• Title/Summary/Keyword: chymotrypsin

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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.

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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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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Studies on peptide during soybean-koji preparation -Part III Amino acid sequence of oligopeptides formed during soybean-koji preparation- (콩고오지 제조중(製造中)의 peptide에 관(關)한 연구(硏究) -제3보(第三報) 콩고오지 제조중(製造中)에 생성(生成)되는 저급(低級) peptide의 구조(構造)-)

  • Kim, Ze-Uook
    • Applied Biological Chemistry
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    • v.6
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    • pp.107-117
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    • 1965
  • (1) In order to study the specificity of Aspergillus soya protease to soybean protein, as well as the types of peptides formed during soybean-koji prerapation the amino acid sequence for the di & tripeptide and N-terminal amino acid residue and C-terminal amino acid residue were identified. As the results of the study, the following were obtained. Gly, Glu. Ala. Ser. Glu. Ser. Ala. Val (Cys, Glu, Ser, Ala, Arg, Try, Leu or Ileu) Asp. Phe (His, Arg, Cys, Asp, Ser, Ala, Leu or Ileu) Glu. Ala (Cys, Gly, Met) Glu. Ala (Asp, Glu,) Gly. Met (Asp, Glu, Ala, Tyr, Leu or Ileu, Lys,) Gly. Leu or Ileu (His, Asp, Glu, Gly, Ser, Lys, Thr, Phe,) Cys. Gly (Asp, Tyr,) Glu. Pro (Asp, Glu, Ser, Gly, Thr, Ala, Val, Leu or Ileu) Try. Ser (Gly, Glu, Arg, Ala, Met, Leu or Ileu,) Asp. Met (Asp, Glu, Ala, Try, Pro, Leu or Ileu,) His Thr (Ser, Gly, Tyr, Pro, Leu or Ileu,) Glu. Gly (Asp, Ala, Ser, Glu,) Leu or Ileu (2) It has revealed that Aspergillus soya protease has considerably wider range of specificity than that of chymotrypsin, pepsin and trypsin but not mold protease and Aspergillus saitoi protease. It can be said that Asp. soya protease split the bond adjacent to glutamic acid, aspartic acid, glycine, serine, alanine, cystine, tryptophan, histidine preferably acidic amino acid as C-terminal amino acid residue.

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Derivatization of Rice Wine Meal Using Commercial Proteases and Characterization of Its Hydrolysates (단백질가수분해효소를 이용한 탁주박의 가수분해 및 그 분해물의 특성)

  • Kim, Chang-Won;Choi, Hyuk-Joon;Han, Bok-Kyung;Yoo, Seung-Seok;Kim, Chang-Nam;Kim, Byung-Yong;Baik, Moo-Yeol
    • Korean Journal of Food Science and Technology
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    • v.43 no.6
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    • pp.729-734
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    • 2011
  • With the goal of transforming rice protein from an insoluble to a soluble form to increase the industrial utilization of rice wine meal (RWM), RWM was derivatized using commercial proteases and the RWM hydrolysates were characterized. Eight commercial proteases were used individually or in combination for hydrolysis of RWM. The degree of hydrolysis was assessed by determining the soluble protein in supernatant using the Lowry assay, protein in precipitates using a semimicro Kjeldahl procedure, and gravimetrically by the weight difference before and after hydrolysis. Protamex, Alcalase and Protease N proteases were most effective for hydrolysis of RWM. Although these assessment methodologies displayed some variation, they generally showed a similar pattern. When the aforementioned three proteases were simultaneously used to treat RWM, no significant difference was observed between the three assays (p<0.05) indicating an absence of enzymatic synergy.

A study on the nonadrenergic noncholinergic neurotransmitters in porcine gastric fundus (돼지 위저부 평활근의 비아드레날린 비콜린성 신경전달물질에 관한 연구)

