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1.
The production cost of cellulolytic enzymes is a major contributor to the high cost of ethanol production from lignocellulosics
using enzymatic hydrolysis. The aim of the present study was to investigate the cellulolytic enzyme production ofTrichoderma reesei Rut C 30, which is known as a good cellulase secreting micro-organism, using willow as the carbon source. The willow, which
is a fast-growing energy crop in Sweden, was impregnated with 1–4% SO2 and steam-pretreated for 5 min at 206°C. The pretreated willow was washed and the wash water, which contains several soluble
sugars from the hemicellulose, was supplemented with fibrous pretreated willow and used for enzyme production. In addition
to sugars, the liquid contains degradation products such as acetic acid, furfural, and 5-hydroxy-methylfurfural, which are
inhibitory for microorganisms. The results showed that 50% of the cellulose can be replaced with sugars from the wash water.
The highest enzyme activity, 1.79 FPU/mL and yield, 133 FPU/g carbohydrate, was obtained at pH 6.0 using 20 g/L carbon source
concentration. At lower pHs, a total lack of growth and enzyme production was observed, which probably could be explained
by furfural inhibition. 相似文献
2.
Cheanyeh Cheng 《中国化学会会志》1998,45(5):679-688
The activity of cellulase has traditionally been described by pH and temperature; however, the buffering medium is also an important factor, Taking plain water as a reference medium, three kinds of buffer including KH2PO4/K5HPO4, citric acid/sodium citrate, and acetic acid/sodium acetate were adopted to survey their effects on the activity of cellulase. Chromatographic assays indicated that xylose, glucose, and cellobiose were the major products and that minor products such as cellotriose and cellotetraose were present in some cases. The activities of cellulase based on glucose production showed that the phosphate buffer acted as a deactivator for cellulase and each of the two organic acid buffers acted as activators for cellulase. The concentration of activation buffer should be high to reach a high cellulase activity; however, this effect would be compensated for by the product inhibition of cellulase. The highest activity obtained was 4.16 ± 0.08 (× 10?3) IU mg?1 for the citric acid/sodium citrate buffer under pH 4.80, 40 °C and an agitation speed of 150 rpm. 相似文献
3.
A new study of the enzymatic hydrolysis of carboxymethyl cellulose with a bulk acoustic wave sensor 总被引:4,自引:0,他引:4
A new bulk acoustic wave (BAW) cellulase sensing technique, which is based on the enzymatic hydrolysis process of sodium carboxymethylcellulose (CMC) by cellulase, was established. The frequency shift curves of BAW sensor indicated that the viscosity of the tested solutions decreased during the hydrolysis process. The hydrolysis rate of CMC by cellulase was calculated from the frequency shift curves. The hydrolysis rate of CMC under different pH conditions at 30°C showed that cellulase had high hydrolysis ability approximately at pH 5.0. Kinetic parameters (the Michaelis constant Km and the maximum rate Vmax) of the process were estimated by using a linear method of Lineweaver–Burk plot. Km is 1.95±0.25 mg ml−1 and Vmax is −(4.25±0.58)×10−3 g1/2 cm−3/2 cP1/2 min−1. Also the activation energy (Ea) of the enzymatic hydrolysis, with a value of 51.99±1.26 kJ mol−1, was estimated in this work. 相似文献
4.
Alexander V. Gusakov Arkady P. Sinitsyn Alejandro G. Berlin Nonna N. Popova Alexander V. Markov Oleg N. Okunev Dmitry F. Tikhomirov Mark Emalfarb 《Applied biochemistry and biotechnology》1998,75(2-3):279-293
A model microassay system was developed to measure indigo backstaining on cotton fabrics in the presence of enzymes on a small
laboratory scale. Backstaining indexes for 11 cellulase samples were measured, and the enzymes were ranked from lower to higher
backstaining. Two multienzyme cellulase preparations were separated into fractions using chromatofocusing on a Mono P column.
Adsorption ability and backstaining properties of purified enzyme fractions were studied. Evidence was obtained that protein
adsorption on cotton fabrics is a crucial parameter causing backstaining (both for crude cellulase samples and purified enzyme
components). 相似文献
5.
