• 제목/요약/키워드: ${\beta},D-glucosidase$

검색결과 89건 처리시간 0.026초

Metabolic Activities of Ginseng and Its Constituents, Ginsenoside Rb1 and Rg1, by Human Intestinal Microflora

  • Choi, Jong-Ryul;Hong, Sung-Woon;Kim, Yu-Ri;Jang, Se-Eun;Kim, Nam-Jae;Han, Myung-Joo;Kim, Dong-Hyun
    • Journal of Ginseng Research
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    • 제35권3호
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    • pp.301-307
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    • 2011
  • To evaluate the difference in expressing pharmacological effects of ginseng by intestinal microflora between Koreans, metabolic activities of ginseng, ginsenoside $Rb_1$ and $Rg_1$ by 100 fecal specimens were measured. The ${\beta}$-glucosidase activity for p-nitrophenyl-${\beta}$-D-glucopyranoside was 0 to 0.42 mmol/min/mg and its average activity (mean${\pm}$SD) was $0.10{\pm}0.07$ mmol/min/mg. The metabolic activities of ginsenosides Rb1 and Rg1 were 0.01 to 0.42 and 0.01 to 0.38 pmol/min/mg, respectively. Their average activities were $0.25{\pm}0.08$ and $0.15{\pm}0.09$ pmol/min/mg, respectively. The compound K-forming activities from ginsenoside Rb1 and ginseng extract were 0 to 0.11 and 0 to 0.02 pmol/min/mg, respectively. Their average compound K-forming activities were $0.24{\pm}0.09$ pmol/min/ mg and $2.14{\pm}3.66$ fmol/min/mg, respectively. These activities all were not different between males and females, or between ages. Although compound K-forming activity from the aqueous extract of ginseng was low compared to that from ginenoside $Rb_1$, their profiles were similar to those of isolated compounds. Based on these findings, we believe that the intestinal bacterial metabolic activities of ginseng components are variable in individuals and may be used as selection markers for responders to ginseng.

Effect of Diet on Enzyme Profile, Biochemical Changes and In sacco Degradability of Feeds in the Rumen of Buffalo

  • Kamra, D.N.;Saha, Sudipto;Bhatt, Neeru;Chaudhary, L. C.;Agarwal, Neeta
    • Asian-Australasian Journal of Animal Sciences
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    • 제16권3호
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    • pp.374-379
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    • 2003
  • Four rumen fistulated Murrah buffaloes were used to study the effect of four diets differing in roughage to concentrate ratio on rumen biochemical changes, microbial enzyme profile and in sacco degradability of feed in a $4{\times}4$ Latin Square design. The animals were fed four diets consisting of 80:20, 70:30, 60:40 and 50:50 ratios of wheat straw and concentrate mixtures, respectively. Wheat straw and concentrate mixture were mixed with water (0.6 l/kg feed) and complete feed mixture was offered to the animals at 8:00 h and 16:00 h in two equal parts. The variation in pH of rumen liquor (difference of maximum and minimum during 0-8 h post feeding) increased with increasing level of concentrate mixture in the diet. There was no effect of diet composition on volatile fatty acids, total nitrogen and trichloro-acetic acid precipitable nitrogen in the rumen liquor, but ammonia nitrogen increased with increasing level of concentrate mixture in the ration. Major portions of all fibre degrading enzymes were present in the particulate material (PM) of the rumen contents, but protease was absent in PM fraction. The activities of micro-crystalline cellulase, acetyl esterase and protease increased with increase in the level of concentrate mixture, but the activities of other enzymes (carboxymethylcellulase, filter paper degrading activity, xylanase, $\beta$-glucosidase and $\beta$-xylosidase) were not affected. The in sacco degradability and effective degradability of feeds increased with increasing level of concentrate mixture in the ration.

