• Title/Summary/Keyword: Protein digestion

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The Role of Protozoa in Feed Digestion - Review -

  • Jouany, J.P.;Ushida, K.
    • Asian-Australasian Journal of Animal Sciences
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    • v.12 no.1
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    • pp.113-128
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    • 1999
  • Protozoa can represent as half of the total rumen microbial biomass. Around 10 genera are generally present on the same time in the rumen. Based on nutritional aspects they can be divided in large entodiniomorphs, small entodiniomorphs and isotrichs. Their feeding behaviour and their enzymatic activities differ considerably. Many comparisons between defaunated and refaunated animals were carried out during the last two decades to explain the global role of protozoa at the ruminal or animal levels. It is now generally considered that a presence of an abundant protozoal population in the rumen has a negative effect on the amino acid (AA) supply to ruminants and contribute to generate more methane but, nevertheless, protozoa must not be considered as parasites. They are useful for numerous reasons. They stabilise rumen pH when animal are fed diets rich in available starch and decrease the redox potential of rumen digesta. Because cellulolytic bacteria are very sensitive to these two parameters, protozoa indirectly stimulate the bacterial cellulolytic activity and supply their own activity to the rumen microbial ecosystem. They could also supply some peptides in the rumen medium which can stimulate the growth of the rumen microbiota, but this aspect has never been considered in the past. Their high contribution to ammonia production has bad consequences on the urinary nitrogen excretion but means also that less dietary soluble nitrogen is necessary when protozoa are present. Changes in the molar percentages of VFA and gases from rumen fermentations are not so large that they could alter significantly the use of energy by animals. The answer of animals to elimination of protozoa (defaunation) depends on the balance between energy and protein needs of animals and the supply of nutrients supplied through the diet. Defaunation is useful in case of diets short in protein nitrogen but not limited in energy supply for animals having high needs of proteins.

The Effect of Sugar Addition and Heat Treatment on the Myofibrillar Protein Extractability (당첨가 및 가열처리가 근원섬유단백질의 추출성에 미치는 영향)

  • Yang, Jong-Beom;Kim, Chang-Han
    • Korean Journal of Food Science and Technology
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    • v.22 no.4
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    • pp.466-472
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    • 1990
  • The effect of sugar addition and heat treatment on the myofibrillar protein extractability was studied. Maillard reaction was dependent on heating time significantly and glucose revealed the highest reactivity for Maillard reaction. The extractability of myofibrillar proteins was lowest in case of glucose addition and decreased according to increasing of heating time, Higher extractability was resulted in by digestion of myofibrillar proteins with enzymes after sugar addition and heat treatment than the undigested samples, as the sample was digested with trypsin that is the highest. And by digestion with trypsin, chymotrypsin and peptidase at a time the extractability of meat proteins increased remarkably.

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Storage Stability of the Synthetic Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Separated from Beef Sarcoplasmic Protein Extracts at Different pH, Temperature, and Gastric Digestion

  • Jang, Ae-Ra;Jo, Cheo-Run;Lee, Moo-Ha
    • Food Science and Biotechnology
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    • v.16 no.4
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    • pp.572-575
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    • 2007
  • The angiontensin converting enzyme (ACE) inhibitory peptides were separated from beef sarcoplasmic protein extract and their amino acid sequences were identified as GFHI, DFHINQ, FHG, and GLSDGEWQ. The 4 peptides were synthesized in a laboratory and the ACE inhibitory activities of pep tides was measured after 2 months of storage at $4^{\circ}C$ under different pH conditions (6.0, 6.5, 7.0, 7.5, and 8.0) and the exposure of different temperatures (70, 80, 90, and $100^{\circ}C$) for 20 min to evaluate industrial use. No significant difference was detected by pH and temperature abuse for 20 min during storage. When the synthetic peptides were digested by pepsin, trypsin, and chymotrypsin, the ACE inhibitory activity was not changed. These results indicated that the 4 synthetic peptides with ACE inhibitory activity were pH-stable, heat-stable, and resistant to proteinases in gastro-intestinal tracts. Therefore, those 4 peptides can be used as a source for functional food product with various applications.