A starter culture ofTrichoderma reesei (Rut-C30) prepared in a liquid fluidized bed reactor (LFBR) gave better growth and greater cellulase production in submerged
fermentation than a conventional shake flask inoculum. The LFBR starter was prepared by first coatingT. reesei spores to 0.25 mm size corncob (1.0x108g-1) in a medium containing 1.0% corncob, 0.5 gL-1 xylose and 0.1 gL-1 lactose in a balanced salt solution, then fluidizing the particles in the LFBR for 36 h to allow germination of the spores,
and covering the particles with an approx 30 μm thick biofilm. This biofilm that developed in constant adherence to the lignocellulosic
carrier, apparently became well adapted to grow rapidly on insoluble cellulose substrates (Solca Floc), and had the enzymes
of the cellulase complex induced for increased cellulase production.
The LFBR starter used in a stirred tank reactor (STR) gave 15 gL-1 biomass production and 6.5 IU mL-1 overall cellulase activity with a volumetric productivity of 64 IU L-1h-1 in a 5 d fermentation, compared with a 7 d shake flask inoculum that gave 11 gL-1 biomass and 3.2 IU mL-1 cellulase activity, with a volumetric productivity of 31IU L-1h-1. The LFBR starter culture retained its viability in dry storage for 6–9 mo. 相似文献
6.
It is commonly observed that the rate of enzymatic hydrolysis of solid cellulose substrates declines markedly with time. In
this work the mechanism behind the rate reduction was investigated using two dominant cellulases of Trichoderma reesei: exoglucanase Cel7A (formerly known as CBHI) and endoglucanase Cel7B (formerly EGI). Hydrolysis of steam-pretreated spruce
(SPS) was performed with Cel7A and Cel7B alone, and in reconstituted mixtures. Throughout the 48-h hydrolysis, soluble products,
hydrolysis rates, and enzyme adsorption to the substrate were measured. The hydrolysis rate for both enzymes decreases rapidly
with hydrolysis time. Both enzymes adsorbed rapidly to the substrate during hydrolysis. Cel7A and Cel7B cooperate synergistically,
and synergism was approximately constant during the SPS hydrolysis. Thermal instability of the enzymes and product inhibition
was not the main cause of reduced hydrolysis rates. Adding fresh substrate to substrate previously hydrolyzed for 24 h with
Cel7A slightly increased the hydrolysis of SPS; however, the rate increased even more by adding fresh Cel7A. This suggests
that enzymes become inactivated while adsorbed to the substrate and that unproductive binding is the main cause of hydrolysis
rate reduction. The strongest increase in hydrolysis rate was achieved by adding Cel7B. An improved model is proposed that
extends the standard endo-exo synergy model and explains the rapid decrease in hydrolysis rate. It appears that the processive
action of Cel7A becomes hindered by obstacles in the lignocellulose substrate. Obstacles created by disordered cellulose chains
can be removed by the endo activity of Cel7B, which explains some of the observed synergism between Cel7A and Cel7B. The improved
model is supported by adsorption studies during hydrolysis. 相似文献
7.
The composition of cellulose, hemicellulose, starch, lignin, pectin, protein, and total lipid content in the selected cellulosic
wastes-tapioca (Manihot esculenta) stem, leaf, petiole, and water hyacinth (Eichhornia crassipes) were determined. The effectiveness of various physical and chemical pretreatments on the enzymatic digestibility of these
wastes were identified. In general, chemical pretreatments were more effective than physical pretreatments. The efficiency
of the pretreatment was checked by subjecting these wastes to enzymatic saccharification after the pretreatments. 相似文献
8.
Methodi L. Chetkarov Fawzy D. Hatour Dimiter N. Kolev 《Monatshefte für Chemie / Chemical Monthly》1985,116(12):1433-1445
TheSomogyi-Nelson colorimetric method is applied in a new manner more suitable for evaluating the kinetics of the enzyme hydrolysis of sodium carboxymethylcellulose (Na-CMC) catalyzed by the cellulase complex. By means of selective inhibition of a chosen enzyme from the cellulase complex it became possible to trace the effect of the other enzymes included in its composition.