Kinetics of a Cloned Special Ginsenosidase Hydrolyzing 3-O-Glucoside of Multi-Protopanaxadiol-Type Ginsenosides, Named Ginsenosidase Type III

  • Jin, Xue-Feng;Yu, Hong-Shan;Wang, Dong-Ming;Liu, Ting-Qiang;Liu, Chun-Ying;An, Dong-Shan;Im, Wan-Taek;Kim, Song-Gun;Jin, Feng-Xie
    • Journal of Microbiology and Biotechnology
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    • 제22권3호
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    • pp.343-351
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    • 2012
  • In this paper, the kinetics of a cloned special glucosidase, named ginsenosidase type III hydrolyzing 3-O-glucoside of multi-protopanaxadiol (PPD)-type ginsenosides, were investigated. The gene (bgpA) encoding this enzyme was cloned from a Terrabacter ginsenosidimutans strain and then expressed in E. coli cells. Ginsenosidase type III was able to hydrolyze 3-O-glucoside of multi-PPD-type ginsenosides. For instance, it was able to hydrolyze the 3-O-${\beta}$-D-(1${\rightarrow}$2)-glucopyranosyl of Rb1 to gypenoside XVII, and then to further hydrolyze the 3-O-${\beta}$-D-glucopyranosyl of gypenoside XVII to gypenoside LXXV. Similarly, the enzyme could hydrolyze the glucopyranosyls linked to the 3-O-position of Rb2, Rc, Rd, Rb3, and Rg3. With a larger enzyme reaction $K_m$ value, there was a slower enzyme reaction speed; and the larger the enzyme reaction $V_{max}$ value, the faster the enzyme reaction speed was. The $K_m$ values from small to large were 3.85 mM for Rc, 4.08 mM for Rb1, 8.85 mM for Rb3, 9.09 mM for Rb2, 9.70 mM for Rg3(S), 11.4 mM for Rd and 12.9 mM for F2; and $V_{max}$ value from large to small was 23.2 mM/h for Rc, 16.6 mM/h for Rb1, 14.6 mM/h for Rb3, 14.3 mM/h for Rb2, 1.81mM/h for Rg3(S), 1.40 mM/h for Rd, and 0.41 mM/h for F2. According to the $V_{max}$ and $K_m$ values of the ginsenosidase type III, the hydrolysis speed of these substrates by the enzyme was Rc>Rb1>Rb3>Rb2>Rg3(S)>Rd>F2 in order.

Substrate reduction therapy as a new treatment option for patients with Gaucher disease type 1: A review of literatures

  • Sohn, Young Bae;Yoo, Han-Wook
    • Journal of Genetic Medicine
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    • 제13권2호
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    • pp.59-64
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    • 2016
  • Gaucher disease type 1 (GD1) is an inherited lysosomal storage disorder caused by deficiency of acid ${\beta}$-glucosidase. The diminished enzyme activity leads to the accumulation of substrates and results in multi-systemic manifestations including hepatosplenomegaly, anemia, thrombocytopenia, and bone diseases. Enzyme replacement therapy (ERT) by infusion of recombinant protein has been the standard treatment for over 20 years. Despite the successful long-term treatment with ERT, several unmet needs remain in the treatment of GD1 such as severe pulmonary and skeletal manifestations. Substrate reduction therapy (SRT) reduces the accumulation of substrates by inhibiting their biosynthesis. Eliglustat, a new oral SRT, was approved in United States and Europe as a first-line therapy for treating adult patients with GD1 who have compatible CYP2D6 metabolism phenotypes. Although eliglustat is not yet available in Korea, introduction and summary of this new treatment modality are provided in this paper by review of literatures. Despite the fact that there are only limited studies to draw resolute conclusions, the current data demonstrated that eliglustat is not inferior to ERT in terms of its clinical efficacy. The approval of eligustat enables eligible adult GD1 patients to have the option of oral therapy although it still needs further studies on long-term outcomes. The individual patient should be assessed carefully for the choice of treatment modality when eliglustat becomes available in Korea. Furthermore, the clinical guidelines for Korean patients with GD1 regarding the use of eliglustat needs to be developed in near future.

