• Title/Summary/Keyword: Protected Protein

Search Result 260, Processing Time 0.03 seconds

Effects of Dietary Heat Extruded Soybean Meal and Protected Fat Supplement on the Production, Blood and Ruminal Characteristics of Holstein Cows

  • Chen, Kuen-Jaw;Jan, Der-Fang;Chiou, Peter Wen-Shyg;Yang, Der-Wei
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.15 no.6
    • /
    • pp.821-827
    • /
    • 2002
  • The purpose of this study was to evaluate the effect of protected fat and heat-extruded soybean meal on the lactation performance of Holstein cows. Twenty-four cows, consisting of 20 lactating cows and 4 rumen-fistulated dry cows, were randomly allocated into four groups with 5 lactating cows and 1 fistulated cow in each group. A replicated 4${\times}$4 Latin square design with four 21 day periods, including 14 days of adaptation and 7 collection days within each period was employed. The experiment was a 2${\times}$2 arrangement, with or without heat-extruded soybean meal and protected fat inclusion. The dietary treatments consisted of supplements of (a) soybean meal (the control), (b) heat-extruded soybean meal, (c) protected fat, and (d) heat-extruded soybean meal and protected fat. The results showed that there were no significant differences in feed intake, milk yield, milk protein content, milk lactose content and body weight change between the dietary treatments. However, cows supplemented with protected fat showed a significantly increased (p<0.05) milk fat yield, 3.5% FCM and total solid yield. The increase in undegradable intake protein (UIP) via heat extruded soybean meal supplement significantly decreased the urea nitrogen concentration in the blood (p<0.05). Dietary fat inclusion significantly increased the blood cholesterol concentration (p<0.01) and decreased the ruminal pH value (p<0.01). Increased dietary UIP significantly decreased the ammonia nitrogen concentration in the rumen (p<0.01), but did not significantly influence the pH and VFA molar percentage in the rumen. It appears that dietary protected fat inclusion could improve milk fat and solid content. Increased dietary undegradable intake protein through heat extruded soybean meal did not improve milk yield. But it could alleviate the adverse effect of decreased milk protein due to dietary fat supplementation. Increased UIP could also decrease the ammonia nitrogen concentration in the rumen and plasma urea nitrogen concentration in the blood.

Lactation Performance of German Fawn Goat in Relation to Feeding Level and Dietary Protein Protection

  • Chowdhury, S.A.;Rexroth, H.;Kijora, C.;Peters, K.J.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.15 no.2
    • /
    • pp.222-237
    • /
    • 2002
  • Effects of high and low levels of feeding with or without protected protein on the performance of lactating goats were studied. Twenty four German Fawn goats either from 1st ($43.37{\pm}3.937$ kg and 2 year old) or 3rd $62.64{\pm}6.783$ kg and 4-5 year old) parity were used for the trial. Feeding levels were 7.2 (I) and 5.2 (II) MJ ME/litre of milk of 3.5% fat in addition to that of the maintenance allowance. At each feeding level, diet had either unprotected (U) or formaldehyde protected (P) soya-meal. Thus, four diets were IU, IP, IIU and IIP, having six animals in each. The diets were composed of hay and pellet (10:4:1 of beet pulp : barley : soya-meal). Effect of feeding level, protein protection, parity, health status and kid number on intake, milk yield, milk composition, growth rate of goats were recorded across the 21 weeks of study. High feeding level resulted increase (p<0.001) in estimated metabolizable energy (ME) and metabolizable protein (MP) availability. Dietary inclusion of protected soya-meal increased (p<0.001) the estimated MP but not the ME availability. Animals in 1st parity ate more (p<0.001) DM (111 vs. 102 g/kg $W^{0.75}$/d) than those in 3rd parity. Animals with twin kids (110 g/kg $W^{0.75}$/d) had higher (p<0.001) DM intake than those with single kid (102 g/kg $W^{0.75}$/d). Fat (4%) corrected milk (FCM) yield was not effected by high (1,924 g/d) or low (1,927 g/d) feeding level but increased (p<0.001) with protected (2,166 g/d) compared with unprotected (1,703 g/d) soya-meal. FCM yield for four dietary combinations were 1,806, 2,078, 1,600 and 2,254 g/d for diets IU, IP, IIU and IIP, respectively. For unit increase (g) in estimated MP availability relative to ME (MJ) intake, FCM yield increased ($1,418{\pm}275.6$) g daily ($r^2$=0.58; p<0.001). Milk fat (3.14 vs. 3.54%; p<0.001) and protein (2.94 vs. 3.04% p<0.05) contents were lower at high than the low feeding level. Protected protein increased (p<0.001) the fat, lactose and net energy (NE) content of milk. Milk urea concentration of 175, 183, 192 and 204 mg/l for diets IU, IP, IIU and IIP, respectively indicated lower RDP content of these diets. The RDP contents were 6.97, 6.70, 7.30 and 6.83 g/MJ of ME for diets IU, IP, IIU and IIP, respectively. Live weight change over the experimental period were 41, 6, 17 and 19 g/d. Absence of any positive response of high feeding was probably due to inefficient rumen fermentation resulting from inadequate RDP supply. Protected protein improved production performance apparently by increasing MP:ME ratio in the absorbed nutrient.

