• 제목/요약/키워드: ${\alpha}$-amylase activity

검색결과 563건 처리시간 0.025초

Barley Malt Treated with Enzymes Increases Polyphenol Content and Antioxidant Activity

  • Phouthaxay, Phonesavanh;Yu, Chi Young;Pang, Yeon Gyu;Salitxay, Timnoy;Kim, Sang Heon;Park, Cheol Ho
    • 한국자원식물학회지
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    • 제28권6호
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    • pp.759-766
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    • 2015
  • The purpose of this study was to improve the functionality of a healthy drink with examining the possibility of manufacturing different enzymes (alpha-, beta-, glucose-amylase) in barley malts (BM) produced in various malting periods. The study showed that enzyme treatment increased significantly total polyphenol content (TPC), DPPH radical scavenging activity and hydroxly radical scavenging activity in malted liquid samples (MLS) which obtained from various malting periods. The highest of TPC were found in Gluco-24M with 1.981 mgTAE/ml, followed by Beta-24M and Alpha-72M with 1.878 mgTAE/ml and 1.845 mgTAE/ml, respectively. The DPPH result revealed that percent of inhibition increased by 71-75% compared to the control. No statistical difference was found between MLS obtained by 24 hr of malting (24 M) and 72 hr of malting (72 M) after enzyme treatment. In addition, an increasing of hydroxyl radical was in the same trend to the TPC and DPPH. The hydroxyl radical scavenging activity of enzyme treated samples was 1,5 times higher than the control. These results suggest the possibility of enzyme application to barley malts obtained in various germination periods for improving quality and functionality of barley malts.

영양강화 Rotifer와 효소활성 향상 Rotifer의 먹이효율 비교 (Comparison of Feed Efficiency Between Rotifers Enriched Lipid-contents to Enrichment and Enhanced Digestive Enzymes Activity to Starch)

  • 권오남;박흠기
    • 한국양식학회지
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    • 제22권1호
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    • pp.105-111
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    • 2009
  • 본 연구는 rotifer가 가진 소화효소환성과 영양적인 측면에서 자어의 소화력을 평가하기 위한 실험을 하였다. 그래서 rotifer의 소화력을 증가시켜 주기 위해 배양수에 starch를 첨가하여 rotifer (starch-rotifer)의 소화효소 활성을 향상시켰으며 지질 영양강화 rotifer (CE-rotifer)와 비교하여 넙치자어를 이용하여 먹이효율 실험을 하였다. 이들 rotifer의 소화효소 (lipase 제외), 총 단백질, 필수아미노산 총량, 필수아미노산(methionin과 phenylalanine)에서 starch-rotifer가 높게 나타났다. 하지만 총지질, 지질 클래스(sterol 제외)및 DHA, EPA와 같은 지방산은 CE-rotifer에서 높게 나타났다. 그러나 sterol과 ST/TG 비는 starch-rotifer에서 유의적으로 높게 나타났다P<0.05). 이 두 가지 rotifer를 공급받은 넙치자어는 부화 후 6일까지 체장과 체중에서 $3.72{\sim}3.79\;mm$$32.9{\sim}37.8\;mg$/larva의 범위로 유의적인 차이가 없었다(P>0.05). 그러나 부화 후 12일째는 CE-넙치에서 starch-넙치가 보다 높은 $5.94{\pm}0.249\;mm$, $144.0{\pm}23.86\;mg$/larva 및 $26.2{\pm}2.13%$의 생존율을 보였다. 이들 두 rotifer를 공급받은 넙치자어의 가수분해 효소 활성은 부화 후 5일째 acidic -amylase, neutral -amylase, TG-lipase, lysozyme 및 acidic Phosphatase에서 starch-넙치에서 유의적으로 높게 조사되었으나, 부화 후 11일째는 CE-넙치의 neutral $\alpha$-amylase, three pretenses, two phosphatases에서 starch-넙치보다 유의적으로 높은 활성을 보였다. 결과적으로 넙치자어는 부화 후 6일까지 영양강화 rotifer를 공급하는 것보다 소화효소 활성을 향상시킨 먹이를 공급하는 것이 자어의 소화력 측면에서 유익하며, 이후 소화기관의 발달로 영양의 흡수가 원활해져서 영양강화 효과가 자어의 성장으로 나타났다고 판단된다. 따라서 이후 소화효소활성과 영양의 측면에서 부화 후 6일 이후에 대한 상세한 고찰이 필요할 것으로 판단된다.