종이의 산성화가 미생물의 분해능에 미치는 영향 (Effect of the paper acidity on the cellulolytic activity of fungi)

  • 한성희;이규식;정용재;이혜윤
    • 보존과학연구
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    • 통권19호
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    • pp.3-22
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    • 1998
  • The effect of pH on degradation of paper by some fungi, which able to degrade cellulose, was investigated. Trichoderma koningii, Aspergillus nigerand Penicillium nigulosum were cultured at $28^{\circ}C$ for 16 days in the selective medium (PH3, PH4, PH5, PH6, PH7, PH8, PH9, PH10, PHC) containing paper as substrate. Each paper was pretreated with each pH buffer (pH 3∼pH 10, D.W.)prior to addition to the selective medium. Enzyme activities in the each culture medium were measured spectroph to metrically using C.M.C., Avicel, PNPG as the substrates for endoglucanase, exoglucanase and $\beta$-glucosidase, respectively. In all experimental fungi, the enzyme activities of PH3 and PH9 medium were usually much higher than those of other experimental groups. However in the PH6medium, enzyme activity was lower than other groups. To analyze the concentration and pattern of protein in the each culture medium, the medium was concentrated by lyophilization. The protein concentration of PH3 and PH9 medium were relatively high (T.koningii; 6.31mg, 6,19mg, A.niger; 1.62mg, 1.96mg, P.nigulosum;2.50mg, 2.73mg, respectively), but that of PH6 was relatively low. The protein pattern of each medium was analyzed by using SDS-PAGE and VDS Image Master Analysis Program. The concentrations of bands in the each lane were usually high at lane2 (PH3) and lane8 (PH9) and low at lane5 (PH6). Therefore, the incresed cellulolytic activity of fungus against acidified paper could be result of structural change and deterioration of paper caused by being acidified.

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전통메주로부터 대두단백질 가수분해효소 생산성 미생물의 분리 및 동정 (Isolation and Identification of Microorganisms Producing the Soy Protein-Hydrolyzing Enzyme from Traditional Mejus)

  • 강민정;김성호;주현규;이갑상;임무현
    • Applied Biological Chemistry
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    • 제43권2호
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    • pp.86-94
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    • 2000
  • 대두 단백질의 효소적 가수분해에 의한 분해물의 맛과 향을 개선시킬 수 있는 효소적 가수분해 system을 확립하기 위하여, 전통메주로부터 대두단백질 분해능이 우수한 균주를 분리하여, 분해 양상이 상이한 효소를 생산하는 곰팡이와 세균 3균주를 선별하여 동정을 실시하였다. 단백질 분해능이 우수한 균주 중 곰팡이 M4는 leucine 활성이, 곰팡이 M5는 azodye 활성이 높았으며, 세균은 leucine활성이 가장 낮은 B16을 선별하여 효소의 작용에 의한 대두 단백의 분해 양상이 상이한 균주로 분리하였다. 분리한 곰팡이 M4는 배양배지에서 균사는 백색이었으며 균핵은 흰색에서 검은 색으로 변화하였다. Slide배양 결과, 분생자두는 방사형이었고, 정낭은 곤봉형이었다. 분생자는 반구형으로 기경자와 단경자가 존재하였다. 분생자병은 무색으로 매끈한 표면이었다. 분류학상 Aspergillus oryzae(ahlburg)종의 특징과 유사하여 이 종으로 분류 동정하고 Aspergillus oryzae M4로 명명하였다. 곰팡이 M5는 MEA배지에서 흰색과 검은색의 균사가 혼재되어 있었다. Slide배양 결과, 회녹색의 균총과 긴(7 mm) 포자낭병이 존재하였다. 포자낭은 회갈색이었고, 큰 포자낭과 기저막에서 작은 포자낭들이 떨어져 나오는 형태를 보였다. 중축은 구형으로 절단된 유리질의 형태이었고, 포자낭 포자는 직경이 작은$(80\;{\mu}m)$ 타원형이었다. 따라서 분류학상 접합균의 Mucor circinelloides의 종과 유사하여 이 종으로 분류 동정하고 Mucor circinelloides M5라 명명하였다. 세균 B16은 백색의 불투명한 colony로서 circular, lobate한 형태였고, 간상형으로 내생포자를 함유하였다. 또한, gram염색, catalase, oxidase, ${\beta}-glucosidase$, V-P test 등에서 양성이었고, D-fructose, ${\alpha}-D-glucose$, maltose, D-mannose, D-raffinose, stachyose, sucrose등의 이용성이 있었다. B16의 형태학적, 생리학적인 특징의 결과, Bacillus megaterium의 특징과 일치하였다. 그러나, 균체 지방산은 Paenibacillus marcerans의 균종과 유사하여 B16은 더 자세한 동정방법과 분류체계를 통해 명확한 동정이 필요하리라 사료되었다. 따라서 B16은 잠정적으로 Bacillus megaterium B16이라 명명하였다.