  • Kim, Tae-wan;Na, Jun-ho;Lee, Jang-hern;Yang, Il-suk
    • Korean Journal of Veterinary Research
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    • v.37 no.1
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    • pp.119-128
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    • 1997
  • The relaxation of gastric fundus smooth muscles is the primary physiological event which induces the receptive relaxation of monogastric animals. L-arginine/Nitric oxide(L-arg/NO) system is known to mediate the inhibitory non-adrenergic non-cholinergic(NANC) neurotransmission in various tissues including gastrointestinal smooth muscles. The longitudinal smooth muscles of porcine gastric fundus showed fast relaxation during electrical field stimulation(EFS) and rebound contraction after EFS in NANC condition. So, the purpose of present study was elucidation of the neurotrasmitters related to the NANC relaxation and explanation of the relation between NANC relaxation and L-arg/NO system. The longitdinal smooth muscles of porcine gastric fundus were hung in the organ bath and under the presence of guanethidine($5{\times}10^{-5}M$), precontraction was induced by carbachol($1{\times}10^{-6}M$). The muscle responses to EFS and drugs were isomerically recorded. The rusults were summarized as follows. 1. The longtudinal muscles of porcine gastric fundus showed frequency-dependent relaxation and rebound contraction to electrical field stimulaton(1ms, 8V, 1~16Hz, 20sec, EFS). These responses were blocked by tetrodotoxin($1{\times}10^{-6}M$). 2. The relaxation and rebound contraction of the longitudinal muscles of porcine gastric fundus to EFS were inhibited by L-NAME($2{\times}10^{-5}M$). The inhibitory effect of L-NAME was antagonized by L-arginine($1{\times}10^{-3}M$), but not by D-arginine($1{\times}10^{-3}M$). 3. Exogenous NO($NaNO_2$, $1{\times}10^{-5}{\sim}1{\times}10^{-4}M$, pH=2.0) caused concentration-dependent relaxation as EFS did. 4. Methylene Blue($2{\times}10^{-5}M$), a soluble guanylate cyclase inhibitor, inhibited the relaxation and rebound contraction of the longitudinal muscles of porcine gastric fundus induced by EFS, but N-ethlmaleimide, a adenylate cyclase inhibitor, did not. 5. 8-Br-cGMP($1{\times}10^{-6}{\sim}3{\times}10^{-6}M$), permeable cGMP analogue, induced dose-dependent relaxation. but 8-Br-cAMP($1{\times}10^{-6}{\sim}3{\times}10^{-6}M$), permeable cAMP analogue, did not. Both did not evoked rebound contraction. 6. ${\alpha}$-chymotrypsin did not affect the relaxation of the longitudinal muscles of porcine gastric fundus. 7. Reactive blue 2($1{\times}10^{-4}M$, 40min) siginificantly inhibited the rebound contraction induced by EFS and inhibited contraction caused by exogenous ATP($1{\times}10^{-4}{\sim}1{\times}10^{-3}M$). These results suggests that NANC relaxation of the longitudinal muscles of porcine gastric fundus mainly mediated by NO and the rebound contraction is related to NO and other neurotransmitters.

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Purification and Characterization of the Bacteriocin Produced by Lactococcus sp. KD 28 Isolated from Kimchi (김치에서 분리한 Lactococcus lactis가 생산하는 박테리오신의 정제 및 특성)

  • Lee, Ji-Young;Choi, Nack-Shick;Chun, Sung-Sik;Moon, Ja-Young;Kang, Dae-Ook
    • Journal of Life Science
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    • v.25 no.2
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    • pp.180-188
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    • 2015
  • The bacterial strain isolated from Kimchi showed antibacterial activity against Micrococcus luteus IAM 1056. The selected strain was identified as Lactococcus lactis by 16S rRNA nucleotide sequence analysis and named as Lactococcus sp. KD 28. The treatment of culture supernatant with proteinase K removed antibacterial activity, indicating its proteinaceous nature, a bacteriocin. This bacteriocin was sensitive to hydrolytic enzymes such as ${\alpha}$-chymotrypsion, trypsin, proteinase K, lipase, ${\alpha}$-amylase and subtilisin A. The bacteriocin was highly thermostable and resistant to heating at $80^{\circ}C$ for up to an hour but 50 % of the total activity was remained at $100^{\circ}C$ for 30 min. The pH range from 2.0 to 8.0 had no effect on bacteriocin activity and it was not affected by solvents such as acetonitrile, isopropanol, methanol, chloroform and acetone up to 50% concentration. The bacteriocin showed antibacterial activity against M. luteus IAM 1056, Lactobacillus delbrueckii subsp. lactis KCTC 1058, Enterococcus faecium KCTC 3095, Bacillus cereus KCTC 1013, B. subtilis KCTC 1023, Listeria ivanovii subsp. ivanovii KCTC 3444, Staphylococcus aureus subsp. aureus KCTC 1916, B. megaterium KCTC 1098 and B. sphaericus KCTC 1184. The bacteriocin was purified through ammonium sulfate concentration, SP-Sepharose chromatography and RP-HPLC. The molecular weight was estimated to be about 3.4 kDa by tricine-SDS-PAGE analysis.