Cerulein 유도 급성췌장염 마우스모델에서 자가분해 조절과 항산화 활성에 미치는 [6]-gingerol의 영향 ([6]-Gingerol Attenuates Autophagy and Increases Activities of Antioxidative Defense Enzymes in Mice with Cerulein-induced Acute Pancreatitis)

  • 김성옥;최영현
    • 생명과학회지
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    • 제23권10호
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    • pp.1280-1287
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    • 2013
  • 열대아시아 원산의 다년생 초본 생강의 주성분인 [6]-gingerol은 항산화 및 항염증 등의 특성이 잘 알려져 있지만 cerulein 유도 급성췌장염에서의 자가분해 관련 유전자 발현 조절과 항산화 효소 활성에 대한 연구는 거의 없다. 본 연구에서는 cerulein 유도 급성췌장염 동물모델에서 [6]-gingerold의 자가분해 조절과 항산화 작용을 조사하였다. 급성췌장염 유발 전 4일 동안 [6]-gingerol (0.1 mg/20 g mouse/day)을 경구투여 한 후 $50{\mu}g/kg$ cerulein을 복강주사로 급성 췌장염을 유도하였다. 그 결과 혈중 ${\alpha}$-amyase 활성, 자가분해 표적 유전자(Beclin-1 및 cleaved LC3-II)의 발현, 지질과산화는 [6]-gingerol 투여군에서 유의적으로 감소하였으며, 항산화지표 효소인 SOD와 GSH-Px 활성은 [6]-gingerol 투여군에서 유의적으로 증가하였다. 이상의 결과들은 천연식물소재 생강의 유효성분 중 하나인 [6]-gingerol이 cerulein 유도 급성 췌장염에서 자가분해 조절과 감소된 항산화효소 활성을 강화하는 효과를 나타내므로 생강이 급성췌장염의 예방과 치료에 대한 기능성 식품소재로 그 활용이 매우 높을 것으로 사료된다.

흑국균(黑麴菌)의 인공변이(人工變異)에 관(關)한 연구(硏究) (Studies on the Mutation of Aspergillus niger)

  • 박윤중;손천배
    • 한국식품과학회지
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    • 제14권1호
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    • pp.72-79
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    • 1982
  • Aspergillus niger CF를 최초(最初)의 균주(菌株)로 하고 이것에 자외선조사처리(紫外線照射處理)를 하여 돌연변이균주(變異菌株) Asp. niger CF-11을 얻었으며 이어서 NTG 처리(處理)에 의(依)하여 Asp. neger CF-11 균주(菌株)에서 변이균주(變異菌株) Asp. niger CF-22 및 CF-21를 분리(分離)하였다. 변이균주(變異菌株)의 특징(特徵)을 조사(調査)하고 밀기울국(麴) 및 밀가루국(麴)에서의 효소생산(酵素生産) 및 산생성(酸生成)을 검토(檢討)한 결과(結果)는 아래와 같다. 1. Asp. niger CF-22 변이균주(變異菌株)는 포자두(胞子頭)의 색(色)이 변(變)한 tan type의 균주(菌株)였으며 CF-22는 최초(最初)의 친주(親株) CF에 비(比)하여 밀기울국배양(麴培養)의 최적조건(最適條件)에서 글루코아밀라아제활성(活性)이 약(約) 2배(倍), ${\alpha}-$아밀라아제활성(活性)은 약(約) 50% 증가(增加)되었다. 2. Asp. niger CF-21 변이균주(變異菌株)는 포자두(胞子頭)의 색(色)은 변(變)하지 않았으나 밀기울국(麴)에서 생육(生育)과 포자착성(胞子着性)이 최초(最初)의 친주(親株) CF보다 늦었다. 이 변이균주(變異菌株)의 산생성력(酸生成力)은 최초(最初)의 친주(親株)보다 약(約) 4배(倍) 많았다. 3. Asp. niger CF-22 변이균주(變異菌株) 및 CF-21 변이균주(變異菌株)는 최초(最初)의 친주(親株)보다 클루코아밀라아제 및 ${\alpha}-$아밀라아제활성(活性)은 증강(增强)되었으나 단백질 가수분해효소의 활성(活性)은 오히려 떨어졌다. 4. 밀기울국(麴)에서 Asp. niger CF-22 변이균주(變異菌株)의 글루코아밀아제 생성(生成)의 최적조건(最適條件)은 $30{\sim}35^{\circ}C$에서 $2{\sim}3$일간(日間)이었으며 ${\alpha}-$아밀라아제의 경우는 $30{\sim}35^{\circ}C$에서 2일간(日間)이었다. 5. Asp. neger CF-21 변이균주(變異菌株)의 산생성력(酸生成力)은 밀기울국(麴)에서 $30^{\circ}C$로 2일후(日後)에 최고(最高)에 달(達)하였으며 밀가루국(麴)에서는 $30^{\circ}C$로 3일후(日後)에 최고(最高)값을 나타내었다. 최적조건(最適條件)에서의 산생성력(酸生成力)은 밀기울국(麴)과 밀가루국(麴) 사이에 차(差)가 별(別)로 없었다.

