing Time 0.042 seconds

In situ ruminal degradation characteristics of dry matter and crude protein from dried corn, high-protein corn, and wheat distillers grains

  • Lee, Y.H.;Ahmadi, F.;Choi, D.Y.;Kwak, W.S.
    • Journal of Animal Science and Technology
    • /
    • v.58 no.9
    • /
    • pp.33.1-33.7
    • /
    • 2016
  • Background: The continuing growth of the ethanol industry has generated large amounts of various distillers grains co-products. These are characterized by a wide variation in chemical composition and ruminal degradability. Therefore, their precise formulation in the ruminant diet requires the systematic evaluation of their degradation profiles in the rumen. Methods: Three distillers grains plus soluble co-products (DDGS) namely, corn DDGS, high-protein corn DDGS (HP-DDGS), and wheat DDGS, were subjected to an in situ trial to determine the degradation kinetics of the dry matter (DM) and crude protein (CP). Soybean meal (SBM), a feed with highly degradable protein in the rumen, was included as the fourth feed. The four feeds were incubated in duplicate at each time point in the rumen of three ruminally cannulated Hanwoo cattle for 1, 2, 4, 6, 8, 12, 24, and 48 h. Results: Wheat DDGS had the highest filterable and soluble A fraction of its DM (37.2 %), but the lowest degradable B (49.5 %; P < 0.001) and an undegradable C fraction (13.3 %; P < 0.001). The filterable and soluble A fraction of CP was greatest with wheat DDGS, intermediate with corn DDGS, and lowest with HP-DDGS and SBM; however, the undegradable C fraction of CP was the greatest with HP-DDGS (41.2 %), intermediate with corn DDGS (2.7 %), and lowest with wheat DDGS and SMB (average 4.3 %). The degradation rate of degradable B fraction ($%\;h^{-1}$) was ranked from highest to lowest as follows for 1) DM: SBM (13.3), wheat DDGS (9.1), and corn DDGS and HP-DDGS (average 5.2); 2) CP: SBM (17.6), wheat DDGS (11.6), and corn DDGS and HP-DDGS (average 4.4). The in situ effective degradability of CP, assuming a passage rate of $0.06h^{-1}$, was the highest (P < 0.001) for SBM (73.9 %) and wheat DDGS (71.2 %), intermediate for corn DDGS (42.5 %), and the lowest for HP-DDGS (28.6 %), which suggests that corn DDGS and HP-DDGS are a good source of undegraded intake protein for ruminants. Conclusions: This study provided a comparative estimate of ruminal DM and CP degradation characteristics for three DDGS co-products and SBM, which might be useful for their inclusion in the diet according to the ruminally undegraded to degraded intake protein ratio.

Determination of Optimal Conditions of Pressure Toasting on Legume Seeds for Dairy Deed Industry : I. Effects of Pressure Toasting on Nutritive Values of Lupinus albus in Lactating Dairy Cows