Angiotensin-I Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Mackerel Muscle Protein (효소에 의한 고등어 근육단백질 가수분해물의 Angiotensin-I 전환효소 저해작용)

  • YEUM Dong-Min;LEE Tae-Gee;BYUN Han-Seok;KIM Seon-Bong;PARK Yeung-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.25 no.3
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    • pp.229-235
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    • 1992
  • Fish protein hydrolysates(FPH) prepared from defatted mackerel meal by proteases such as complex enzymes, bromelain, alcalase, $\alpha-chymotrypsin,$ trypsin, papain and pepsin were tested for inhibitory activity against angiotensin-I converting enzyme(ACE). Among proteases tested, the hydrolysates obtained from the treatment of complex enzymes or bromelain showed relatively higher activity. ACE inhibitory activity of the hydrolysates increased until hydrolysis of 8 hrs, and was stable by heat treatment for 20min at $100^{\circ}C.$ From the profiles of fractionation of the hydrolysates with Bio-gel P-2, the most active fraction had about MW 1,450 and it's amino acid was abundant in Asp, Glu, Lys, Leu, Val and Ala. $IC_{50}\;(amounts\;of\;inhibitors\;needed\;for\;50\%\;inhibition)$ of the active fraction of the hydrolysates obtained from the treatment of complex enzyme and bromelain was 90 and $130 {\mu}g,$ respectively.

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Proteolysis of Defatted Rice Bran Using Commercial Proteases and Characterization of Its Hydrolysates (탈지미강 단백질의 가수분해 및 분해물의 특성 연구)

  • Kim, Chang-Won;Kim, Hyun-Seok;Kim, Byung-Yong;Baik, Moo-Yeol
    • Food Engineering Progress
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    • v.15 no.1
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    • pp.41-47
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    • 2011
  • The defatted rice bran (DRB) was enzymatically hydrolyzed using eight commercial proteases for 4hr at optimum pH and temperature. Proteolytic hydrolysates were examined in supernatant and precipitate using lowry, semimicro kjeldahl and gravimetric method using weight difference before and after enzymatic hydrolysis. In lowry and kjeldahl protein assay method, two proteases (Alcalase and Protease N) were found to be the most effective enzymes. In gravimetric method, 60.6~118.3 mg protein/g DRB was hydrolyzed after eight commercial proteases treatments. Similar to lowry and kjeldahl method, 118.3 and 107.1 mg protein/g DRB were hydrolyzed after Alcalase and Protease N treatments, respectively. When two or three effective proteases (Protamex, Alcalase and Protease N) were applied at one time to obtain synergistic effect, significant increase (P<0.05) was observed when three proteases were applied at one time (63.4 mg protein/g DRB in lowry method and 204.5 mg protein/g DRB in gravimetric method). This result suggests that Alcalase and Protease N were the most effective enzymes for proteolysis of DRB and three commercial enzymes (Protamex, Alcalase and Protease N) showed the synergistic effect on the hydrolysis of DRB.

Studies on the Growth Characteristics of Bifidobacteria, Organic Acids and n-hexanal Contents During the Fermentation of Enzyme Treated Soy Yogurt (효소처리 분리대두단백의 요구르트 발효 중 비피더스균의 생육특성 및 유기산과 n-hexanal 함량에 관한 연구)

  • 이숙영;이정은;박미정;권영실
    • Korean journal of food and cookery science
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    • v.14 no.5
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    • pp.589-596
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    • 1998
  • This study was carried out to evaluate the quality attributes of soy yogurts prepared by different types of oligosaccharides (fructooligosaccharide, galactooligosaccharide , isomaltooligosaccharide) and Bifidobacteria (B. bifidum B. breve, B. infantis) containing enzyme treated soy protein isolate in terms of pH, titratable acidity, total number of viable cells of Bifidobacteria, ${\alpha}$-galactosidase activity, organic acids, volatile compounds. The pH values of soy yogurts fermented by B. bifidum showed the highest significantly but those fermented by B. infantis showed the lowest significantly, while the titratable acidity of soy yogurts were vice versa. The viable cells of Bifidobacteria of all soy yogurts showed more than 10$\^$9/ CFU/ml and soy yogurts fermented by B. infantis showing below pH 4.6 showed more than 10$\^$9/ CFU/ml after storage at 4$^{\circ}C$ for 7 days. The activity of ${\alpha}$-galactosidase showed the highest in the culture of B. infantis among the Bifidobacteria tested. Among the Bifidobacteria tested, the contents of lactic acid and acetic acid showed the highest in soy yogurts fermented by B. infantis but citric acid and propionic acid were the lowest. Among the Bifidobacteria tested, the contents of n-hexanal showed the highest in soy yogurts fermented by B. breve and a little amounts of acetaldehyde were present in all soy yogurts.

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