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김치 분리균인 Bacillus sp. JK-43이 생산하는 Cyclodextrin Glucanotransferase의 생산 및 특성 (Production and Characterization of Cyclodextrin Glucanotransferase fronm Bacillus sp. JK-43 Isolated from Kimchi)

  • 전홍기;배경미;김영희;백형석
    • 한국식품영양과학회지
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    • 제29권1호
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    • pp.41-48
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    • 2000
  • 김치 시료로부터 자동산화되지 않으며 열 및 중성 pH에서 안정한 AA 유도체인 AA-2G를 생산할 수 있는 당전이활성을 가진 CGTase 생산균주를 분리하였고, 분리균주의 형태학적, 배양학적, 생리학적 성질 및 16s-rDNA sequences를 조사한 결과 그람 양서의 간균으로 호기성이며 내생포자를 형성하는 전형적인 중온성 Bacillus sp. JK-43으로 동정되었다. Bacillus sp. JK-43의 CGTase는 AA-2G 뿐만 아니라 AA-6G로 추정되는 물질을 함께 생산하였으며, 효소 최적생산조건은 1.0% soluble starch, 1.0% yeast extract, 1.0% $Na_2CO_3\;0.1%\;K_2HPO_4,\;그리고\;0.02%\;MgSO_4{\cdot}7H_2O$가 함유된 배지에서 pH 7.0, $37^{\circ}C$에서 26시간 동안 진탕배양하였을 때였다. 각종 당공여채에 따른 Bacillus sp. JK-43의 AA-2G 생산성을 조사한 결과 ${\beta}-CD$에서 가장 높은 AA-2G 생산성을 보였으며, 식혜제도페액인 엿기름 및 밥당화액에서도 비교적 높은 AA-2G 생산성을 보였다. 또한 여러 가지 당수용체에 대한 JK-43의 CGTase의 당전이 반응을 검토한 결과 sucrose, mannitol 및 inositol에서 높은 당전이 수율인 70~90%를 나타내었다.

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Bacillus coagulans NRR1207이 생산하는 α-galactosidase에 의한 대두박 비소화성분의 가수분해 (Hydrolysis of Non-digestible Components of Soybean Meal by α-Galactosidase from Bacillus coagulans NRR1207)

