• 제목/요약/키워드: cellulase activities

검색결과 274건 처리시간 0.023초

몇 종류의 곰팡이에서 분리되는 Crude Cellulase의 다당류 분해능력의 조사 (Investigation of the Hydrolysis of Polysaccharides by Crude Cellulases prepared from Several Species of Fungi)

  • 김은수;김영민;이인규;최태주
    • 미생물학회지
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    • 제13권3호
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    • pp.85-90
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    • 1975
  • Crude cellulases freshly prepared from cultures of Aspergillus niger, Prnicillum motatum, Trichoderma vride 16273 and Trichoderma viride 16374 were assayed on 4 different substrates including Na-CMC, cellulose powder, starch and sucrose. Enzyme prepared from A. niger contained highly active hydrolytic enzymes of the 4 substrates assayed. P. notatum [yielded relatively lower amount of cellulase but the extracts were also highly reactive on starch and sucrose. Trichoderma viride 16274 yielded very little cellulase and invertase, but the extracts showed a high degree of amylase activity. Trichoderma viride 16374, however, yielded collulase comparable to that of Penicillium notatum, but lower activities of amylase and invertase were seen. Commercial cellulases prepared from Penicillium notatum (cellulase[K]) and Trichoderma viride(cellulase[J]) indicated enzyme activities closely parallel to the crude enzymes freshly prepared from fungus cultures. The optimum pH's of cellulolytic activities of cellulase[K] and cellulase[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase[K] and cellualse[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase [K] and cellulase [J] were $60{\circ}C$ and $50{\circ}C$ respectively. Assuming the average molecular weight of Na-CMC is about 115,000, the Km values of cellulase [K] and cellulase[J] were found to be $3.3{\times}10^{-5}/nM$ and $3.3{\times}10^{-4}/nM$ respectively.

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한국산 Rhizopus의 효소활성에 관한 연구 (第 1 報) - Amylase, protease 및 cellulase 활성에 관하여- (Studies on the Enzyme Activities of Rhizopus distributed in South Korea(1) - On the amylase, protease and cellulase activities-)

  • 이영녹;윤경하;이평우;배광승;박용근;정성균;서항원
    • 미생물학회지
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    • 제14권2호
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    • pp.49-49
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    • 1976
  • Enzyme activities, such as glucoamylase dextrinogenic amylase, cellulase, acid protase and neutral protease, of Rhizopus isolated from various substrates collected throughout South Korea are measured, and their enzyme activities are surveyed from taxonomical, ecological and physiological viewpoint. Effect of carbon sources and phytohormones on the amylalse production of Rhizopus are also measured. Among the 735 strains of Phizopus isolated, strain number 587 exhibiting most prominent dextrinogenic amylase and netral protease activity is selected as the best strain, and the strain number 673, 108, 329, 165 and 728 are seleted for their predominant cellulase, acid protease, glucoamylase, dextrinogenic amylase and neutral protease activities, respectively. R.acidus and R.nigricans which exhibited relatively higher callulalse activity, showed lower activities for both amylase. R.tritici exhibited higher protease activity. The relations between activities and various substrates of wild strains are not outstnading difference, although the strains isolated from inland region exhibited more or less higher amylase and cellulase activities, than those of coast region, generally. Lactose and dextrin are most effective carbon sources for glucoamylase and dextrinogenic amylase production of the Rhizopus niveus, respectively. Although all phytohormones tested are effective for production of amylase by the Rhizopus strains, except nicotinamide for glucoamylase production, biotin and ascorbate are most effective for dextrinogenic amylase and glucoamylase production, respectively.

