• 제목/요약/키워드: cellulase complex

검색결과 55건 처리시간 0.024초

Characterization of an Extracellular Cellulose-Hydrolyzing Enzyme Complex from a Thermotolerant Strain of Aspergillus sp.

  • Lusta, Konstantin A.;Chung, Il-Kyung;Sul, Ill-Whan;Park, Hee-Sung;Shin, Dong-Ill
    • Journal of Microbiology and Biotechnology
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    • 제9권6호
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    • pp.873-876
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    • 1999
  • Aspergillus sp. CX-l strain grown on microcrystalline cellulose resulted in the accumulation of high levels of cellulase and xylanase activities that were higher by two to four folds than those from the conventional commercial producer, Trichoderma reesei QM9414. Aspergillus sp. CX-1 demonstrated greater thermo stability and better catalytic characteristics of total cellulase activity (FPase) as compared to T. reesei and Aspergillus niger F-2039.

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섬유소-펙틴 분해력이 있는 새로운 Aspergillus tubingensis의 분리와 특성 규명 (Isolation and Characterization of a Novel Aspergillus tubingensis with a Hydrolyzing Activity of Cellulose-pectin Complex)

  • 김영민;서원숙;홍진영;최홍서;김주환
    • 한국미생물·생명공학회지
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    • 제31권2호
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    • pp.124-128
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    • 2003
  • 대전광역시 근교의 야산과 들판 등지에서 썩은 나뭇잎, 짚, 흙을 채취하여 각각을 배양한 다음 Congo red test에 의해 cellulase 활성을 보이는 균주를 선별하였다. Genomic DNA를 분리한 후 PCR을 수행하여 DNA sequence를 Gene Bank를 통해 분석한 결과 A. tubingensis로 밝혀졌다. 이것을 배양하여 상등액을 crude enzyme으로 사용하여 온도와 pH를 달리하면서 효소의 활성정도를 측정하였다. 대조균주로 A. oryzae KCTC 6291를 이용하였고, 본 연구를 통하여 분리한 균주인 A. tubingensis가 생산하는 cellulase는 A. oryzae의 cellulase에 비하여 각각 다른 온도와 pH에서 높은 안정성을 보여주었다. A. tubingensis는 각각의 온도에서 활성의 정도가 비슷했으며, 45$^{\circ}C$, 55$^{\circ}C$에서 높은 활성을 나타내고 있지만, 고르게 활성이 나타났다. 또한 pH 12.0에서 가장 높은 활성을 보여 주었고, pH 2.0, 3.0, 4.0에서는 양쪽 모두 거의 활성이 없었으며, 중성, 염기성에 대해서 활성에는 큰 변화가 없었다. 따라서, 분리 동정한 A. tubingensis는 온도와 pH에서 고르게 활성을 나타내므로 생균제로 활용할 수 있는 범위가 클 것으로 여겨진다.

동양달팽이 Nesiohelix samarangae 소화관에서의 cellulase 활성에 대한 세포화학적 및 면역세포화학적 연구 (Cytochemical and Immunocytochemical Study on the Cellulase Activity in the Digestive Tract of the Land Snail Nesiohelix)

  • 정계헌;이용석;김은정
    • 한국패류학회지
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    • 제14권2호
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    • pp.149-159
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    • 1998
  • In order to observe the anticellulolytic localization in the epithelia of the digestive tract such as esophagus, crop, and intestine of a Korean land snail N. samarangae, a cytochemical method and a immunogold labelling method were applied. For the cytochemical study on the cellulase activity, Benedict reaction method applied. And for the immunocytochemical study, the rabbit serum immunoglobuins (IgG) was obtained from the rabbits injected with cellulase which was extracted from body fluid of the snail. The digestive tract tissues of N. samarangae were fixed with 4% paraformaldehyde and 2% OsO4 and embedded in Lowicryl K4M at -40$^{\circ}C$ under UV light (360 nm). The thin sections were loaded on the nickel grids and stained with the serum IgG and protein A-gold complex (particle size: 10 nm). Observations were undertaken with transmission electron microscope (Jeol, JEM-1010). The epithelium of the digestive tract was consisted of five types of cells. In the cytochemical study, the reaction products were found along the periphery of the vacuoles derived from the Bebedict reaction. In the immunocytochemical study, the protein-A gold particles were selectively labelled in Type 1, Type 3 and Type 4 cells in intestinal tissue. membranes of rER, in the surrounding cytoplasm of the rER and secretory granules, and in the apical cytoplasm of the cells. On the material being secreted from the apical cytoplasm was also labelled with the immunogold particles. The all results obtained throughtout present study suggest that the intestinal epithelium of the snail N. samarangae seretes cellulase as one of digestive enzymes.