  • 라석한;렌친핸드;박민길;김완섭;백승희;남명수
    • 생명과학회지
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    • 제28권11호
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    • pp.1347-1353
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    • 2018
  • 본 연구는 한국전통약용식물(구기자, 오미자 잎)의 발효물로부터 분리한 Bacillus coagulanse NRR1207의 발효 특성을 파악하고 Bacillus coagulans NRR1207의 ${\alpha}$-galactosidase의 활성과 이를 통한 대두박의 비소화성분의 분해를 확인하였다. Bacillus coagulans NRR1207이 생산하는 효소 중 ${\alpha}$-galactosidase, ${\beta}$-galactosidase, ${\alpha}$-glucosidase가 가장 높은 40 nmol 이상의 활성을 나타내었다. Bacillus coagulans NRR1207의 발효 특성은 10% skim milk에서 배양했을 때, pH는 급속히 감소했고 적정 산도는 1.9%까지 증가했고 생균수도 발효 24시간에 8.8 log CFU/ml로 증가했다. 유당은 배양 72시간째 완전히 고갈되었고 유산 생산 능력도 탁월했다. Bacillus coagulans NRR1207을 대두박에 접종 후 배양시간에 따른 생균수의 변화는 배양 시작 시 7.6 log CFU/ml, 배양 16시간에 최고에 도달하여 9.0 log CFU/ml이었고 배양 72시간에 8.3 log CFU/ml로 Bacillus coagulans NRR1207이 왕성하게 잘 성장하였다. 대두박의 비소화성분 분해는 Bacillus coagulans NRR1207 접종 후 발효 24, 48, 72시간이 경과하면서 이 균이 생산한 ${\alpha}$-galactosidase에 의해 비소화성분인 stachyose와 raffinose가 대부분 분해되고 galactose가 생성되었다. 따라서 Bacillus coagulans NRR1207은 대두박의 비소화성분을 분해하는 생균제(Probiotics)로써 이용하여 식품 및 가축 사료 이용성 증대에 활용이 가능할 것으로 사료된다.

한국산 마전분의 이화학적 특성 (Physicochemical Properties of Several Korean Yam Starches)

  • 김화선;김상순;박용곤;석호문
    • 한국식품과학회지
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    • 제23권5호
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    • pp.554-560
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    • 1991
  • 한국에서 재배되고 있는 긴마, 단마 및 참마에서 분리한 전분의 특성을 조사한 결과는 다음과 같다. 전분의 평균 입자크기는 각각 단마 $23.5{\mu}m$, 긴마 $23.9{\mu}m$ 및 참마 $18.2{\mu}m$로 나타났고 표면 형태는 품종에 관계없이 불규칙한 난형을 나타내었으며 입자의 표면은 매끈하였다. 마전분의 아밀로오스 함량은 $29{\sim}33%$였고 물결합력은 $109.9{\sim}118.3%$ 였으며 온도변화에 따른 광투과도는 $70{\sim}75^{\circ}C$에서 상승 현상을 나타내는데 특히 참마는 $85^{\circ}C$부근에서 double stage 형태를 나타내었다. 팽윤력과 용해도는 단마가 다소 높은 수치를 나타내었고, 5% 마전분의 아밀로그램에 의하면 $80.3{\sim}84.3^{\circ}C$의 높은 호화 개시온도로 $95^{\circ}C$에서 가열시 계속적인 점도 상승 현상을 나타내었다. 마전분에 glucoamylase를 작용시킨 결과 반응 48시간후 최고 34%의 낮은 분해율을 보인반면 DMSO에 의해서는 반응 48시간 후 최고 100%의 용해율을 나타내었다. 마전분 및 전분에서 분리, 정제한 아밀로오스와 아밀로펙틴의 ${\beta}-amylolysis limit$는 마전분의 경우 $71.8{\sim}75.5%$를 나타내었고 아밀로오스에 있어서는 $90.2{\sim}92.1%$였으며 아밀로펙틴의 경우 $63.7{\sim}66.9%$를 나타내었다. 전분을 Sepharose CL-2B column으로 겔 크로마토그라피한 결과 모두 2개의 peak로 분리되었으며 pullulanase로 마밀로펙틴의 ${\alpha}-1,6-glucosidase$결합을 가수분해시킨 후 Sephadex G-75로 겔 크로마토그라피한 결과 peak II와 peak III의 정점에서의 중합도는 각각 15와 40부근이며 peak II에 대한 peak III의 중량비는 $2.15{\sim}2.42$ 분포를 나타내었다.

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