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Effects of Heat-oxidized Soy Protein Isolate on Growth Performance and Digestive Function of Broiler Chickens at Early Age

  • Chen, X.;Chen, Y.P.;Wu, D.W.;Wen, C.;Zhou, Y.M.
    • Asian-Australasian Journal of Animal Sciences
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    • v.28 no.4
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    • pp.544-550
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    • 2015
  • This study was conducted to investigate effects of heat-oxidized soy protein isolate (HSPI) on growth performance, serum biochemical indices, apparent nutrient digestibility and digestive function of broiler chickens. A total of 320 1-day-old Arbor Acres chicks were randomly divided into 4 groups with 8 replicates of 10 birds, receiving diets containing soy protein isolate (SPI, control group) or the same amount of SPI heated in an oven at $100^{\circ}C$ for 1, 4, or 8 h, for 21 days, respectively. The results indicated that compared with the control group, body weight gain and feed intake of birds fed diet containing SPI heated for 8 h were significantly lower (p<0.05). Serum urea nitrogen concentration was higher in the broilers fed diet containing SPI heated for 4 or 8 h at d 21 (p<0.05). In contrast, serum glucose content was decreased by HSPI substitution at d 21 (p<0.05). The relative pancreas weight in HSPI groups was higher than that in the control group at d 21 (p<0.05). Meanwhile, the opposite effect was observed for relative weight of anterior intestine and ileum in broilers fed a diet containing SPI heated for 8 h (p<0.05). Birds fed diets containing SPI heated for 4 or 8 h had a decreased lipase activity in anterior intestinal content at d 14 and 21 (p<0.05), respectively. In addition, the same effect was also noted in broilers given diets containing SPI heated for 1 h at d 21 (p<0.05). Similarly, amylase, protease and trypsin activity in anterior intestinal content were lower in broilers fed diets containing SPI heated for 8 h at d 21 (p<0.05). The apparent digestibility of dry matter (DM) from d 8 to 10 and DM, crude protein (CP), and ether extract from d 15 to 17 were lower in broilers fed diets containing SPI heated for 8 h (p<0.05). Besides, birds given diets containing SPI heated for 4 h also exhibited lower CP apparent digestibility from d 15 to 17 (p<0.05). It was concluded that HSPI inclusion can exert a negative influence on the growth performance of broilers, which was likely to result from the simultaneously compromised digestive function.

Influence of dietary supplementation of autolyzed whole yeast and yeast cell wall products on broiler chickens

  • Ahiwe, Emmanuel Uchenna;Abdallh, Medani Eldow;Chang'a, Edwin Peter;Omede, Apeh Akwu;Al-Qahtani, Mohammed;Gausi, Harriet;Graham, Hadden;Iji, Paul Ade
    • Asian-Australasian Journal of Animal Sciences
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    • v.33 no.4
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    • pp.579-587
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    • 2020
  • Objective: This study evaluated the effect of yeast products on growth performance, visceral organ weights, endogenous enzyme activities, ileal nutrient digestibility and meat yield of broiler chickens fed diets containing autolyzed whole yeast (WY) and yeast cell walls (YCW) at varying levels of inclusion. Methods: Nine dietary treatments consisting of WY or YCW included at 0.5, 1.0, 1.5, or 2.0 g/kg diet and a control diet without yeast supplementation was used in the experiment. Each of the nine treatments was replicated six times with nine birds per replicate. Birds were housed in cages, in climate-controlled rooms and fed starter, grower and finisher diets. Results: There was an improvement (p<0.05) in body weight gain and feed conversion ratio on d 10, 24, and 35 for birds fed 1.0 to 2.0 g/kg WY or YCW diet. Small intestine weight was heavier on d 10 and 24 for birds on higher levels of WY and YCW compared to the control group. On d 10 and 24, there was a significant increase (p<0.05) in tissue protein content and pancreatic enzyme activities (trypsin and chymotrypsin) of birds on 1.5 to 2.0 g/kg WY and YCW diets compared to the control group. Compared to the control group, birds on WY (2.0 g/kg diet) and YCW (at 1.5 and 2.0 g/kg diet) had better (p<0.05) protein digestibility on d 24. On d 35, there was significant improvement (p<0.05) in percentage of carcass, absolute and relative breast weight for broiler chickens fed WY and YCW mostly at 2 g/kg diet compared to birds on the control diet. Conclusion: Supplementation of diets with autolyzed WY and YCW products especially at 1.5 to 2.0 g/kg diet improved broiler chicken performance and meat yield through their positive effects on ileal protein digestibility and pancreatic enzyme activities.

