scholarly journals Cellulolytic enzyme system of Trichoderma koningii. Separation of components attacking native cotton

1968 ◽  
Vol 109 (2) ◽  
pp. 217-227 ◽  
Author(s):  
T. M. Wood
Keyword(s):  
Enzyme System ◽  
Soluble Sugars ◽  
Low Molecular Weight ◽  
Cellulolytic Enzyme ◽  
Enzyme Complex ◽  
Factor Activity ◽  
Trichoderma Koningii ◽  
S Factor ◽  
Separation Of Components ◽  
Swelling Factor

1. Cell-free culture filtrates from Trichoderma koningii were concentrated by precipitation with ammonium sulphate between the limits of 20% and 80% saturation. 2. Removal of a low-molecular-weight carboxymethylcellulase (CM-cellulase) component by chromatography on Sephadex G-75 had no effect on the ability of the enzyme complex to solubilize cotton. 3. Further chromatography on DEAE-Sephadex separated a component (C1) from the Cx (CM-cellulase) and β-glucosidase activities. Separately these components had little ability to produce soluble sugars from cotton, but when recombined in their original proportions this capacity was almost completely recovered. 4. The Cx component was further fractionated on SE-Sephadex into a fraction containing only CM-cellulase and a fraction showing CM-cellulase and β-glucosidase activities: the latter two components could be separated by heat treatment. 5. The C1 component had no swelling factor (S-factor) activity (Marsh, Merola & Simpson, 1953; Reese & Gilligan, 1954) on its own, but it had a synergistic effect on the S-factor activity associated with the CM-cellulase and β-glucosidase components.

scholarly journals The cellulase of Fusarium solani. Resolution of the enzyme complex

1969 ◽  
Vol 115 (3) ◽  
pp. 457-464 ◽  
Author(s):  
T. M. Wood
Keyword(s):  
Fusarium Solani ◽  
Cellulase Activity ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Gel Chromatography ◽  
Trichoderma Koningii ◽  
S Factor ◽  
Ph Range ◽  
The Individual ◽  
Swelling Factor

1. Culture filtrates from Fusarium solani were fractionated by ion-exchange chromatography on DEAE-Sephadex, followed by gel chromatography on Sephadex G-100, into a C1 component, a Cx component (CM-cellulase) and a β-glucosidase (cellobiase) component. 2. The individual components showed little capacity for the solubilization of cotton fibre (cellulase activity), but when recombined in their original proportions 81% of the original cellulase activity was recovered. 3. The C1 components of F. solani and Trichoderma koningii were similar in their pH optima, heat stabilities over the pH range 5–8 and elution volumes on Sephadex G-100. 4. The C1 component of F. solani synergized with the Cx component of T. koningii and conversely. 5. The C1 and the β-glucosidase components of F. solani were devoid of the swelling-factor (S-factor) activity associated with the Cx component.

Matrix metalloproteinases in stroke

2017 ◽  
pp. 110-117
Author(s):  
А.А. Пальцын
Keyword(s):  
Matrix Metalloproteinases ◽  
Enzyme System ◽  
Enzyme Complex ◽  
Pathogenic Factors ◽  
Pathogenic Action ◽  
Activity Of Enzymes ◽  
Living Tissues ◽  
Current Reconstruction ◽  
Metalloproteinase Activity

Матриксные металлопротеиназы - ферментный комплекс, необходимый для сохранения гомеостаза. Он участник нормальной, постоянно текущей реконструкции всех живых тканей. Действие патогенных факторов нарушает слаженную работу этого комплекса. Часто нарушение выражается излишней активностью ферментов, усиливающей патогенное действие. Однако и заживление, форсированное новообразование тканевых элементов, может происходить только при повышенной, в сравнении с нормой, активности металлопротеиназ. Такая ситуация требует от медицины умения разумно вмешиваться в работу ферментной системы. В статье представлены некоторые результаты этих вмешательств. Matrix metalloproteinases - enzyme complex necessary for maintenance of the homeostasis. He is a participant of normal, constantly current reconstruction of all living tissues. Action of pathogenic factors breaks harmonious work of this complex. Often violation is expressed by the excessive activity of enzymes amplifying pathogenic action. However and healing, which is accelerated new growth of tissue elements, can happen only at raised, compared with norm, metalloproteinase activity. Such situation demands from medicine of ability participate reasonably in work of enzyme system. The article presents some of the results of these actions.

scholarly journals Paenibacillus curdlanolyticus Strain B-6 Xylanolytic-Cellulolytic Enzyme System That Degrades Insoluble Polysaccharides

2006 ◽  
Vol 72 (4) ◽  
pp. 2483-2490 ◽  
Author(s):  
Patthra Pason ◽  
Khin Lay Kyu ◽  
Khanok Ratanakhanokchai
Keyword(s):  
Growth Phase ◽  
Enzyme Preparation ◽  
Enzyme System ◽  
Crude Enzyme ◽  
Cellulolytic Enzyme ◽  
Crude Enzyme Preparation ◽  
Multienzyme Complexes ◽  
Sds Page ◽  
Paenibacillus Curdlanolyticus ◽  
Cellulose Binding