A Method for Protein Identification Based on MS/MS using Probabilistic Graphical Models (확률그래프모델을 이용한 MS/MS 기반 단백질 동정 기법)

  • Li, Hong-Lan;Hwang, Kyu-Baek
    • Proceedings of the Korean Information Science Society Conference
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    • 2012.06b
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    • pp.426-428
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    • 2012
  • In order to identify proteins that are present in biological samples, these samples are separated and analyzed under the sequential procedure as follows: protein purification and digestion, peptide fragmentation by tandem mass spectrometry (MS/MS) which breaks peptides into fragments, peptide identification, and protein identification. One of the widely used methods for protein identification is based on probabilistic approaches such as ProteinProphet and BaysPro. However, they do not consider the difference in peptide identification probabilities according to their length. Here, we propose a probabilistic graphical model-based approach to protein identification from MS/MS data considering peptide identification probabilities, number of sibling peptides, and peptide length. We compared our approach with ProteinProphet using a yeast MS/MS dataset. As a result, our model identified 27 more proteins than ProteinProphet at 1% of FDR (false discovery rate), confirming the importance of peptide length information in protein identification.

A Study on Factors Affecting Anaerobic Digestion of Waste Activated Sludge (活性슬러지의 嫌氣性消化에 미치는 影響因子에 관한연구)

  • 최홍복;황경엽;김윤신
    • Journal of Environmental Health Sciences
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    • v.23 no.1
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    • pp.28-33
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    • 1997
  • This study was carried out to investigate factors affecting anaerobic digestion enhancement of waste activated sludge(WAS). In order to this investigation, the degradability and rupture of microorganisms cell present in WAS, and mesophilic anaerobic digestion(MAD) of these compounds, were also evaluated. The micro-organisms cell in WAS were ruptured by a mechanical jet stream and smashed under pressure of 30 bar. The rupture level of micro-organisms cell in WAS were determined using phosphate, soluble protein and soluble chemical oxygen demand (SCOD)concentrations. It was found that the rupture level of micro- organisms cell within WAS increased with increasing pretreatment times, and the pretreated WAS once under pressure of 30 bar resulted in an increase in VS removal and methane production of 5%, 9% over the intact WAS of 35%, 71%, respectively, in batchwise MAD of 6-day and 14-day retention time. With the pretreatment and MAD of 6-day retention time used, mesophlic bioconvertibility as the biogasification of WAS were found to be significantly higher biogas of 1, 850 ml than 300 ml under intact WAS. In conclusion it can be stated mechanical pretreatment enhances WAS bioconvertibility, while under identical treatment conditions, resulted in a considerable decrease in the bioconvertibility of intact WAS.

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The survey of Trichinella spiralis infection in finishing pigs using the pepsin-digestion method and ELISA in Korea (조직인공소화법과 ELISA를 이용한 국내 출하돈의 선모충(Trichinella spiralis) 감염실태 조사)

  • Seo, Hunsu;Woo, Gye-Hyeong;Youn, Hee-Jeong
    • Korean Journal of Veterinary Research
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    • v.44 no.2
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    • pp.269-277
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    • 2004
  • Trichinella spiralis is one of the important zoonotic parasites with a wide variety of vertebrates hosts in nature. The purpose of this study were to analyze ESP(Excretory-Secretory Protein) antigen, to evaluate ELISA for the serological diagnosis of Trichinosis, and to survey T. spiralis infection in finishing pigs using the pepsin digestion method and ELISA in Korea. In the analysis of ESP antigen by SDS-PAGE and Western blot, 4 major bands (70, 55, 52.6, and 49 kDa) were revealed from the ESP antigen. Predilection sites of T. spiralis were the diaphragm, the tongue, masseter muscles, intercostal muscle, and hindlimb in orders in the experimentally infected rats. Sera from 581 swine were tested by ELISA with ESP antigen. The 54 (9.3%) sera were suspected as positive reactors, however, these 54 sera were determined as false positives by the use of Western blotting. This study demonstrated that the ELISA was not suitable for the examination of T. spiralis in pork. The diaphragm muscle samples of 251 finishing pigs were tested by the method of pepsin-digestion for the presence of Trichinella larvae, however, T. spiralis was not detected from the samples. We could not find out T. spiralis infection in pig in Korea pork.