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Molecular Dynamics Simulation of Enantioselectivity in Metoprolol in complex

  • Jang, Seok-Young;Park, Kyung-Lae
    • 대한약학회:학술대회논문집
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    • 대한약학회 2002년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2
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    • pp.356.3-357
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    • 2002
  • Metoprolol (MT) is one kinds of adrenergic beta-blockers. Its (S)-enantiomer is known to be more active than the (R). Recently. the x-ray structure of beta-blocker. (S)-propranolol (a-naphthyl analogue), complexed in a mould fungal cellulase. Cel7A. was reported and the (R)-form did not build any complex. And in our previous study the conformation and stability of MT in carboxymethylated beta-cyclodextrin (BCD) complex was determined by NMR. HPLC, UV and electrophoresis measurement. (omitted)

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복합효소를 이용한 고추 추출액의 이화학적 및 관능적 특성 (Physicochemical and Sensory Properties of Red Pepper Extract treated with Enzyme Complex)

  • 이종열;최구희;이경행
    • 한국식품영양학회지
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    • 제28권4호
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    • pp.628-634
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    • 2015
  • 고추 추출액의 수율 및 생리적 기능성을 향상시키기 위하여 고추에 cellulase(C 처리군), pectinase(P 처리군), amylase(A 처리군)를 각각 또는 이들 효소들을 혼합(CP, CA, PA 및 CPA 처리군) 첨가하여 2~8시간동안 가수분해시킨 후 가열처리하고, 여과시킨 추출액에 대하여 이화학적 및 관능적 평가를 측정하였다. 효소 처리 고추 추출액의 수율은 효소 처리를 하지 않았을 때 38.84% 정도로 매우 낮게 나타났지만, 효소처리군이 높은 수율을 보였고, 효소 단독처리군보다는 병용처리 시 수율이 증가하였으며, 효소 처리 시간이 길어질수록 유의적으로 수율이 증가하는 것으로 나타났다. 특히 cellulase + pectinase + amylase(CPA) 복합처리군은 추출수율이 74.37%까지 증가하였다. 가용성 고형분의 함량변화는 대조군의 경우에는 8.51% 를 나타내었으나, 효소처리군은 대조군보다 높은 함량을 나타내었으며, CA 혼합처리군과 CPA 혼합처리군이 가장 높은 가용성 고형분 함량을 보였다. 환원당의 함량 또한 효소 처리에 의하여 증가하는 것으로 나타났다. 효소 처리에 의한 색도의 변화에서는 대조군과 효소처리군 간에 색도의 변화를 보이지는 않았다. 효소 처리한 고추 추출액에 대한 관능검사 결과에서는 전반적으로 효소 처리를 하지 않은 대조군에 비하여 효소 처리 시 기호도 면에서 우수한 것으로 나타나, 고추 추출물 제조를 위한 효소 처리는 수율 및 기호도 증진을 위한 좋은 방법으로 사료된다.

Studies on Fermentation Conditions for-Cellulolytic enzymes Production using Trichoderma viride

  • 김종민;유두영
    • 한국미생물생명공학회:학술대회논문집
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    • 한국미생물생명공학회 1977년도 추계학술발표회 및 특별 강연초록
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    • pp.197.4-197
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    • 1977
  • Efficient utilization of cellulosic material as renewable resources is drawing an increasing degree of attention in the scientific community. As part of our endeavor to improve the production of cellulase complex system, several factors that influence production of cellulolytic enzyme system have been studied.

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In Vitro Antagonistic Activity Evaluation of Lactic Acid Bacteria (LAB) Combined with Cellulase Enzyme Against Campylobacter jejuni Growth in Co-Culture

  • Dubois-Dauphin, Robin;Sabrina, Vandeplas;Isabelle, Didderen;Christopher, Marcq;Andre, Thewis;Philippe, Thonart
    • Journal of Microbiology and Biotechnology
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    • 제21권1호
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    • pp.62-70
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    • 2011
  • The antibacterial effects of nine lactic acid bacteria (LAB) against Campylobacter jejuni were investigated by using agar gel diffusion and co-culture assays. Some differences were recorded between the inhibition effects measured with these two methods. Only two LAB, Lb. pentosus CWBI B78 and E. faecium THT, exhibited a clear anti- Campylobacter activity in co-culture assay with dehydrated poultry excreta mixed with ground straw (DPE/GS) as the only growth substrate source. It was observed that the supplementation of such medium with a cellulase A complex (Beldem S.A.) enhanced the antimicrobial effect of both LAB strains. The co-culture medium acidification and the C. jejuni were positively correlated with the cellulase A concentration. The antibacterial effect was characterized by the lactic acid production from the homofermentative E. faecium THT and the lactic and acetic acids production from the heterofermentative Lb. pentosus CWBI B78. The antagonistic properties of LAB strains and enzyme combination could be used in strategies aiming at the reduction of Campylobacter prevalence in the poultry production chain and consequently the risk of human infection.