Development of mass spectrometric analysis of $\alpha_1$(I) and $\alpha_2$(I) chain Collagen ($\alpha_1$(I)및 $\alpha_2$(I)사슬 콜라겐의 질량분석법 개발 연구)

  • Kim, Kwang-Yon;Cho, Seon-Young;Lee, Sang-Han;Nnm, Hae-Seon;Kim, Sung-Ho
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.6 no.2
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    • pp.134-143
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    • 2005
  • Collagen is the important structural proteins in mammals with various peptide composition and cross-linkings. The direct analysis of collagen protein was not suitable because of its structural complexity and diversity. In this study, we suggest the simple way of collagen analysis by introducing matrix-assisted laser desorption/ionization time-of flight mass spectrometry (MALDI-TOF MS) to identify the collagen and its trypsin-digested fragments, and by subsequent time-of-flight tandem mass spectrometry(Q-TOF MS/MS) to analyze the amino acid sequences of identified fragments. Using the collagen samples extracted from the tail of mouse, 10 separated bands were found in SDS-PAGE, and the masses of most bands could be more finely determined by MALDI-TOF MS. When each 10 separated proteins was tryptic digested and introduced to MALDI-TOF, the Gly1056-Arg1073 fragment from $\alpha_1$-chain was identified in four bands, and the Gly1056-Arg1073 fragment from $\alpha_2$-chain was identified in five bands, both in type I collagen. Although few fragments were found because of the cross-linkings left in digested collagen sample, it could be determined that the type I collagen existed at least in 7 separated bands. When the amino acid sequences of two identified fragments were analyzed by Q-TOF MS/MS, both sequences were identical with those determined by MALDI-TOF MS. It suggested that the two peaks in MALDI-TOF MS caused by the fragments identified in this work could be used as the fingerprint to simply identify type I collagen in protein samples.

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preparation of Sauce from Enzymatic Hydrolysates of Cod Frame Protein (대구 Frame 단백질 가수분해물을 이용한 효소분해간장의 제조)

  • 김세권;빅표잠;김규형
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.29 no.4
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    • pp.635-641
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    • 2000
  • In order to utilize the protein source from a fish proessing by-product, cod was hydrolyzed with various enzymes such as tuna pyloric caeca crude enzyme (TPCCE), a-chymotrypsin, trypsin, papain and pronase E. The TPCCE hydrolysate acquired the highest sensory properties on taste, odor and color. The resultant cod rfame protein hydrolysate (CFPH) which was hydrolyzed with TPCCE, was separated through a series of ultrafiltration membranes with molecular weight cut-off (MWCO) of 30, 10, 5 and 1 kDa, and four types of permeates in cluding 30 K (permeate from 30 kDa membrane), 10 K (permeate from 10 kDa membrane), 5 K (permeate from 5 kDa membrane) and 1 K (permeate from 1 kDa membrane) were obtained. The natural sauces were prepared with 30 K, 10 K, 5 K and 1 K hydrolysate, and the sauce prepared with 1 K hydrolysate was the best score in sensory evaluations. In addition the mixed sauce prepared with 1 K hydrolysate and commercial soy sauce was similar to commercial sauce in sensory properties. These results suggest that the mixed sauce would be utilized as the substitute of acid-hydrolysis sauce.

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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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Antioxidative Activity of Enzymatic Hydrolysates Derived from Anchovy Muscle Protein (멸치육 단백질 효소가수분해물의 항산화작용)

  • YEUM Dong-Min;LEE Tae-Gee;PARK Yeung-Ho;KIM Seon-Bong
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.30 no.5
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    • pp.842-849
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    • 1997
  • This study was designed to investigate the antioxidative activity of enzymatic hydrolysates prepared from defatted anchor muscle by various pretenses. In these hydrolysates, the hydrolysates derived from pepsin and Protamex showed the strongest antioxidative activity. Enzymatic hydrolysates also showed the synergistic effects on antioxidative activity of $\alpha-tocopherol$, and almost no change in butylated hydroxytoluene (BHT). Peroxidation of metal ions $(Fe^{3+},\;Cu^{2+})$ was inhibited by enzymatic hydrolysates. Ten fractions (P-1 to P-10) were fractionated from the peptic hydrolysates by Amberlite IR-120 and Bio-gel P-2 column chromatography. The maximum antioxidative activity was observed in the traction P-2 (fraction No. $26\~31$). In amino acid composition of before and after hydrolysis of defatted anchovy muscle and the active fractions (P-2), contents of aspartic arid and glutamic acid were increased, but alanine, cysteine, tyrosine and phenylalanine were decreased.