Effect of protected Methionine and Lysine on Milk yield and Composition in Holstein Dairy Cow under Different Dietary Crude Protein Levels : Meta-analysis (사료 내 수준별 조단백질 조건에서 보호메티오닌과 보호라이신의 사료첨가 급여가 착유우유생산성 및 유성분에 미치는 영향 : 메타분석)

  • Choi, Nag-Jin
    • Korean Journal of Organic Agriculture
    • /
    • v.24 no.4
    • /
    • pp.957-967
    • /
    • 2016
  • The present study was conducted to investigate effect of dietary protected amino acid on milk yield and composition in dairy cow using meta-analysis. Total 21 research papers were employed in analysis, and mixed model was used for the analysis of effects. Effect of protected methionine (PM) and combination of protected methionine and lysine (PML) were investigated under two different levels of dietary crude protein (CP, <18% and >18%). For performance of dairy cow, milk yield, milk composition including milk fat and protein content and yield and 4% FCM (fat corrected milk) production were used for analysis. In case of milk yield, a trend of increment was found at PM supplementation at low CP (P=0.055). However, the effect of PM at high CP was detected as not significant (P>0.05). In case of milk protein, inclusion of PM at low CP showed significant decrement (P<0.05). However, there was no significant effect of MP on milk protein at high CP (P>0.05). Supplementation of MP at high CP level showed significant increment of milk fat (P<0.05). MP supplementation represented significant increment of 4% FCM production (P<0.05) regardless of dietary CP levels. Effects of PML on milk yield and composition at both of low and high dietary CP were not significant in this study. However, it seem to be that there was a possible positive effect of MPL application at high dietary CP on performance of dairy cow.

WHOLE-BODY PROTEIN TURNOVER IN GOATS ENHANCED BY SUPPLEMENTING A DIET WITH RUMEN PROTECTED METHIONINE

  • Muramatsu, T.;Hatano, T.;Ueda, Y.;Furuse, M.;Okumura, J.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.7 no.2
    • /
    • pp.279-288
    • /
    • 1994
  • Three experiments were conducted with female Japanese Saanen goats to investigate the effects of rumen protected methionine (RPMet) on N utilization and whole-body protein turnover. Whole-body leucine flux from which whole-body protein turnover rates were derived was measured by primed- continuous infusion of L-[$^{15}N$] leucine in combination with gas chromatography-mass spectrometry. Throughout the experiments RPMet was added to a diet to supply 1.5 g DL-methionine per goat per day. Irrespective of the major N sources (i.e., protein or urea) in the diet, both N deposition and whole-body protein synthesis were increased (p<0.05), and urinary N excretion was decreased (p<0.05) by supplementing with RPMet, but not by supplementing with methionine. It was concluded, therefore, that under the present experimental conditions, the RPMet supplement was efficiently bypassed to result in enhanced body protein synthesis of the goat.

Protected (bypass) Protein and Feed Value of Hazelnut Kernel Oil Meal

  • Saricicek, B.Z.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.13 no.3
    • /
    • pp.317-322
    • /
    • 2000
  • In situ and in vivo digestion trials were conducted to determine the degradation of dry matter (DM), crude protein (CP) and effective protein degtadability (EPD), and digestibility of nutrients of Hazelnut kernel oil meal (HKOM), and effects of HKOM on nitrogen (N) balance. In the in situ study, nylon bag were suspended in the rumen of 3 Karayaka rams to estimate protected protein. Protein sources were analyzed for pepsin soluble protein (PSP) using a Pepsin Digestion Method. In the digestion trials, 4 Karayaka rams (36 mo.) were used in a $4{\times}4$ Latin square to evaluate the digestibility of nutrients and N retention to measure effects of diets containing HKOM, soybean meal (SBM) corn gluten meal (CGM) and urea (U). The degradability of DM and CP, and PSP content of HKOM were lower (p>0.05) than that of SBM, but higher (p<0.001) than that of CGM. EPD of HKOM was higher (p<0.01) than that of SBM or CGM. The apparent digestion coefficients of organic matter and CP for HKOM were lower than for SBM, but higher than for CGM. N retention of HKOM was higher than that of SBM and lower than that of CGM (p>0.05). In conclusion, these data may indicate that the HKOM is a high digestible feed source with a value between SBM and CGM.