ABSTRACT A facultatively anaerobic bacterium, Paenibacillus curdlanolyticus B-6, isolated from an anaerobic digester produces an extracellular xylanolytic-cellulolytic enzyme system containing xylanase, β-xylosidase, arabinofuranosidase, acetyl esterase, mannanase, carboxymethyl cellulase (CMCase), avicelase, cellobiohydrolase, β-glucosidase, amylase, and chitinase when grown on xylan under aerobic conditions. During growth on xylan, the bacterial cells were found to adhere to xylan from the early exponential growth phase to the late stationary growth phase. Scanning electron microscopic analysis revealed the adhesion of cells to xylan. The crude enzyme preparation was found to be capable of binding to insoluble xylan and Avicel. The xylanolytic-cellulolytic enzyme system efficiently hydrolyzed insoluble xylan, Avicel, and corn hulls to soluble sugars that were exclusively xylose and glucose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of a crude enzyme preparation exhibited at least 17 proteins, and zymograms revealed multiple xylanases and cellulases containing 12 xylanases and 9 CMCases. The cellulose-binding proteins, which are mainly in a multienzyme complex, were isolated from the crude enzyme preparation by affinity purification on cellulose. This showed nine proteins by SDS-PAGE and eight xylanases and six CMCases on zymograms. Sephacryl S-300 gel filtration showed that the cellulose-binding proteins consisted of two multienzyme complexes with molecular masses of 1,450 and 400 kDa. The results indicated that the xylanolytic-cellulolytic enzyme system of this bacterium exists as multienzyme complexes.

On the Specificity of Juvenile Hormone Biosynthesis in the Male Cecropia Moth

1981 ◽  
Vol 36 (7-8) ◽  
pp. 579-585 ◽  
Author(s):  
Martin G. Peter ◽  
Paul D. Shirk ◽  
Karl H. Dahm ◽  
Herbert Roller
Keyword(s):  
Juvenile Hormone ◽  
Enzyme System ◽  
Reaction Rates ◽  
Corpora Allata ◽  
Low Molecular Weight ◽  
Methyltransferase Activity ◽  
Accessory Sex Glands ◽  
Juvenile Hormone Biosynthesis ◽  
Hormone Biosynthesis ◽  
Natural Enantiomer

Abstract The accessory sex glands (ASG) of adult male Cecropia contain an enzyme that methylates juvenile hormone acids (JH-acids) in the presence of S-adenosyl-L-methionine (SAM). The methyltransferase is highly specific. The reaction rates decrease in the order JH-I-acid, JH-II-acid and JH-III-acid; in each case the natural enantiomer is esterified predominantly. Methyltrans­ ferase activity with the same substrate specificity was also demonstrated in adult female corpora allata (CA). Male CA have only marginal methyltransferase activity. The CA of male H. cecropia contain substantial amounts of JH-I-acid and JH-II-acid (minimum: 5 pmol/pair). When kept in organ culture, they release JH-acids into the medium. Radiolabeled propionate and mevalonate are incorporated efficiently into the carbon skeletons of the JH-acids. The enzyme system performing these transformations cannot be forced to produce JH-III-acid even in the presence of high mevalonate concentrations, though homomevalonate may enhance biosynthesis of JH-I-acid and JH-II-acid more than tenfold. It becomes evident that the regulation of JH titer balances with regard to the homologous structures during insect development is not merely a question of the availability of low molecular weight precursors, but in addition that of highly specific enzymes acting as regulatory entities in the later steps of the biosynthetic sequence.

scholarly journals Characterization of cellulolytic enzyme system of Schizophyllum commune mutant and evaluation of its efficiency on biomass hydrolysis

2017 ◽  
Vol 81 (7) ◽  
pp. 1289-1299 ◽  
Author(s):  
Warasirin Sornlake ◽  
Phatcharamon Rattanaphanjak ◽  
Verawat Champreda ◽  
Lily Eurwilaichitr ◽  
Suthathip Kittisenachai ◽  
...  
Keyword(s):  
Enzyme System ◽  
Schizophyllum Commune ◽  
Cellulolytic Enzyme ◽  
Biomass Hydrolysis

The Cellulolytic Enzyme System ofThermoactinomyces

1979 ◽  
pp. 331-345 ◽  
Author(s):  
BÄRBEL HÄGERDAL ◽  
JOHN FERCHAK ◽  
E. KENDALL PYE ◽  
JOHN R. FORRO
Keyword(s):  
Enzyme System ◽  
Cellulolytic Enzyme

scholarly journals Biochemical characterization and synergism of cellulolytic enzyme system from Chaetomium globosum on rice straw saccharification

2016 ◽  
Vol 16 (1) ◽  
Author(s):  
Wanwitoo Wanmolee ◽  
Warasirin Sornlake ◽  
Nakul Rattanaphan ◽  
Surisa Suwannarangsee ◽  
Navadol Laosiripojana ◽  
...  
Keyword(s):  
Rice Straw ◽  
Biochemical Characterization ◽  
Enzyme System ◽  
Chaetomium Globosum ◽  
Cellulolytic Enzyme

Preparation and Properties of Matrix-Supported Horseradish Peroxidase

1975 ◽  
Vol 53 (8) ◽  
pp. 868-874 ◽  
Author(s):  
Greg J. Bartling ◽  
Swaraj K. Chattopadhyay ◽  
Charles W. Barker ◽  
Harry D. Brown
Keyword(s):  
Horseradish Peroxidase ◽  
Chemical Synthesis ◽  
Enzyme Immobilization ◽  
Thermal Denaturation ◽  
Enzyme System ◽  
Nucleophilic Attack ◽  
Enzyme Complex ◽  
Ph Optimum ◽  
Enzyme Coupling ◽  
Substrate Kinetics

A new method of enzyme immobilization has been described using poly(4-methacryloxybenzoic acid) as the carrier. Activation of the polymer, prior to enzyme attachment, was achieved with N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline. The enzyme coupling step proceeded through nucleophilic attack by the protein on a mixed carbonic anhydride. The degree of polymer activation was determined by analysis for quinoline, a by-product of the reaction. The polymer–enzyme complex was compared to the enzyme in solution in terms of pH optimum, substrate kinetics, and thermal denaturation. Potential uses of the polymer–enzyme system in chemical synthesis of benzoquinone derivatives are discussed.

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