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Molecular Cloning and Expression of a Novel Protease-resistant GH-36 $\alpha$-Galactosidase from Rhizopus sp. F78 ACCC 30795

  • Yanan, Cao;Wang, Yaru;Luo, Huiying;Shi, Pengjun;Meng, Kun;Zhou, Zhigang;Zhang, Zhifang;Yao, Bin
    • Journal of Microbiology and Biotechnology
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    • v.19 no.11
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    • pp.1295-1300
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    • 2009
  • A 2,172-bp full-length gene (aga-F78), encoding a protease-resistant $\alpha$-galactosidase, was cloned from Rhizopus sp. F78 and expressed in Escherichia coli. The deduced amino acid sequence shared highest identity (45.0%) with an $\alpha$-galactosidase of glycoside hydrolase family 36 from Absidia corymbifera. After one-step purification with a Ni-NTA chelating column, the recombinant Aga-F78 migrated as a single band of ~82 and ~210 kDa on SDS-PAGE and nondenaturing gradient PAGE, respectively, indicating that the native structure of the recombinant Aga-F78 was a trimer. Exhibiting the similar properties as the authentic protein, purified recombinant Aga-F78 was optimally active at $50^{\circ}C$ and pH 4.8, highly pH stable over the pH range 5.0-10.0, more resistant to some cations and proteases, and had wide substrate specificity (pNPG, melidiose, raffinose, and stachyose). The recombinant enzyme also showed good hydrolytic ability to soybean meal, releasing galactose of $415.58\;{\mu}g/g$ soybean meal. When combined with trypsin, the enzyme retained over 90% degradability to soybean meal. These favorable properties make Aga-F78 a potential candidate for applications in the food and feed industries.

Proteomic analysis of Korean mothers' human milk at different lactation stages; postpartum 1, 3, and 6 weeks (출산 후 경과한 날에 따른 한국인 산모의 모유 단백체 분석)

  • Park, Jong-Moon;lee, Hookeun;Song, Seunghyun;Hahn, Won-Ho;Kim, Mijeong;Lee, Joohyun;Kang, Nam Mi
    • Analytical Science and Technology
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    • v.30 no.6
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    • pp.348-354
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    • 2017
  • In this study, patterns of proteome expression were monitored and specifically expressed proteins in human milk were detected in collected human milk after 1 week, 3 weeks, and 6 weeks from delivery. A quantitative shotgun proteomic approach was used to identify human milk proteins and reveal their relative expression amounts. For each sample, two independent human milk samples from two mothers were pooled, and then three replicated shotgun proteomic analyses were carried out. Casein, which is a highly abundant protein in human milk, was removed, and then trypsin was treated to produce a digested peptide mixture. The peptides were loaded in the home-made reversed-phase C18 fused-silica capillary column, and then the eluted peptides were analyzed by using a linear ion-trap mass spectrometer. The relative quantitation of proteins was performed by the normalized spectral count method. For each sample, 81-109 non-redundant proteins were identified. The identified proteins consisted of glycoproteins, metabolic enzyme, and chaperon enzymes such as lactoferrin, carboxylic ester hydrolase, and clusterin. The comparative analysis for the 63 proteins, which were reproducibly identified in all three replications, revealed that 25 proteins were statically significant differentially expressed. Among the differentially expressed proteins, Ig lambda-7 chain C region and tenascin drastically decreased with the delivery time.

