• 제목/요약/키워드: Digestive enzymes

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Industrial Applications of Rumen Microbes - Review -

  • Cheng, K.J.;Lee, S.S.;Bae, H.D.;Ha, J.K.
    • Asian-Australasian Journal of Animal Sciences
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    • 제12권1호
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    • pp.84-92
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    • 1999
  • The rumen microbial ecosystem is coming to be recognized as a rich alternative source of genes for industrially useful enzymes. Recent advances in biotechnology are enabling development of novel strategies for effective delivery and enhancement of these gene products. One particularly promising avenue for industrial application of rumen enzymes is as feed supplements for nonruminant and ruminant animal diets. Increasing competition in the livestock industry has forced producers to cut costs by adopting new technologies aimed at increasing production efficiency. Cellulases, xylanases, ${\beta}$-glucanases, pectinases, and phytases have been shown to increase the efficiency of feedstuff utilization (e.g., degradation of cellulose, xylan and ${\beta}$-glucan) and to decrease pollutants (e.g., phytic acid). These enzymes enhance the availability of feed components to the animal and eliminate some of their naturally occurring antinutritional effects. In the past, the cost and inconvenience of enzyme production and delivery has hampered widespread application of this promising technology. Over the last decade, however, advances in recombinant DNA technology have significantly improved microbial production systems. Novel strategies for delivery and enhancement of genes and gene products from the rumen include expression of seed proteins, oleosin proteins in canola and transgenic animals secreting digestive enzymes from the pancreas. Thus, the biotechnological framework is in place to achieve substantial improvements in animal production through enzyme supplementation. On the other hand, the rumen ecosystem provides ongoing enrichment and natural selection of microbes adapted to specific conditions, and represents a virtually untapped resource of novel products such as enzymes, detoxificants and antibiotics.

Cellulase Activity of Symbiotic Bacteria from Snails, Achatina fulica

  • Kim, Jon Young;Yoon, Sae Min;Kim, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
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    • 제43권5호
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    • pp.628-640
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    • 2015
  • Cellulase is the key enzyme in the use of cellulose-based biomaterials. Because of its structure, cellulose is difficult to be degraded by enzymes. In order to utilize cellulose-based biomaterials efficiently, evolutionary wisdom of how to use enzymes accurately and harmoniously in a biological system is needed, such as the cellulose digestive system in animals. In this study, the symbiotic bacteria from snails, Achatina fulica, were identified and their cellulase activity was evaluated. The 16S rRNA sequence analysis of 100 aerobic bacteria showed that they belonged to 9 genus and almost half of the bacteria were Lactococcus spp. Among 100 identified strains, only two Aeromonas sp. strains showed cellulase activity. Aeromonas sp. KMBS020 had both endo-${\beta}$-glucanase and ${\beta}$-glucosidase activities but Aeromonas sp. KMBS018 had ${\beta}$-glucosidase activity only. None of the 100 bacterial colonies had any cellobiohydrolase activity.

Cellulose Hydrolysis by Digestive Enzymes of Reticulitermes speratus, a Native Termite from Korea

  • Lee, Young-Min;Kim, Hyun-Jung;Cho, Moon-Jung;Shin, Keum;Kim, Young-Kyoon;Kim, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
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    • 제38권2호
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    • pp.140-148
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    • 2010
  • This study was to investigate the enzymatic hydrolysis of cellulose using the cellulase from whole body of the native termite collected in Milyang-si, Kyungsangnamdo, Korea. In the results, optimal temperature and pH for the enzyme of native termites were $45^{\circ}C$ and pH 5.5 for both endo-${\beta}$-1, 4-glucanase and ${\beta}$-glucosidase. Enzyme activity of the termite enzyme was shown $8.8{\times}10^{-2}\;FPU/m{\ell}$. And the highest glucose hydrolysis rate of cellulose by the digestive enzyme from test termites was 24.5% based on the glucan, comparing 59.7% by commercial enzyme (only celluclast 1.5 L) at 1% (w/v) substrate and 36 hours in hydrolysis time. This hydrolysis rate by the digestive enzyme from test termites was comparatively high value in 41% level of the commercial enzyme. When cellulose was hydrolyzed by the digestive enzyme of the native termite, glucose hydrolysis was almost completed in 12 hours which was the considerably reduced time for cellulose hydrolysis. It was suggested that the quiet short reaction time for cellulose hydrolysis by the enzyme from native termite could be a very high advantage for development of hydrolysis cellulase for lignocellulosic biomass.