Effects of protein content and the inclusion of protein sources with different amino acid release dynamics on the nitrogen utilization of weaned piglets

  • Hu, Nianzhi;Shen, Zhiwen;Pan, Li;Qin, Guixin;Zhao, Yuan;Bao, Nan
    • Animal Bioscience
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    • v.35 no.2
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    • pp.260-271
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    • 2022
  • Objective: We aimed to investigate the effect of the differing amino acid (AA) release dynamics of two protein sources on the growth performance, nitrogen deposition, plasma biochemical parameters, and muscle synthesis and degradation of piglets when included in their diets at normal and low concentrations. Methods: Forty-eight piglets (Duroc×Landrace×Large White) with initial body weight of 7.45±0.58 kg were assigned to six groups and fed one of 6 diets. The 6 dietary treatments were arranged by 3×2 factorial with 3 protein sources and 2 dietary protein levels. They are NCAS (a normal protein content with casein), NBlend (a normal protein content with blend of casein and corn gluten meal), NCGM (a normal protein content with corn gluten meal), LCAS (a low protein content with casein), LBlend (a low protein content with blend of casein and corn gluten meal), LCGM (a low protein content with corn gluten meal). The release dynamics of AA in these diets were determined by in vitro digestion. The digestibility, utilization and biological value of nitrogen in piglets were determined by micro Kjeldahl method. Plasma insulin was measured by enzyme-linked immunosorbent assay kits. The protein expression of mediators of muscle synthesis and degradation was determined by western blotting. Results: Although the consumption of a low-protein diet supplemented with crystalline AA was associated with greater nitrogen digestion and utilization (p<0.05), the final body weight, growth performance, nitrogen deposition, and phosphorylation of ribosomal protein S6 kinase 1 and eIF4E binding protein 1 in the muscle of pigs in the low-protein diet-fed groups were lower than those of the normal-protein diet-fed groups (p<0.05) because of the absence of non-essential AA. Because of the more balanced release of AA, the casein (CAS) and Blend-fed groups showed superior growth performance, final body weight and nitrogen deposition, and lower expression of muscle ring finger 1 and muscle atrophy F-box than the CGM-fed groups (p<0.05). Conclusion: We conclude that the balanced release of AA from CAS containing diets and mixed diets could reduce muscle degradation, favor nitrogen retention, % intake and improve growth performance in pigs consuming either a normal- or low-protein diet.

Effect of Replacing Corn and Wheat Bran With Soyhulls in Lactation Cow Diets on In Situ Digestion Characteristics of Dietary Dry Matter and Fiber and Lactation Performance