한국산 Rhizopus의 효소활성에 관한 연구 (第 1 報) - Amylase, protease 및 cellulase 활성에 관하여- (Studies on the Enzyme Activities of Rhizopus distributed in South Korea(1) - On the amylase, protease and cellulase activities-)

  • 이영녹;윤경하;이평우;배광승;박용근;정성균;서항원
    • 미생물학회지
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    • 제14권2호
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    • pp.47-56
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    • 1976
  • Enzyme activities, such as glucoamylase dextrinogenic amylase, cellulase, acid protase and neutral protease, of Rhizopus isolated from various substrates collected throughout South Korea are measured, and their enzyme activities are surveyed from taxonomical, ecological and physiological viewpoint. Effect of carbon sources and phytohormones on the amylalse production of Rhizopus are also measured. Among the 735 strains of Phizopus isolated, strain number 587 exhibiting most prominent dextrinogenic amylase and netral protease activity is selected as the best strain, and the strain number 673, 108, 329, 165 and 728 are seleted for their predominant cellulase, acid protease, glucoamylase, dextrinogenic amylase and neutral protease activities, respectively. R.acidus and R.nigricans which exhibited relatively higher callulalse activity, showed lower activities for both amylase. R.tritici exhibited higher protease activity. The relations between activities and various substrates of wild strains are not outstnading difference, although the strains isolated from inland region exhibited more or less higher amylase and cellulase activities, than those of coast region, generally. Lactose and dextrin are most effective carbon sources for glucoamylase and dextrinogenic amylase production of the Rhizopus niveus, respectively. Although all phytohormones tested are effective for production of amylase by the Rhizopus strains, except nicotinamide for glucoamylase production, biotin and ascorbate are most effective for dextrinogenic amylase and glucoamylase production, respectively.

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Chitinolytic and Chitosanolytic Activities from Crude Cellulase Extract Produced by A. niger Grown on Apple Pomace Through Koji Fermentation

  • Dhillon, Gurpreet Singh;Brar, Satinder Kaur;Kaur, Surinder;Valero, Jose R.;Verma, Mausam
    • Journal of Microbiology and Biotechnology
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    • 제21권12호
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    • pp.1312-1321
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    • 2011
  • Enzyme extracts of cellulase [filter paper cellulase (FPase) and carboxymethyl cellulase (CMCase)], chitinase, and chitosanase produced by Aspergillus niger NRRL-567 were evaluated. The interactive effects of initial moisture and different inducers for FP cellulase and CMCase production were optimized using response surface methodology. Higher enzyme activities [FPase $79.24{\pm}4.22$ IU/gram fermented substrate (gfs) and CMCase $124.04{\pm}7.78$ IU/gfs] were achieved after 48 h fermentation in solid-state medium containing apple pomace supplemented with rice husk [1% (w/w)] under optimized conditions [pH 4.5, moisture 55% (v/w), and inducers veratryl alcohol (2 mM/kg), copper sulfate (1.5 mM/kg), and lactose 2% (w/w)] (p<0.05). Koji fermentation in trays was carried out and higher enzyme activities (FPase $96.67{\pm}4.18$ IU/gfs and CMCase $146.50{\pm}11.92$ IU/gfs) were achieved. The nonspecific chitinase and chitosanase activities of cellulase enzyme extract were analyzed using chitin and chitosan substrates with different physicochemical characteristics, such as degree of deacetylation, molecular weight, and viscosity. Higher chitinase and chitosanase activities of $70.28{\pm}3.34$ IU/gfs and $60.18{\pm}3.82$ to $64.20{\pm}4.12$ IU/gfs, respectively, were achieved. Moreover, the enzyme was stable and retained 92-94% activity even after one month. Cellulase enzyme extract obtained from A. niger with chitinolytic and chitosanolytic activities could be potentially used for making low-molecular-weight chitin and chitosan oligomers, having promising applications in biomedicine, pharmaceuticals, food, and agricultural industries, and in biocontrol formulations.