Effects of Dietary Fructooligosaccharide on Digestive Enzyme Activities, Intestinal Microflora and Morphology of Growing Pigs

  • Xu, Z.R.;Zou, X.T.;Hu, C.H.;Xia, M.S.;Zhan, X.A.;Wang, M.Q.
    • Asian-Australasian Journal of Animal Sciences
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    • 제15권12호
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    • pp.1784-1789
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    • 2002
  • One hundred and twenty-eight growing barrows (Jiaxing Black${\times}$Duroc${\times}$Landrace) at an average BW of 20.8 kg were allocated to four treatments for 42 days, each of which was replicated four times with eight pigs per replicate and used to investigate the effects of fructooligosaccharide (FOS) on digestive enzyme activities, intestinal microflora and morphology of growing pigs. The pigs received the same basal corn-soybean meal diet and FOS was added to the basal diet at 0, 2, 4, 6 g/kg diet at the expense of corn, respectively. As compared to control, supplementation with 4 and 6 g/kg FOS significantly improved average daily gain and feed efficiency. Addition of FOS enhanced the growth of Bifidobacterium and Lactobacillus, but inhibited Clostridium and Escherichia coli in the small intestinal and proximal colonic contents. Supplementation with 4 and 6 g/kg FOS significantly improved the activities of total protease, trypsin and amylase in the small intestinal contents. However, FOS had no significant effect on the activity of lipase in the small intestinal contents as well as the digestive enzymes in pancreas. Morphological measurement of jejunal mucosa did show response to consumption of FOS. Villus height and the villus height to crypt depth ratio at the jejunal mucosa were significantly higher with 4 and 6 g/kg FOS supplementation as compared to control.

황복, Takifugu obscurus, 초기 단계의 소화효소 변화 (The Changes of Digestive Enzyme Activity in Early Stages of the River Puffer, Takifugu obscurus)

  • 손군희;한경남;장정순
    • 한국수산과학회지
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    • 제34권6호
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    • pp.577-583
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    • 2001
  • 황복의 소화효소의 변화과정을 부화직후부터 부화 후 65일까지 측정 하였다. 발육단계에 따른 소화효소의 발현과 활성의 변화에서 $\alpha-amylase$ 비활성은 전장 10mm에서 0.0493U/mg의 최소값을 나타낸 후, 전장 19mm를 전후하여 0.1480 U/mg의 최대값을 나타냈다. Trypsin과 pepsin 비활성은 전장 16mm에서 각각 0.0264U/mg, 0.0258U/mg 와 전장 24mm에서 0.0178U/mg, 0.0201 U/mg의 값을 가지는 두 번의 peak를 보였고, 이 시기에 황복 자치어의 성장률도 증가하는 경향을 보였다. 또한, trypsin과 pepsin의 비활성을 비교하여 보면, 자어기인 전장 $4\~5mm$와 치어 II기인 전장 $19\~24mm$에서는 pepsin이 높았고, 치어 I 기인 전장 $11\~16mm$와 유어기인 전장27 mm 이후에서는 trypsin이 높았다.

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어류의 조직중에 분포하는 알카리성 단백질분해효소의 활성조건 (Alkaline Pretense Activity of the Tissue Extracts from Some Different Kinds of Fish)

  • 남택정;변재형
    • 한국수산과학회지
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    • 제16권2호
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    • pp.147-153
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    • 1983
  • To check the differences of the digestive enzymes by the bait habits and the proteolytic activities of the fissile extracts from the fish, omnivorous filefish (Navodon modestus), carnivorous cat shark (Scilliorhinus tarazame) and bloodsucking hag fish (Eptatretus burgeri) were sampled for this experiment. The activity of crude alkaline protease extracted from the muscle and the internal organs of the samples was determined with casein as substrate. The activity of the proteolytic enzymes showed remarkable differences by the organs of the fish. The optimum condition of the pretenses from the muscle revealed in range of pH 7.8-8.3, at $60-65^{\circ}C$, while those of the enzymes from the internal organs were at about pH 8.2, $45-55^{\circ}C$, but those of hag fish were at about pH 6.7, $45-55^{\circ}C$. The proteolytic activity of the enzyme of alimentary canal in filefish and in hag fish was 57 and 11 times stronger than that of muscle, respectively. The crude enzyme from the alimentary canal of file fish showed the strongest proteolytic activity in samples submitted and that of cat shark was the lowest. The activity of pancreatic alkaline protease in cat shark was 50 fold higher than that of muscle alkaline protease in the fish.

