• 제목/요약/키워드: Digestive enzyme

검색결과 199건 처리시간 0.03초

판크레아틴의 규격 표준화 연구 (Standardization of Pancreatin)

  • 신지은;윤혜경;김동현
    • Journal of Pharmaceutical Investigation
    • /
    • 제33권4호
    • /
    • pp.273-279
    • /
    • 2003
  • Pancreatin is a enzyme mixture breaking down carbohydrates, proteins and lipids. Most pancreatin used in Korea is imported from foreign countries. However, guideline of each country for pancreatin produced from each country is different. Therefore, guideline for pancreatin imported from several countries, such as Europe, Japan and America, it is standardized to control its quality. Assay of enzyme activity for pancreatin in KP is similar to tat in JP, but it is significantly different from those in FP ad in USP. We measured pancreatin digestive activities of 17 commercial products. Activity assay of digestive enzymes, starch- and lipid-digestive enzymes, for pancreatin by KP method (including JP) was difficult compared to those by FIP ad USP methods. Particularly, activity assays of starch- and lipid-digestive enzymes by KP method were mistakable, ad varied in diluted samples than those by FIP. However, activity assay of protein-digestive enzyme by KP method was similar to that by FIP. Starch-digestive enzyme activities of 17 commercial pancreatins by KP method were lower 0.079-fold compared to those by FIP method. Their protein-digestive enzyme activities by KP method were higher 75.7-fold than those by FIP method. Their lipid-digestive enzyme activities by KP method were lower 0.234-fold compared to those by FIP method.

Cellulase Production in the Digestive Organs of Reticulitermes speratus, a Native Termite from Milyang, Korea

  • Lee, Young-Min;Kim, Yoon-Hee;Cho, Moon-Jung;Shin, Keum;Kim, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
    • /
    • 제38권5호
    • /
    • pp.421-428
    • /
    • 2010
  • This study investigated on enzyme production in the digestive organs of the native termite (Reticulitermes speratus) in Milyang, Korea. Four types of major cellulases [EG (endo-1,4-${\beta}$-glucanase), BGL (${\beta}$-glucosidase), CBH (cellobiohydrolase) and BXL (${\beta}$-1,4-xylosidase)] were present in the digestive organs of the termite. The strong enzyme activity for BGL was found from the native termite, and also shown that the enzyme was distributed in the salivary gland, foregut, and hindgut. BXL, which breaks down hemicellulose near the amorphous region, was detected mainly from salivary gland, foregut, and midgut. However, CBH was distributed mainly in the hindgut. Meanwhile, EG which degrades cellulose, was found mainly in the hindgut and salivary glands. These facts indicate that celluases production patterns are differ from different sites compare to the same species found in Japan, suggesting that enzyme production in the digestive organs of termites is changed according to their habitats.

우릉쉥이(Cynthia roretzi v. Drasche)의 소화효소에 대하여 (제1보) Amylase의 효소적 성질 (Studies on the Digestive Enzyme of Cynthia roretzi V. Drasche. I . Some Enzymatic properties of Hmylase.)

  • 서석구;양한술
    • 약학회지
    • /
    • 제5권1호
    • /
    • pp.45-50
    • /
    • 1960
  • Some enzymatic properties of Cynthia roretzi v. (Drasche Korean : U-Rung-Shei) was studied by author and obtained the following results; 1. The optimum pH of the digestive gland amylase was 6.8-7.0 2. Activity of metallic ion on the amylase showed the following order; 10$^{-3}$ M M $n^{++}$>10$^{-3}$ M $Co^{++}$>10$^{-4}$ M $Mg^{++}$>10$^{-4}$ M $Ca^{++}$>10$^{-2}$ M Z $n^{++}$>10$^{-2}$ M P $b^{++}$ 3. The digestive gland enzyme inactivated at 70.deg. C. 4. When the enzyme concentration increase 2 times, the enzymatic activity also increase, but not propertionally. 5. The digestine gland amylase showed remarkably higher enzymatic activity than the intestinal amylase. 6. The digestive gland amylase from the ascidian showed remarkably higher enzymatic activity than the heptancreatic amylase from shell fish (Turbo (Batillus) Cornutus Solander).nder).nder).

  • PDF

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
    • /
    • 제38권2호
    • /
    • pp.140-148
    • /
    • 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.

우릉쉥이(Cynthia roretzi v. Drasche)의 소화효소에 대하여 (제2보) Proteinase의 효소적 성질 (Studies on the Digestive Enzyme of Cynthia roretzi V. Drasche. II. Some propeinic properties of Amylase.)