Impact on Inflammation and Recovery of Skin Barrier by Nordihydroguaiaretic Acid as a Protease-Activated Receptor 2 Antagonist

  • Kim, Hyo-Young;Goo, Jung-Hyun;Joo, Yeon-Ah;Lee, Ha-Yoen;Lee, Se-Mi;Oh, Chang-Taek;Ahn, Soo-Mi;Kim, Nam-Hoon;Hwang, Jae-Sung
    • Biomolecules & Therapeutics
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    • v.20 no.5
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    • pp.463-469
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    • 2012
  • Atopic dermatitis is a chronic, inflammatory disease of the skin with increased transepidermal water loss. Both an abnormal inflammatory response and a defective skin barrier are known to be involved in the pathogenesis of atopic dermatitis. Protease activated receptor 2 (PAR2) belongs to a family of G-protein coupled receptors and is activated by both trypsin and a specific agonist peptide, SLIGKV-$NH_2$. PAR2 is expressed in suprabasal layers of the epidermis and regulates inflammatory responses and barrier homeostasis. In this study, we show that nordihydroguaiaretic acid (NDGA) inhibits the PAR2-mediated signal pathway and plays a role in skin barrier recovery in atopic dermatitis. Specifically, NDGA reduces the mobilization of intracellular $Ca^{2+}$ in HaCaT keratinocytes by down-regulating inflammatory mediators, such as interleukin-8, thymus and activation-regulated chemokine and intercellular cell adhesion molecule-1 in HaCaT keratinocytes. Also, NDGA decreases the protein expression of involucrin, a differentiation maker of keratinocyte, in both HaCaT keratinocytes and normal human epidermal keratinocytes. We examined NDGA-recovered skin barrier in atopic dermatitis by using an oxazolone-induced atopic dermatitis model in hairless mice. Topical application of NDGA produced an increase in transepidermal water loss recovery and a decrease in serum IgE level, without weight loss. Accordingly, we suggest that NDGA acts as a PAR2 antagonist and may be a possible therapeutic agent for atopic dermatitis.

Electrophoretic analysis of the major protein of erythrocyte membrane in man, bovine, horse, and dog: their relation to erythrocyte sedimentation rate (사람, 소, 말, 개의 적혈구막 단백의 전기 영동법에 의한 분석 - 적혈구 침강 속도와의 관계 -)

  • Bahk, Yeong-woo
    • Korean Journal of Veterinary Research
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    • v.41 no.1
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    • pp.21-28
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    • 2001
  • The protein of the bovine, horse and dog erythrocyte membrane were analyzed by polyacrylamide gel eletrophoresis in sodium dodecyl sulfate and their relation to the sedimentation rate of animal erythrocytes were investigated by treating the erythrocytes with proteinases such as trypsin and chymotrypsin. Protein content in erythrocyte membrane was in human, in Jindo dog, in cattle and in horse, showing similar in among. The erythrocyte sedimentation rates bovine erythrocytes from Hostein and Korean native cattle were very slow compared with the human one(1/7 as slow as the human one) as reported previously. Although the general protein profiles of the bovine erythrocyte membranes were almost similar to that of human, bovine erythrocyte membranes showed one additional protein band, called band Q in this study, which migrated electrophoretically to the mid-position between band 2 and band 3 in human erythrocyte membranes. The erythrocyte sedimentation of race horse were very fast compared with the human one are reported previously. Although the general protein profiles of the race horse erythrocyte membranes were almost similar to that of human, band 3 content was showing higher in race horse(34.7%) than in human(25.3%). The general protein profile of the Jindo dog erythrocyte membrane was almost similar to the human patterns, Jindo dog erythrocyte membranes showed one absent protein band. It was band 7. The glycoprotein profiles of the bovine erythrocyte membranes revealed by periodic acid-Schiff(PAS) stain showed a marked difference from that of human. The PAS-1(glycophorin) and PAS-2(sialoglycoprotein) present in human erythrocyte membrane were almost absent from the bovine erythrocyte membranes showed a strong PAS-positive band near the origin of the electraphorograms, which is named as PAS-B in this study. The PAS-1 and PAS-2 present in human erythrocyte membrane were almost absent from race horse erythrocyte membranes, but PAS-2 was more in only race horse from that of human. The PAS-1 and PAS-2 were absolutely absent from the Jindo dog erythrocyte membrane. These results suggest the slow sedimentation rate of bovine erythrocytes is due in part to the presence of band Q protein fraction and PAS-B glycoprotein in the bovine erythrocytes, and that the fast sedimentation rate of race horse erythrocyte is due in part to the presence of more band 3 protein fraction and PAS-E glycoproteins in the race horse erythrocytes.

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