톱밥배양한 느타리버섯 균사생장시 생산되는 각종 효소변화 (Changes in activities of protease, phenoloxidase and cellulase during mycelium growth of Pleurotus ostreatus in sawdust cultures)

  • 장현유;김광포;차동열
    • 한국균학회지
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    • 제24권2호통권77호
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    • pp.149-154
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    • 1996
  • 느타리버섯 균사를 톱밥에 배양할 때 분비되는 여러 가지 extracellular enzyme중 pretense, phenoloxidase, cellulase가 배양조건을 달리하였을 때 변화양상을 요약하면 먼저 톱밥의 종류에 따라서는 참나무톱밥에 비해 포플라톱밥이 specific activity가 높은 경향이었다. 첨가제 종류에 따라서는 밀기울에 비해 미강이 약간 높았으며 혼합비율이 30, 20, 10%순으로 높았다. 수분함량은 3가지 효소 모두 70%에서, 배지의 PH에 따라서 protease는 pH 4와 9, cellulase는 pH6, phonoloxidase는 pH 5와 7, 배양온도는 3가지 효소 모두 $25^{\circ}C$, 목초액 농도에 따른 pretense와 phonoloxidase는 무처리가 처리보다 총활성이 높았으며, cellulase는 0.5%에서 총활성이 가장 높았다.

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한국산 Aspergillus의 셀룰라아제 활성에 관한 연구 (2) : 균주의 계통과 효소활성 (Cellulase Activities of Aspergilli distributed in South Korea Acivelase, CMCase and Salicinase Activities of the Strains Surveyed in Taxonomical Viewpoint)

  • Lee, Yung-Nok;Park, Yong keun
    • 미생물학회지
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    • 제15권3호
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    • pp.113-121
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    • 1977
  • The 685 strains of Korean Sspergilli are isolated, cultured purely, and their Avicelase, CMCase and Salicinase activities are measured, in order to select the best strains exhibiting predominant cellulase activities, and to survey their cellulase activities in taxonomical and ecological viewpoints. Strains No.175, 255 and 254 are selected as the best Avicelase producing strains, strains No.131, 151 and 116 are selected as the best CMCase producing strains, and strains nO.456, 457 and 253 are selected as the best Salicinase producing strains. A niger group and A, clavatus group exhibited the highest activities of Avcelase and Salicinase, respectively. A.iniger group and A, clavatus groups are showed the highest activites of CMCase. Among the different species tested, the activities of Avicelase, CMCase andSalicinase are highest in A.phoenicis, A.clavatus, and A. japonicus and A.giganteus, respectively. Cellulase activities of Aspergilli from the inland regions of Korea are higher, more or less, than those of the strains from the other regions. Avicelase and CMCase activities of Aspergilli isolated from bread and Korean cake are relatively higher, and Salicinase activities of the strains isolated from the cereals are higher than those of the strains from the other habitat substrate.

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인삼 종자의 성숙과 후숙 과정에서 배유세포내 섬유소 가수분해효소의 분포 및 기능 (Localization and Function of Cellulase in Endosperm Cells of Panax ginseng Seeds during Maturation and After-ripening)

  • 유성철
    • Journal of Plant Biology
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    • 제36권4호
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    • pp.327-335
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    • 1993
  • The active sites, intracellular transport, function of cellulase in association with the disintegration of the storage materials of the endosperm cells during seed maturation and after-ripening of Panax ginseng C.A. Meyer seeds were studied by electron microscopy. Cytochemical activities of the cellulase occurred in protein bodies and vesicles of endosperm cells in seed with red seed coat. In after-ripening seed, the activities were strongly found in the cell wall of endosperm near the umbiliform layer and on neighbouring vesicles, so it is assumed that these cells begin to be decomposed. Cellulase activities were initiated before the decomposition of storage materials. But, no activity was observed in the umbiliform layer, so it is suggested that cellulase lose its activity after the completion of lysis process.