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Distribution and Activities of Hydrolytic Enzymes in the Rumen Compartments of Hereford Bulls Fed Alfalfa Based Diet

  • Lee, S.S.;Kim, C.-H.;Ha, J.K.;Moon, Y.H.;Choi, N.J.;Cheng, K.-J.
    • Asian-Australasian Journal of Animal Sciences
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    • 제15권12호
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    • pp.1725-1731
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    • 2002
  • The distribution and activities of hydrolytic enzymes (cellulolyti, hemicellulolytic,pectinolytic and others) in the rumen compartments of Hereford bulls fed 100% alfalfa hay based diets were evaluated. The alfalfa proportion in the diet was gradually increased for two weeks. Whole rumen contents were processed into four fractions: Rumen contents including both the liquid and solid fractions were homogenized and centrifuged, and the supernatant was assayed for enzymes located in whole rumen contents (WRE); rumen contents were centrifuged and the supernatant was assayed for enzymes located in rumen fluids (RFE); feed particles in rumen contents were separated manually, washed with buffer, resuspended in an equal volume of buffer, homogenized and centrifuged and supernatant was assayed for enzymes associated with feed particles (FAE); and rumen microbial cell fraction was separated by centrifugation, suspended in an equal volume of buffer, sonicated and centrifuged, and the supernatant was assayed for enzymes bound with microbial cells (CBE). It was found that polysaccharide-degrading proteins such as $\beta$-1,4-D-endoglucanase, $\beta$-1,4-D-exoglucanase, xylanase and pectinase enzymes were located mainly with the cell bound (CBE) fraction. However, $\beta$-D-glucosidase, $\beta$-D-fucosidase, acetylesterase, and $\alpha$-L-arabinofuranosidase were located in the rumen fluids (RFE) fraction. Protease activity distributions were 37.7, 22.1 and 40.2%, and amylase activity distributions were 51.6, 18.2 and 30.2% for the RFE, FAE and CBE fractions, respectively. These results indicated that protease is located mainly in rumen fluid and with microbial cells, whereas amylase was located mainly in the rumen fluid.

MCT와 LCT가 혈청(血淸)의 효소활성(酵素活性)에 미치는 영향(影響) (Effect of Medium and Long Chain Triglyceride Diets on the Serum Enzyme Activity in the Rats)

  • 조정순
    • 한국응용과학기술학회지
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    • 제4권2호
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    • pp.57-62
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    • 1987
  • To investigate the effect of feeding rats medium-chain triglyceride(MCT), triglyceride containing primarily $C_8$ and $C_10$ fatty acids, it were compared to the effects of feeding triglycerides composed of long-chain triglyceride (LCT), corn oil and lard, on the serum enzyme activity. For 4 weeks rats fed a diet containing 20% MCT or LCT ${\cdot}$ MCT, as compared with LCT, had the following effects: 1) The total lactic dehydrogenase(LDH) activities in the serum of all experimental group were significantly decreased then those of control group. 2) The activities of glutamic oxaloacetic transaminase (GOT) in the serum of all experimental group were decreased than those of control group. 3) The activities of glutamic pyruvic transaminase (GPT) in the serum of all experimental group were decreased, MCT and LCT group were singinficantly decreased than of control group. 4) The activities of ${\alpha}-amylase$ in the serum of all groups were significantly increased than those of control group. 5) According to electrophoresis, LDH of LDH isoezyme activities in MCT and Lard group were increased with those of $LDH_5$ in corn oil group were increased than those of control gourp. It is suggested that the MCT and LCT fed to rats influence on the activity of various serum enzymes.

칼럼크로마토그라피에 의한 아스퍼질러스 계통의 .alpha.-아미라제 및 프로테아제의 결정화 1 (Crystallization of a-Amylase and Protease of Aspergillus oryzae from Columm Chromatography (I))

  • 서항원
    • 미생물학회지
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    • 제9권4호
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    • pp.163-168
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    • 1971
  • Neutral protease which was obtained from a genus of Aspergilli as the crystal form were investigated for their purification and properties. The results of biochemical and enzymatic studies for their purification and properties in this enzyme were as follows. 1) On the wheat media containing 70%-water and $CaCo_{3}$, Aspergilus oryzae S.H.W. 131 is satisfactorily grown under the basic optimum conditions temperature $27^{\circ}C$- $30^{\circ}C$at relative humidity 100% for three days. 2) The enzyme solution extracted with water is successively purified through the passing on column of Asmti-177N for decolorization of it. And ion exchanger such as DEAAE Sphadex A-50 or Shepadex G-100 and fraction collector is necessary for the sepearte treatments of this enzyme. After washing it with organic solvents as aceton-EtOH, etc., it should be dried on the vacuum dryer at $40^{\circ}C$) The protease activity is determined by the amounts of amino acids, tyrosine. 4) The optimum pH of neutral protease is 6.0-8.0. 5) In effectively decomposing with this neutral protease, the optimum temperature is $35^{\circ}C$. 6) It is interesting that the amounts of metal ion affects the activity of neutral protease. For examples, if it were treated with manganic ion, its activity would be more effective than any other that.