고온 알칼리성 Bacillus sp. F204의 Cellulase 유전자의 Escherichia coli 및 Bacillus subtilis에의 Cloning 및 발현 (Cloning of Thermophilic Alkalophilic Bacillas sp. F204 Cellulase Gene and Its Expression in Escherichia coli and Bacillus subtilis)

  • 정영철;김양우;강신권;노종수;박재현;성낙계
    • 한국식품과학회지
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    • 제23권1호
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    • pp.31-36
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    • 1991
  • 고온, 알칼리성 Bacillus sp. F204의 CMCase 유전자를 pUC19의 HindIII부위에 연결하여 전이된 E.coli 형질전환체 중 2개의 재조합 플라스미드 즉, pBC191과 pBC192를 선발하였는데, 이들은4.6 Kb와 5.8 Kb HindIII 절편을 각각 함유하고 있었다. pBC191의 4.6 Kb HindIII 절편을 BamHI, EcoRI, KpnI, PvuII 부위가 각각 1개씩 존재하였다. Dioxigenin-labeled deoxyuridin-triphosphate에 4.6 Kb 절편을 표식한 것을 probe로 하여 상동성을 검정한 결과 모균주와 강한상동성이 없었고, 면역학적 실험에서도 Bacillus sp. F204 유래임이 인정되었다. pBC191의 4.6 Kb 절편을 E.coli의 발현 벡타인 pKK223-3과 Bacillus vector인 pGR71에 연결시켜 구축한 pKC231과 pGC711은 각각 pBC191에 비하여 효소활성이 3.2배와 2.8배정도 증가되었으며, 그리고 E.coli에서는 대부분 세포내와 periplasmic 분획에서 검출되었다. 기질 특이성을 조사한 결과에 의하면 pBC191과 pBC192는 CMCase gene을 코딩하고 있는 것으로 나타났다.

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Double Labeling of Binding Sites in Cellulosic Substrates Using Endo- and Exoglucanase-Gold Complexes

  • Bae Hyeun-Jong
    • Plant Resources
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    • 제8권3호
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    • pp.175-180
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    • 2005
  • Thin sections of cellulose fibers were incubated with an endo- and an exoglucanase labeled with gold particles of differing sizes. The hydrolytic sites were then visualized under transmission electron microscopy (TEM). The potential interaction between the ${\beta}$-1, 4-glucan substrates and the endo- and the exoglucanases was investigated using cellulosic and lignocellulosic substrates. The simultaneous visualization was very successful in distinguishing preferred substrates for each cellulase in lignocellulosic substrates. When plant lignocellulose was preincubated with endocellulase, density of the gold labeling greatly increased suggesting that preliminary exposure of lignocellulosic material to endocellulase may have enhanced the accessibility of the substrate to endocellulase and exocellulase. This result provided a plausible explanation for the observed endo/exo cellulase co-hydrolysis.

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Trichoderma viride QM 9414가 생산하는 Cellulase 특성에 관한 연구 (Studies on the Characterization of Cellulase Produced by Trichoderma viride QM 9414)

  • 윤은숙;이혜정
    • 한국식품영양학회지
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    • 제3권1호
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    • pp.57-68
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    • 1990
  • In order to obtain the fundamental informations on cellulase of Trichoderma viride QM 9414 for its production and utilization, some physico-chemical properties of the enzyme were reviewed. When T. viride QM 9414 was cultured on wheat bran medium, filter paper-disintegrating and carboxymethyl cellulose-saccharifying activity were increased with the cell growth, and thereafter CMC-saccharifying activity was kept on almost the same leved while filter-paper disintegrating activity was decreased sharply. And B-glucosidase was formed maximally on the late stationary phase of growth. The crude cellulase of cell-free extracts was purified by (NH4)2SO4 fractionation, Sephadex-G 200 column chromatography and DEAE Sephadex A-50 column chromatography. Filter paper-disintegrating, CMC-saccharifying and B-glucosidase activity were purified 10-fold, 47-fold and 38-fold, respectively. The crude enzyme was proved to be a complex of three different enzyme proteins which were showing filter paper-disintegrating, CMC-saccharifying and B-glucosidase activity. The optimal pH of the three enzyme components was alike pH 4.0, and the optimal temperature for CMC-saccharifying, filter paper-disintegrating and B-glucosidase activity were 4$0^{\circ}C$, 45$^{\circ}C$ and 5$0^{\circ}C$ respectively. The Km and Vmax values of CMC saccharifying activity for CMC were 0.485% and 3.10, and the Km and Vmax vallues of B-glucosidase for PNPG were 0.944$\times$10-3M and 0.097, respectively. The Km and Vmax values of filter paper-disintegrating activity for Avicel were determined to be 0.09% and 0.178, respectively. B-Glucosidase activity was competitively inhibited by glucose, and the Ki value for this enzyme was 3.54$\times$10-3M, CMC saccharifying activity was found to be greatly inhibited by cellobiose.

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