  • Yu, P.;Goelema, J.O.;Tamminga, S.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.12 no.8
    • /
    • pp.1205-1214
    • /
    • 1999
  • Whole lupinus albus seeds were pressure toasted at temperatures of 100, 118 and $136^{\circ}C$ for 3, 7, 15 and 30 min to study rumen degradation and post-rumen digestion and to determine optimal heating conditions for the Dutch dairy feed industry. In sacco nylon bag and mobile bag techniques were employed for rumen and intestine incubations to determine ruminal degradation characteristics and intestinal digestion of crude protein (CP) in 4 lactation rumen cannulated and 4 lactating intestinal cannulated Dutch dairy cows fed 47% hay and 53% concentrate according to Dutch dairy requirements. Measured rumen degradation characteristics were soluble fraction (S), undegradable fraction (U), potentially degradable fraction (D), lag time (T0) and rate of degradation (Kd) of insoluble but degradable fraction. Percentage bypass feed protein (BCP), ruminal microbial protein synthesized based on available nitrogen (N_MP) and that based on available energy (E_MP), true protein supplied to the small intestine (TPSI), truly absorbed BCP (ABCP), absorbed microbial protein (AVP) in the small intestine, endogenous protein losses in the digestion (ENDP), true digested protein in the small intestine (TAP or DVE in Dutch) and degraded protein balance (PDB or OEB in Dutch) were totally evaluated using the new Dutch DVE/OEB System. Pressure toasting decreased (p<0.001) rumen degradability of CP. It reduced S (p<0.05) and Kd (p=0.06), increased D (p<0.05) and U (p<0.01) but did not alter T0 (p>0.05), thus resulting in dramatically increased BCP (p<0.001) with increasing time and temperature from 73.7 (raw) up to 182.5 g/kg DM ($136^{\circ}C/15min$). Although rumen microbial protein synthesized based on available energy (E_MP) was reduced, true protein (microbial and bypass feed protein) supplied to the small intestine (TPSI) was increased (p<0.001) from 153.1 (raw) to 247.6 g/kg DM ($136^{\circ}C/15min$). Due to digestibility of BCP in the intestine not changing (p>0.05) average 87.8%, the absorbed BCP increased (p<0.001) from 62.3 (raw) to 153.7 g/kg DM ($136^{\circ}C/15min$). Therefore DVE value of true digested protein in the small intestine was significantly increased (p<0.001) from 118.9 (raw) to 197.0 g/kg DM ($136^{\circ}C/15min$) and OEB value of degraded protein balance was significantly reduced (p<0.001) from 147.2 (raw) to 63.1 g/kg DM ($136^{\circ}C/15min$). It was concluded that pressure toasting was effective in shifting degradation of CP of lupinus albus from the rumen to small intestine without changing intestinal digestion. Further studies are required on the degradation and digestion of individual amino acids and on the damaging effects of processing on amino acids, especially the first limiting amino acids.

Detection of Anticancer Activity from the Root of Angelica gigas In Vitro

  • Ahn, Kyung-Seop;Sim, Woong-Seop;Kim, Ik-Hwan
    • Journal of Microbiology and Biotechnology
    • /
    • v.5 no.2
    • /
    • pp.105-109
    • /
    • 1995
  • Anticancer activity of a fraction of the ethanol extract from the root of Korean angelica (Angelica gigas Nakai) was recognized in human cancer cell lines HeLa $S_3$, K-562, and Hep $G_2$. The extract blocked the phorbol ester-inducing megakaryocytic differentiation of K-562 cells, which indicated the modification of protein kinase C (PKC) activity. In vitro assay showed the activation of PKC by the extract. An effective fraction of the Angelica gigas extract, of which $R_f$ value was 0.64 in a thin layer chromatography, was a different component from those of European angelicas. The $ED_50$ value of the fraction was 8, 9, and $16\;\mu\textrm{m}/ml$ against HeLa $S_3\;Hep\;G_2$, and K-562 cells, respectively, while the fraction showed higher $ED_50$ values against normal cell lines.

  • PDF

Radial Distribution Proximate Composition and Minerals within Naked Barley Kernel (쌀보리 입자내의 일반성분 및 무기질의 분포)

  • Park, Sung-Hee;Kim, Kwan;Kim, Sung-Kon;Park, Yang-Kyun
    • Applied Biological Chemistry
    • /
    • v.32 no.4
    • /
    • pp.441-443
    • /
    • 1989
  • The major kernels$(7{\sim}10\;mesh)$ of naked barley were pearled to give an average yield for each pearling of about 5% flour, with 70% of the naked barley left as residual kernel. The contents of protein, fat and ash were in the highest in the fraction of 1,2 and 3, respectively. These fractions contained 1, 4 times of protein, 3.16 times of fat and 3.08 times of ash more than those values of original kernel. Residual kernels contained 62% of protein, 38% of fat and 35% of ash in the original kernel. Among minerals, the content of Ca, Na, Fe and Mn were in the highest in fraction 1 ; P, Mg and Zn in fraction 2 ; and K and Cu in fraction 3. Concentrations of these minerals were the lowest in the residual kernel. Magnesium showed the deepest concentration gradient, while iron was evenly distributed within the kernel.