Chemical Modification Studies of Yeast Farnesyl Protein Transferase

  • Sohn, Seung-Wan;Jun, Gyo;Yang, Chul-Hak
    • BMB Reports
    • /
    • v.30 no.4
    • /
    • pp.280-284
    • /
    • 1997
  • Phenylglyoxal diethyl pyrocarbonate (DEPC), and 1-cyclohexyl-3-[2-morpholinoethyl]-carbodiimide metho-p-toluenesulfonate (CMC) are modifying reagents specific for arginine, histidine, and aspartate or glutamate, respectively. They were found to inactivate S. cerevisiae farnesyl protein transferase (FPTase). The peptide substrate protected the enzyme against inactivation by CMC and the other substrate farnesyl pyrophosphate showed protection against inactivation by phenylglyoxal. while neither of the two substrates protected the enzyme against DEPC inactivation. These results suggest the presence of aspartate/glutamate, arginine and histidine residues at the active site of this enzyme.

  • PDF

Effects of Foliar Application of Glycine Betaine on the Growth and Contents of Osmolyte in Tomato Seedling (Glycine betaine 엽면 처리가 토마토 유묘의 생육과 삼투조절물질 함량에 미치는 영향)

  • Kang, Nam-Jun;Kwon, Joon-Kook;Lee, Jae-Han;Park, Jin-Myeon;Rhee, Han-Chul;Choi, Young-Hah
    • Journal of Bio-Environment Control
    • /
    • v.15 no.4
    • /
    • pp.390-395
    • /
    • 2006
  • Effects of exogenously foliar applied glycine betaine (GB) on the growth and contents of osmolyte in tomato seedling was investigated. Plants treated with exogenous glycine betaine induced better biomass production and plant height during chilling stress than the untreated plants. The total soluble sugar contents in GB foliar-applied plants lower than that of untreated plants 28 days after foliar application. Total water soluble protein contents in GB foliar-applied plants did not change 28 days after chilling stress. In untreated plant, it decreased rapidly in the beginning of chilling stress. Proline contents in untreated plants rapidly increased by the beginning of chilling stress, and then slightly decreased during the next 3 weeks. However proline contents in GB foliar-applied plants did not change during the 28 days chilling stress period. The results suggest that foliar application of GB is a effect methods to increase the chilling tolerance of tomato seedlings in protected cultivation system at low temperature season.

The Mitochondrial Tricarboxylate Carrier of Silver Eel: Chemical Modification by Sulfhydryl Reagents

  • Capobianco, Loredana;Impagnatiello, Tecla;Ferramosca, Alessandra;Zara, Vincenzo
    • BMB Reports
    • /
    • v.37 no.5
    • /
    • pp.515-521
    • /
    • 2004
  • The tricarboxylate (or citrate) carrier was purified from eel liver mitochondria and functionally reconstituted into liposomes. Incubation of the proteoliposomes with various sulfhydryl reagents led to inhibition of the reconstituted citrate transport activity. Preincubation of the proteoliposomes with reversible SH reagents, such as mercurials and methanethiosulfonates, protected the eel liver tricarboxylate carrier against inactivation by the irreversible reagent N-(1-pyrenyl)maleimide (PM). Citrate and L-malate, two substrates of the tricarboxylate carrier, protected the protein against inactivation by sulfhydryl reagents and decreased the fluorescent PM bound to the purified protein. These results suggest that the eel liver tricarboxylate carrier requires a single population of free cysteine(s) in order to manifest catalytic activity. The reactive cysteine(s) is most probably located at or near the substrate binding site of the carrier protein.

Chemical Modification of Yeast Farnesyl Protein Transferase Expressed in E. coli

  • Kim, Hyun-Kyung;Yang, Chul-Hak
    • Bulletin of the Korean Chemical Society
    • /
    • v.27 no.4
    • /
    • pp.529-534
    • /
    • 2006
  • Chemical modification of the S. cerevisiae farnesyl protein transferase (FPT) with CMC, phenylglyoxal and DEPC resulted in enzyme inactivation, depending upon the reagent concentration. The peptide substrate GST-PEP-I, a GST-fused undecapeptide mimicking the C-terminus of $p21^{Ki-ras}$, protected the enzyme against inactivation by CMC which is specific to either aspartate or glutamate, while the other substrate farnesyl pyrophosphate (FPP) showed protection against phenylglyoxal which is the specific modifier of arginine residues, dependent on the substrate concentrations. Neither of the two substrates protected the enzyme against histidine inactivation by DEPC. It is suggested that there is at least one aspartate or glutamate residue at the peptide substrate binding site, and that at least one arginine residue is located at the binding site of FPP. There also seems to be at least one histidine residue which is critical for enzymic activity and is exposed toward the bulk solution, excluded from the substrate binding sites.