  • 서석수;양한석
    • 약학회지
    • /
    • 제5권1호
    • /
    • pp.51-55
    • /
    • 1960
  • Some enzymatic properties of Cynthia roretzi V. Drasche (Korean:U-Rung-Shei) was studied by author and obtained the following results; 1. The optimum pH of the digestive gland proteinase ws 7.4-7.6 2. Activity of metallic ion on the Proteinase showed following order; 10$^{-3}$ M. M $n^{++}$>1-$^{-3}$ M. $Co^{++}$>10$^{-4}$ M. $Mg^{++}$\ulcorner10$^{-2}$ M.S $r^{++}$. Inhibition of metallic ion on the Proteinase showed following order: 10$^{-3}$ M. A $g^{+}$>10$^{-3}$ M. c $d^{++}$>10$^{-3}$ M. P $b^{++}$>10$^{-3}$ M. Z $n^{++}$ 3. The digestive gland enzyme inactivated at 70.deg. C, but no influence at 50.deg. C. 4. When the enzyme concentration increase 2 times, and 3 times, the enzymatic activity also increase, but not proportionally 5. The digestive gland Proteinase showed remarkably higher enzymatic activity than the intestinal Proteinase. 6. The digestive gland amylase brom the ascidion showed remarkably higher enzymatic activity than the heptaponcreatic amylase from shell fish (Turbo (Batillus) Cornutus Solander).).er).).).er).).

  • PDF

이매패류 3종의 당면체 소화효소 활성 (Digestive Enzyme Activity within Crystalline Style in Three Species of Bivalves)

  • 주선미;권오남;김재원;이정식
    • 한국패류학회지
    • /
    • 제27권1호
    • /
    • pp.9-14
    • /
    • 2011
  • 연구는 3종의 이매패류를 대상으로 당면체의 소화효소 활성에 대해 조사하였다. 본 연구에 사용된 이매패류는 꼬막(n=61), 지중해담치 (n=30) 및 개조개 (n=30) 이며, 이들은 한국 남해안에서 2010년 5월에 채집하였다. 당면체의 소화 효소 활성 분석은 분광광도계를 이용하였다. 꼬막, 지중해담치, 개조개의 당면체를 구성하는 소화효소는 amylase와 cellulase가 약 90%로 대부분을 차지하였다. 그리고 꼬막, 지중해담치, 개조개의 당면체를 구성하는 소화효소 중 protease 의 활성도가 가장 낮았으며, 각각 0.02, 0, 0.08%로 나타났다. 당면체를 구성하는 소화효소 활성도는 3종 모두 cellulase > amylase > chitinase > laminarinase의 순으로 나타났다.

Lack of any Association between Insertion/Deletion (I/D) Polymorphisms in the Angiotensin-converting Enzyme Gene and Digestive System Cancer Risk: a Meta-analysis

  • Liu, Jin-Fei;Xie, Hao-Jun;Cheng, Tian-Ming
    • Asian Pacific Journal of Cancer Prevention
    • /
    • 제14권12호
    • /
    • pp.7271-7275
    • /
    • 2013
  • Objective: To investigate the association between the gene polymorphisms of angiotensin-converting enzyme (ACE) and digestive system cancer risk. Method: A search was performed in Pubmed, Medline, ISI Web of Science and Chinese Biomedical (CBM) databases, covering all studies until Sep 1st, 2013. Statistical analysis was performed by using Revman5.2 and STATA 12.0. Results: A total of 15 case-control studies comprising 2,390 digestive system cancer patients and 9,706 controls were identified. No significant association was found between the I/D polymorphism and digestive cancer risk (OR=0.93, 95%CI = (0.75, 1.16), P=0.53 for DD+DI vs. II). In the subgroup analysis by ethnicity and cancer type, no significant associations were found for the comparison of DD+DI vs. II. Results from other comparative genetic models also indicated a lack of associations between this polymorphism and digestive system cancer risks. Conclusions: This meta-analysis suggested that the ACE D/I polymorphism might not contribute to the risk of digestive system cancer.

Effects of Supplementing Different Levels of a Commercial Enzyme Complex on Performance, Nutrient Availability, Enzyme Activity and Gut Morphology of Broilers