  • PDF

Nutriproteomics: Identifying the Molecular Targets of Nutritive and Non-nutritive Components of the Diet

  • Barnes, Stephen;Kim, Helen
    • BMB Reports
    • /
    • v.37 no.1
    • /
    • pp.59-74
    • /
    • 2004
  • The study of whole patterns of changes in protein expression and their modifications, or proteomics, presents both technological advances as well as formidable challenges to biological researchers. Nutrition research and the food sciences in general will be strongly influenced by the new knowledge generated by the proteomics approach. This review examines the different aspects of proteomics technologies, while emphasizing the value of consideration of "traditional" aspects of protein separation. These include the choice of the cell, the subcellular fraction, and the isolation and purification of the relevant protein fraction (if known) by protein chromatographic procedures. Qualitative and quantitative analyses of proteins and their peptides formed by proteolytic hydrolysis have been substantially enhanced by the development of mass spectrometry technologies in combination with nanoscale fluidics analysis. These are described, as are the pros and cons of each method in current use.

Physiological Activities of Different Molecular Weight Fractions of Crude Polysaccharides from Dŏdŏk (Codonopsis lanceolata)

  • Kim, Dong-Soo;Kim, Byoung-Mok;Lee, Myung-Ki
    • Preventive Nutrition and Food Science
    • /
    • v.11 no.4
    • /
    • pp.261-267
    • /
    • 2006
  • This study investigated the physiological activities of different molecular weight (MW) fractions of crude polysaccharide from $D\check{o}d\check{o}k$ (Codonopsis lanceolata). The crude polysaccharide cut off for each fraction was: <1,000 MW (Fr I), 1,000 MW

Studies on Constituents of Higher Fungi of Korea(XXXV) -Antitumor Components Extracted from the Carpophores and Cultured Mycelia of Laccaria laccata- (한국산(韓國産) 고등(高等) 균류(菌類)의 성분(成分) 연구(硏究)(제(第)35보(報)) -애기졸각버섯의 항암(抗癌) 성분(成分)-)

  • Kim, Sook-Hee;Woo, Myoung-Sik;Kim, Byong-Kak
    • The Korean Journal of Mycology
    • /
    • v.10 no.4
    • /
    • pp.155-163
    • /
    • 1982
  • To find antitumor components, a protein-bound polysaccharide fraction was obtained by extracting with hot water and precipitating with ethanol from the carpophores and the cultured mycelia of Laccaria laccata. The fraction was examined for antitumor activity against sarcoma 180 implanted in mice. The component extracted from the carpophores showed 75% and 65% tumor inhibition ratios in the doses of 20 mg and 50 mg/kg/day, respectively. The protein bound polysaccharide fraction of the cultured mycelia of L. laccata also showed 57.8% tumor inhibition ratio in the dose of 20 mg/kg/day. The chemical analysis of the protein-bound polysaccharide fraction showed that it contained a polysaccharide and a protein. The hydrolysates of the polysaccharide moiety contained six and one unknown monosaccharides. Fourteen amino acids were identified in the hydrolysates of the protein moiety.

  • PDF

Studies on nucleic acid and protein biosyntheses of Chlorella cells during the course of the chloroplast development (클로렐라의 엽록체 발생과정에 있어서의 핵산 및 단백질의 생합성에 관한 연구)