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Metabolism and drug interactions of Korean ginseng based on the pharmacokinetic properties of ginsenosides: Current status and future perspectives

  • Jong Dae Park
    • Journal of Ginseng Research
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    • 제48권3호
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    • pp.253-265
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    • 2024
  • Orally administered ginsenosides, the major active components of ginseng, have been shown to be biotransformed into a number of metabolites by gastric juice, digestive and bacterial enzymes in the gastrointestinal tract and also in the liver. Attention is brought to pharmacokinetic studies of ginseng that need further clarification to better understand the safety and possible active mechanism for clinical application. Experimental results demonstrated that ginsenoside metabolites play an important role in the pharmacokinetic properties such as drug metabolizing enzymes and drug transporters, thereby can be applied as a metabolic modulator. Very few are known on the possibility of the consistency of detected ginsenosides with real active metabolites if taken the recommended dose of ginseng, but they have been found to act on the pharmacokinetic key factors in any clinical trial, affecting oral bioavailability. Since ginseng is increasingly being taken in a manner more often associated with prescription medicines, ginseng and drug interactions have been also reviewed. Considering the extensive oral administration of ginseng, the aim of this review is to provide a comprehensive overview and perspectives of recent studies on the pharmacokinetic properties of ginsenosides such as deglycosylation, absorption, metabolizing enzymes and transporters, together with ginsenoside and drug interactions.

Pectinase 처리 전후의 현미의 물리적 변화 분석 (Analysis on Physical Changes of Pectinase-Treated Brown Rice (Oryza sativa))

  • 피경태;김근철
    • 생명과학회지
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    • 제23권4호
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    • pp.554-559
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    • 2013
  • 현미에는 탄수화물 뿐 아니라 비타민, 미네랄 등과 같은 영양성분이 함유되어 있다. 현미는 당뇨 등과 같은 질환관리에 매우 유용하지만, 취반 등의 어려움 등으로 대중적인 소비가 어려운 실정이다. 본 연구에서는 현미 표면에 풍부한 섬유소를 제거하기 위해 분해 효소를 이용하는 가공 방법의 가능성을 수행하였다. 일정시간 물에 담근 후 현미의 무게 변화를 측정하였을 때, 대조군 또는 collagenase 가공한 현미에 비해 pectinase 가공한 현미의 무게가 심하게 증가하는 것을 알 수 있었다. 수용액에서 현미를 침지한 후 pectinase를 처리하면 현미의 미강 부분이 거칠어지고, 미세한 구멍이 형성되는 것을 전자현미경 관찰을 통하여 확인하였다. 또한 이러한 pectinase를 이용한 현미 가공에도 불구하고 현미고유의 영양성분은 거의 완벽하게 보존되고 있음을 알 수 있었다. 한편, pectinase 가공 전후의 현미를 대상으로 수분 흡수력, 녹말 반응도의 차이를 조사하였을 때, pectinase 처리 현미에서 높은 수분흡수력, 녹말 반응도가 있음을 알 수 있었다. 이러한 결과는 기존의 현미 도정 방법에 비해 pectinase 처리에 의해 현미 가공방법은 영양성분이 보존될 뿐 아니라 식감, 미감 등에서 우수한 가공방법임을 제시할 수 있다.

메밀급여가 Streptozotocin 유발 당뇨쥐의 췌장 소화효소 활성에 미치는 영향 (Effects of Buckwheat on the Activities of Pancreatic Digestive Enzymes in Streptozotocin-Induced Diabetic Rats)

  • 이정선;이명헌;손흥수;맹영선
    • 한국식품영양과학회지
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    • 제25권5호
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    • pp.831-838
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    • 1996
  • STZ 유발 당뇨쥐에 날메밀, 볶은메밀, 찐메밀을 식이의 50%가 되도록 각각 혼합한 메밀식 이를 급여하여 2주간 사육시킨 후 변의 단백질 함량, 췌장무게, 췌장의 $\alpha-amylase,$ chymotrypsin, lipase환성 및 변의 $\alpha-amylase,$ chymotrypsin, trypsin 활성을 각각 측정하였다. 변중 단백질 함량은 당뇨대조군에 비하여 당뇨날메밀군, 당뇨볶은메밀군, 당뇨찐메밀군에서 각각 99%, 91%, 103% 유의적으로 증가하였으며 , 췌장 무게는 당뇨대조군과 비교하여 당뇨날메밀군에서 24% 유의적으로 증가하였다. 췌장의 $\alpha-amylase$ 및 lipase 환성은 당뇨대조군과 당뇨메밀군들 사이에 유의적인 차이가 없었으나 chymotrypsin 활성은 당뇨찐메밀군에서 45% 유의적으로 감소하였다. 변의 $\alpha-amylase활성은$ 당뇨대조군과 당뇨메밀군들 사이에 유의적인 차이가 없었으나, chymotrypsin 활성은 모든 당뇨메밀군들에서, trypsin 활성은 당뇨볶은메밀군에서 유의적으로 증가하였다.

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