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Comparison of Digestive Function Among Rabbits, Guinea-Pigs, Rats and Hamsters. II. Digestive Enzymes and Hindgut Fermentation

  • Yu, Bi;Chiou, Peter Wen-Shyg;Kuo, Chung-Yi
    • Asian-Australasian Journal of Animal Sciences
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    • 제13권11호
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    • pp.1508-1513
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    • 2000
  • The aim of this trial was to study the response of laboratory animals including omnivores (rats) and herbivores (rabbits, guinea pigs and hamsters) to the same level of dietary fiber on their digestive enzymes and hindgut fermentation. Ten weanling animals of each of four species, rabbits, guinea-pigs, rats and Syrian hamster, were fed a basal diet of 18% crude protein and 10% crude fiber for six weeks. The digesta and tissue of each intestinal segment were collected to measure the activity of digestive enzymes. Rabbits contained the highest secreted pepsin activity in the stomach, whereas rats contained the highest protease and ${\alpha}-amylase$ activity in the small intestine, and lower fibrous hydrolases in the hindgut than rabbits, guinea pigs and hamsters. The total VFA productions in the caecum and colon were highest in rats, followed by hamsters and rabbits, while the guinea pigs contained the lowest VFA and a different pattern of VFA molar ratio from the other laboratory animals. The degree of hindgut fermentation in these laboratory animals was in reverse to the trend for their fiber digestion.

Development of Gastric and Pancreatic Enzyme Activities and Their Relationship with Some Gut Regulatory Peptides in Grazing Sheep

  • Xia, Lang;Cailian, Wang
    • Asian-Australasian Journal of Animal Sciences
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    • 제24권4호
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    • pp.500-508
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    • 2011
  • Forty-four Gansu Alpine Fine-wool lambs were used to study changes in the activities of three gastric and five pancreatic enzymes under grazing conditions between 0 and 56 days of age. The lambs were slaughtered on days 0, 3, 7, 14, 21, 28, 42 and 56, the abomasal contents, mucosa and pancreas were immediately removed and placed into liquid nitrogen and enzyme activities were determined. Gastric enzyme (chymosin, pepsin and pregastrc esterase) activities were relatively high at birth, especially chymosin, but decreased quickly between day 0 and 21. The activity of pepsin changed insignificantly with increasing age. There was no significant change in the pancreatic enzyme activities (trypsin, chymotrypsin, ${\alpha}$-amylase, lipase and lactase). The activity of trypsin was relatively higher than that of the other pancreatic enzymes, and lactase activity was low. These ontogenic patterns might be under the control of many gut regulatory peptides, the plasma concentrations of which changed simultaneously. Some gastric and pancreatic enzymes were correlated with plasma concentrations of these gut regulatory peptides.

자동산화 Methyl Linoleate가 Mouse혈청의 효소활성에 미치는 영향 (급성 독성) (The Effect of Autoxidized Methyl Linoleate on the Serum Enzyme Activity in the Mouse (Acute Toxicity))

  • 백태홍;정낙승
    • 한국응용과학기술학회지
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    • 제1권1호
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    • pp.23-31
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    • 1984
  • In order to investigate the acute toxicity of autoxidized methyl linoleate(AOML) on the activity of serum enzymes in the mouse, we administered once 0.45ml of AOML to ICR strain mouse by using stomach tube. The following results were obtained: The total lactic dehydrogenase(LDH) activities in the serum of AOML group were generally increased than those of normal group. According to electrophoresis, the activities of LDH, were increased while those of LDH, were decreased. The activities of glutamic oxaloacetic transaminase(GOT), glutamic-pyruvic transaminase(GPT) and ${\alpha}-amylase$ in the serum of AOML group were increased more than those of normal group. The activities of alkaline phosphatase in the serum of AOML group were increased but those of isozyme were not confirmed in the normal and AOML group. In the serum protein of AOML group, albumin was increased, on the other hand ${\gamma}-globulin$ was decreased. At the peripheral blood slide smear, lymphocytes were significantly decreased but neutrophils were increased and the morphological change of erythrocytes was observed. From these results we conclude that the AOML fed to mouse influences on the activity of various serum enzymes and blood cells in the mouse.