  • Meng, Qingxiang;Lu, Lin;Min, Xiaomei;McKinnon, P.J.;Xiong, Yiqiang
    • Asian-Australasian Journal of Animal Sciences
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    • v.13 no.12
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    • pp.1691-1698
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    • 2000
  • An in situ digestion trial (Experiment 1) and a lactation trial (Experiment 2) were conducted to determine the effects of replacing corn and wheat bran with soyhulls (SH) in lactating dairy cow diets on the extent and kinetics of digestion of DM and NDF, and lactation performance. In experiment 1, five mixed feeds consisting of mixed concentrate and roughages (50:50 on a DM basis) were formulated on isonitrogenous and isoenergetic bases to produce five levels (0, 25, 50, 75 and 100%) of SH replacement for corn and wheat bran. SH had high in situ digestion (92 and 89% for potentially digestible DM and NDF) and fairly fast digestion rate (7.2 and 6.3 %/h for DM and NDF). Increasing level of SH replacement resulted in increased NDF digestibility (linear, p=0.001-0.04) and similar DM digestibility (beyond 12 h incubation, p=0.10-0.41). As level of SH replacement increased, percentage of slowly digestible fraction (b) of DM increased (linear, p=0.03), percentage of rapidly digestible fraction (a) of DM tended to decrease (linear, p=0.14), and DM digestion lag time tended to be longer (linear, p=0.13). Percentage of potentially digestible fraction (a+b) and digestion rate (c) of slowly digestible fraction of dietary DM remained unaltered (p=0.36-0.90) with increasing SH in the diet. Increasing level of SH for replacing corn and wheat bran in the diet resulted in increases in percentages of b (quadratic, p<0.001), a (linear, p=0.08), a+b (quadratic, p=0.001) and a tendency to increase in c for NDF (linear, p<0.19). It was also observed that there was a satisfactory fit of a non-linear regression model to NDF digestion data ($R^2=0.986-0.998$), but a relatively poor fit of the model to DM digestion data ($R^2=0.915-0.968$). In experiment 2, 42 lactating Holstein cows were used in a randomized complete block design. SH replaced corn and wheat bran in mixed concentrates at 0, 25, and 50%, respectively. These mixed concentrates were mixed with roughages and fed ad libitum as complete diets. Replacing corn and wheat bran with SH at 0, 25 and 50% levels did not influence (p=0.56-0.95) DM intakes (18.4, 18.6, and 18.5 kg/d), milk yields (27.7, 28.4 and 27.6 kg/d), 4% fat-corrected-milk (FCM) yields (26.2, 27.6, and 27.3 kg/d) and percentages of milk protein (3.12, 3.17 and 3.18%), milk lactose (4.69, 4.76 and 4.68%) and SNF (8.50, 8.64, and 8.54%). On the other hand, milk fat percentges linearly increased (3.63, 3.85 and 3.90% for SH replacement rates of 0, 25 and 50% in the diet, p=0.08), while feed costs per kg FCM production were reduced.

Changes in Physicochemical Properties of Soybean Protein due to Acetylation during Incubation with Glucose

  • Kim, Myung-Hee;Kim, Jin-Hee;Kim, Kang-Sung
    • Journal of Environmental Health Sciences
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    • v.30 no.4
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    • pp.308-313
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    • 2004
  • Native and acetylated soybean protein with acetylation percentage of $25\%$ were incubated with glucose to induce Maillard reaction. Acetylation of ${\varepsilon}$-amino group of lysine residues changed the conformation of soybean protein. The direct uv spectrum of native and acetylated soybean protein showed conformational changes with accessibility of tyrosine and tryptophan residues increased. Acetylation suppressed Maillard reaction between soybean protein and glucose. Acetylated soybean protein showed improved water sorption, fat binding, foam formation, and emulsion activity of the protein, but depressed brown pigment development and trypsin digestion. Thus aceylation prevented deterioration of certain functional characteristics that occurred during storage, besides causing functional characteristics to be improved on its own.

Studies on Heated Protein Quality Using Homoarginine Method

  • Lee, Kyung--Hee;Hel
    • Preventive Nutrition and Food Science
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    • v.1 no.1
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    • pp.10-15
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    • 1996
  • To determine the quality of heated protein, in vitro method, invluding lysine, lysionalanine, and fructose-lysine as well as homoarginine by guanidination of lysine, was assessed using heated casein with of without glucose. In vivo methods such as PER, digestibility and BV were also tried on homoarginine, lysinoalanine, fructoselysine, and lysine. The nonreactive lysine for huanidination was hardly digestive, while the non heat damaged lysine side chanis in the protein were accessible for guanidination as well as for the digestion. A linear correlation(${\gamma}$=0.80) was obstained between PER and digestibility of the analysed lysine. Digestibility of homoarginine was higher that of true protein. However, in the guanidinated heated casein with glucose, digestibility of homoarginine was significantly reduced. It is suggested that the homoarginine method may mislead to over- or underestimation of the damaged protein quality.

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