  • 이영녹;이종삼
    • Korean Journal of Microbiology
    • /
    • v.8 no.1
    • /
    • pp.1-12
    • /
    • 1970
  • Nucleic acid and protein biosynthese of the glucose-bleached Chlorella cells in relation to the process of the chloroplast reformation were traced, by measuring the changes in the amounts of cell constituents and nuclease activities of the cells during the greening process. The contents of RNA and protein of the glucose-bleached cells decreased significantly, shile the contents of nucleotides and amino acids of the cells increased to compared with those of the control, showing that the biosynthetic activities of RNA and protein of the cells were inhibited severely in the glucose-bleaching process. In the early greening process of the glucose-bleached Chlorella cells the contents of RNA and protein of the cells increased significantly, while the contents of nucleotides nad amino acids of the cells increased to compared with those of the control, showing that the biosynthetic activities of RNA and protein of the cells were inhibited severely in the glucose-bleaching process. In the early greening process of the glucose-bleached Chlorella cells the contents of RNA and protein of the cells increased significantly wihout any increase in the chlorophyll contents showing that the massive biosynthese of RNA and protein proceed prior to the chlorophyll bioynthesis in the cells. The phosphate contents in the DNA fraction of the glucose-bleached cells decreased, but the contents of acid-insoluble polyphosphate increased to compared with those of the control in the early greening porcess, exhibiting that the incorporation of the phosphorus from acid-insoluble polyphosphate into DNA was retarded. In the greening process of the glucose-bleached cells the ribonuclease nad deoxyribonuclease activities of the cells decreased to compared with those of the control, although the initial activities of the both enzymes in the cell were far great compared with the control. Although the initial phosphate contents in the lipid fraction of the glucose-bleached Chlorella cells were more great than the control, the phosphate contents in the lipid fraction of the cells decreased in the early greening process to compared with control, and then increased in the late developmental stages in which massive chlorophyll biosynthesis occured.

  • PDF

Studies on the Biochemical Nature of the Protein Constituents of Panax Ginseng Root (인삼(人蔘) 단백성분의 생화학적성질(生化學的性質)에 관한 연구)

  • Kim, Young-Choong;Chung, Bo-Sup;Lee, Kang-No;Koo, Hyang-Ja;Ahn, Sang-Mee;Huh, Hoon
    • Journal of Nutrition and Health
    • /
    • v.16 no.2
    • /
    • pp.115-124
    • /
    • 1983
  • The biochemical nature of the protein constituents of six year old fresh Panax ginseng root was studied. Total protein constituents were extracted with phosphate buffer of pH 7.4, ionic strength of 0.1 and fractionated by ultrafiltration using four different membranes which cut down the materials of molecular weight of 500, 1,000, 5,000 and 10,000, respectively. Each fraction was subjected to ion exchange chromatography using DEAE - cellulose to isolate component proteins. The protein fraction larger than molecular weight of 10,000 was refractionated by the method of ammonium sulfate precipitation. The electrophoresis of the refractionated protein constituents was performed. The amino acid composition of the protein constituents was determined by gas- liquid chromatography. From the results, it could be summarized that eleven different protein constituents smaller than molecular weight of 10,000 were isolated from the fresh Panax ginseng root. At least eleven different protein constituents larger than molecular weight of 10,000 were identified from the electrophoretic patterns. These protein costituents seem to be compounded of all or some of five different subunits.

  • PDF

Protein Binding of Disopyramide -Displacement by Mono-N-Dealkyl-Disopyramide and Variation with Commerial Source of Alpha-1-Acid Glycoprotein-

  • Haughey, David B.;Steinberg, Irving;Lee, Min-Hwa
    • Journal of Pharmaceutical Investigation
    • /
    • v.15 no.1
    • /
    • pp.1-7
    • /
    • 1985
  • Previous studies show that the free (unbound) fraction of disopyramide in human serum is drug concentration dependent~ at corresponding serum disopyramide concentrations that are achieved clinically. $^1^{\sim}^3^)\;Moreover$, disopyramide free fraction values vary several fold at any given drug concentration in human serum and tend to decrease as serum cocentrations of alpha-I-acid glycoprotein(AAG) incrase.$^4^)$ A recent $study^5^)$ demonstrates that the free fraction of disopyramide inhuman serum increases almost 2-fold following the addition of $14.4{\mu}M/L$ mono-N-dealkyldisopyramide. These studies and others. $^6^),\;^7^)$ prompted the present investigation to characterize the protein binding of disopyramide in human serum and solutions of AAG in the presence of mono-N-dealkyldisopyramide (a major metabolite of, disopyramide) and to determine the utility of using commercially available alpha-I-acid glycoprotein for drug protein binding displacement studies. Because many basic and acidic compounds are known to bind to alpha-I-acid $glycoprotein^8^)$ the present study. was performed to determine whteher commercially available AAG would provide a convenient protein source for such binding studies.

  • PDF