  • Yuan, Jiu;Yao, Junhu;Yang, Fengxia;Yang, Xiaodan;Wan, Xinjie;Han, Jincheng;Wang, Yaojie;Chen, Xinke;Liu, Yurui;Zhou, Zhenfeng;Zhou, Ningbo;Feng, Xinyu
    • Asian-Australasian Journal of Animal Sciences
    • /
    • 제21권5호
    • /
    • pp.692-700
    • /
    • 2008
  • A trial was conducted to study the influence of different levels of a commercial enzyme complex on performance, nutrient availability, blood parameters, digestive tract measurements, amylase and trypsin activity of the digestive tract and gut morphology in broilers fed the typical diets in north China. There were four treatments: the control diet and the other three enzyme complex supplemented diets which were 180 mg/kg, 360 mg/kg and 720 mg/kg enzyme complex supplemented to the control diet, respectively. The birds fed the diets supplemented with 180 mg/kg and 360 mg/kg enzyme complex had better performance and nutrient availability, the activities of amylase and trypsin in the digestive tract in the two treatments were improved, the villus height and surface area of villus in the small intestine increased and the crypt depth and epithelial thickness of small intestine decreased. Relative weights of pancreas and relative weights and lengths of small intestine decreased. However, the addition of 720 mg/kg enzyme complex had no effects on these parameters and increased crypt depth and epithelial thickness of the small intestine. The data suggested that suitable supplementation of enzyme complex was beneficial for the birds, while excess enzyme complex inhibited secretion of endogenous enzyme and destroyed the structure of the small intestine.

Effects of Nutritional Level on Digestive Enzyme Activities in the Pancreas and Small Intestine of Calves Slaughtered at Same Body Weight

  • Wang, X.B.;Ogawa, T.;Suda, S.;Taniguchi, K.;Uike, H.;Kumagai, H.;Mitani, K.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • 제11권4호
    • /
    • pp.375-380
    • /
    • 1998
  • Six Holstein heifer calves weaned at 45 days-of-age were randomly allocated into high daily gain (1.1 kg/d, HDG) and low daily gain (0.56 kg/d, LDG) groups, and were slaughtered at 170 kg of live weight. Energy intake level in the feeding period was 2.4 $\times$ maintenance in 105 days for HDG and 1.4 $\times$ maintenance in 216 days for LDG calves. Total length of the small intestine was identical between groups, but both weights of the pancreas and of the small intestinal mucosa were greater (p < 0.01) for HDG calves. Alpha-amylase, lipase, proteinase, and trypsin activities of the whole pancreas were higher (p < 0.05) in HDG calves. Disaccharidase activity of the whole small intestinal mucosa was also higher (p < 0.10) for HDG than for LDG calves. However, the enzymatic activities, expressed as per gram or per protein of the pancreas and the small intestinal mucosa, were not affected (p > 0.10) by the plane of nutrition. These results suggest that the digestive enzyme activity in the small intestine varies primarily with the weight of tissues synthesizing the enzyme.

계의 췌장소화효소 분비에 미치는 사료성분에 관한 연구 (Dietary Factors for Secretary Digestive Enzyme from the Pancreas in the Chicken)

  • 양성익
    • 한국가금학회지
    • /
    • 제16권4호
    • /
    • pp.219-232
    • /
    • 1989
  • 본 연구는 닭에 있어서 사료성분에 대한 췌장소화효소(amylase. trypsinogen 및 chymotrypsinogen) 분비기구에 대해서 검토했다. 먼저, 췌효소분비의 단기응답실험에 유용한 새로운 췌액채취법을 개발했다. 이 방법을 이용해서 아미노산 및 glucose를 날개정맥으로 투여한 결과 phenylalanine만이 trypsinogen 및 Chymotrypsinogen이 증가되었지만 그 외의 아미노산 및 glucose에 의해서는 분비증가 효과가 없었다. Cholecystokinin(CCK)투여 에 의해 췌효소분필는 즉각적으로 높은 분비반응을 보였으며, 이 반응은 또한 농도의존성을 나타냈다. CCK투여는 chymotrypsinogen의 쪽이 amylase 및 trypsinogen보다 높은 비율로 분비되는 선택적인 분비반응을 나타냈다. 아미노산과 CCK을 공동투여하면 첨가한 아미노산의 종류에 따라 췌효소분비반응은 여러 가지 형태로 증가되었지만 glucose와의 공동투여에서는 CCK 단독투여와 비교해서 차가 없었다. Valine과 arginine을 여러 가지 농도로 CCK와 공동 투여한 결과, valnine에서는 0.5mM일때, arginin에서는 5mM일때 가장 높은 분비반응을 보였다. 위의 결과로부터 아미노산의 조합에 의한 췌효소분비반응에 대해서 검토했다. 즉, 아미노산 mixture, threonine+phenylalanine+isoleucine, Threonine+phenylalanine, threonine+isoleucine 및 phenylalanine+isoleucine과 CCK를 공동투여 했다. 각 물질을 투여한 후 50분간 분비한 효소를 비교하면, threonine+phenylalanine에 의한 췌효소분비반응은 아미노산 mixture에 의한 분비반응과 동일하게 높은 반응을 보였다. 이상의 결과로부터 닭에 있어서 췌장소화효소분비는 CCK와 아미노산의 사이에 협동작용이 있으며, 그 협동작용은 아미노산의 종류에 따라 선택적인 분비반응을 함으로써 장내소화가 진행된다고 본다.

  • PDF