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담자균(擔子菌)이 생산(生産)하는 효소(酵素)에 관(關)한 연구(硏究) -제2보(第二報) Cellulase 및 Xylanase의 성질(性質)- (Studies on the Enzymes Produced by Basidiomycetes -Part II. Properties of Cellulase and Xylanase-)

  • 홍재식;권용주
    • Applied Biological Chemistry
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    • 제24권4호
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    • pp.260-266
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    • 1981
  • Pleurotus ostreatus 301과 Lentinus edodes 3-1을 볏짚배지(培地)에 배양(培養)하여 배양중(培養中)에 생성(生成)된 cellulase와 xylanase의 성질(性質)을 검토(檢討)한 결과(結果) P. ostreatus 301의 cellulase 활성(活性)은 기질농도(基質濃度) 0.6%, L. edodes 3-1은 0.8%, xylanase는 양균주(兩菌株)에서 1%까지는 비례적(比例的)으로 증가(增加)하였다. 반응시간(反應時間)에 따른 환원당(還元糖)의 생성(生成)은 양균주(兩菌株)에서 cellulase는 60분(分), xylanase는 30분(分)까지 비례적(比例的)으로 증가(增加)하였다. 최적(最適) pH는cellulase에서 P. ostreatus 301은 pH 4.0, L. edodes 3-1은 pH 4.5이었으며 xylanase는 양균주(兩菌株)가 pH 5.0이었다. pH 안정범위(安定範圍)는 P. ostreatus 301의 cellulase에서 pH $4.0{\sim}6.0$, L. edoder 3-1은 pH $3.0{\sim}5.0$이었고 xylanase는 P. osteatus 301에서 pH $4.5{\sim}6.0$, L. edodes 3-1에서는 pH $3.5{\sim}6.0$이었다. 최적온도(最適溫度)는 P. ostreatus 301의 cellulase에서 $40^{\circ}C$, L. edodes 3-1의 xylanase는 $45^{\circ}C$이었고, L. edodes 3-1의 cellulas와 P. ostreatus 301의 xylanase는 $50^{\circ}C$ 이었으며 열안정성(熱安定性)은 최적온도(最適溫度) 이하이었고, $70^{\circ}C$, 10분(分)으로 대부분 실활(失活)되었다. 염류(鹽類)의 영향(影響)은 L. edodes 3-1의 cellulase는 $Co^{++},\; Mg^{++}$에 의해서 효소력(酵素力)이 증가(增加)되었으며,$Mg^{++},\;Cu^{++}$에 의해서는 양균주(兩菌株)에서 심한 조해(阻害)를 를 보였고 xylanase는 $Ca^{++},\;Co^{++},\;Mg^{++}\;Cd^{++}$ 등은 약간 증가(增加)를 보였고, $Hg^{++}$은 조해(阻害)가 심했다.

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Production of Thermostable $\alpha$-Amylase and Cellulase from Cellulomonas sp.

  • EMTIAZI, G.,;I. NAHVI,
    • Journal of Microbiology and Biotechnology
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    • 제14권6호
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    • pp.1196-1199
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    • 2004
  • A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.

Cloning and Characterization of a Bifunctional Cellulase-Chitosanase Gene from Bacillus lichenformis NBL420

  • HONG, IN-PYO;HONG-KI JANG;SHIN-YOUNG LEE;SHIN-GEON CHOI
    • Journal of Microbiology and Biotechnology
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    • 제13권1호
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    • pp.35-42
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    • 2003
  • A 1,3 kb cellulase gene encoding novel bifunctional cellulase-chitosanase activity was cloned from biopolymer-producing alkali-tolerant B. lichenformis NBL420 in E. coli. A recombinant cellulase-chitosanase, named CelA, was expressed and purified to homogeneity. The activity staining and the enzymatic characterization of the purified CeIA revealed bifunctional activities on carboxymethyl cellulose (CMC) and glycol-chitosan. The similar characteristics of the enzymatic activities at the optimum pH, optimum temperature, and thermostability Indicated that CelA used a common catalytic domain with relaxed substrate specificity. A comparison of the deduced amino acids in the N-terminal region revealed that the mature CelA had a high homology with the previously identified bifunctional cellulase-chitosanase of Myxobacter sp. AL- 1.