Symbols Used E enzyme (E—cellulase;E—exo-cellobiohydrolase;E—-glucosidase) - [E] w weight concentration of enzymeE - S substrate (Na-CMC—sodium carboxymethylcellulose) - [S]0 weight concentration of substrateS - I inhibitor (I—lactose;I—calcium chloride;I—condurrite-B-epoxide) - P product (P—oligosaccharides;P—cellobiose;P—D-glucose) - P end product (K , K , K ) - DP degree of polymerization - DS degree of substitution - ES enzyme-substrate complex (E S, E S, E S) - EP enzyme-product complex (E P, E P) - EI enzyme-inhibitor complex (E I, E I, E I) - M s molecular mass of substrateS - K s substrate constant (K s , K s , K s ) - K I inhibitor constant (K I , K I , K I ) - K m Michaelis-Menten constant - k +1,k +2 (k +2 ,k +2 ,k +2 ) forward rate constants - k –1 reverse rate constant - 0 initial rate of reaction - V maximal reaction rate - A change in absorbance - molar absorption coefficient - wavelength Herrn Prof. Dr.Hans Tuppy zum 60. Geburtstag herzlichst gewidmet. 相似文献
Kinetik und Mechanismus der Hydrolyse von Natriumcarboxymethylcellulose (Na-CMC) durch einen Cellulase-Komplex
Zusammenfassung Die kolorimetrische Methode nachSomogyi undNelson wird nach einem neuen Verfahren zur Verfolgung der Kinetik der hydrolytischen Spaltung von Natriumcarboxymethylcellulose (Na-CMC), katalysiert durch den Cellulase-Komplex, angewandt. Durch selektive Inhibierung eines bestimmten Enzyms des Cellulase-Komplexes kann man die Wirkung der anderen zu seiner gesamten Zusammensetzung gehörenden Enzyme verfolgen.
Symbols Used E enzyme (E—cellulase;E—exo-cellobiohydrolase;E—-glucosidase) - [E] w weight concentration of enzymeE - S substrate (Na-CMC—sodium carboxymethylcellulose) - [S]0 weight concentration of substrateS - I inhibitor (I—lactose;I—calcium chloride;I—condurrite-B-epoxide) - P product (P—oligosaccharides;P—cellobiose;P—D-glucose) - P end product (K , K , K ) - DP degree of polymerization - DS degree of substitution - ES enzyme-substrate complex (E S, E S, E S) - EP enzyme-product complex (E P, E P) - EI enzyme-inhibitor complex (E I, E I, E I) - M s molecular mass of substrateS - K s substrate constant (K s , K s , K s ) - K I inhibitor constant (K I , K I , K I ) - K m Michaelis-Menten constant - k +1,k +2 (k +2 ,k +2 ,k +2 ) forward rate constants - k –1 reverse rate constant - 0 initial rate of reaction - V maximal reaction rate - A change in absorbance - molar absorption coefficient - wavelength Herrn Prof. Dr.Hans Tuppy zum 60. Geburtstag herzlichst gewidmet. 相似文献
9.
The enzyme cellulase fromAspergillus oryzae was resolved into four multiple forms, using anion exchange chromatography on DEAE Sephadex A-50 and gel filtration on Sephadex G-75. The stages of fractionation were followed by electrophoresis on cellulose acetate strips. These enzyme forms are characterized by different enzyme activities and isoelectric points.
Herrn Univ.-Prof. Dr.Hans Tuppy zum 65. Geburtstag herzlichst gewidmet. 相似文献
10.
Functional expression of a β-d-1,4 glucanase-encoding gene (egl1) from a filamentous fungus was achieved in both Escherichia coli and Saccharomyces cerevisiae using a modified version of pRS413. Optimal activity of the E. coli-expressed enzyme was found at incubation temperatures of 60°C, whereas the enzyme activity was optimal at 40°C when expressed
by S. cerevisiae. Enzyme activity at different pH levels was similar for both bacteria and yeast, being highest at 5.0. Yeast expression resulted
in a highly glycosylated protein of approx 60 kDa, compared to bacterial expression, which resulted in a protein of 30 kDa.
The hyperglycosylated protein had reduced enzyme activity, indicating that E. coli is a preferred vehicle for production scale-up. 相似文献