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1.
Recent developments in molecular breeding and directed evolution have promised great developments in industrial enzymes as
demonstrated by exponential improvements in β-lactamase and green fluorescent protein (GFP). Detection of and screening for
improved enzymes are relatively easy if the target enzyme is expressible in a suitable high-throughput screening host and
a clearly defined and usable screen or selection is available, as with GFP and β-lactamase. Fungal cellulases, however, are
difficult to measure and have limited expressibility in heterologous hosts. Furthermore, traditional cellulase assays are
tedious and time-consuming. Multiple enzyme components, an insoluble substrate, and generally slow reaction rates have plagued
cellulase researchers interested in creating cellulase mixtures with increased activities and/or enhanced biochemical properties.
Although the International Union of Pure and Applied Chemists standard measure of cellulase activity, the filter paper assay
(FPA), can be reproduced in most laboratories with some effort, this method has long been recognized for its complexity and
susceptibility to operator error. Our current automated FPA method is based on a Cyberlabs C400 robotics deck equipped with
customized incubation, reagent storage, and plate-reading capabilities that allow rapid evaluation of cellulases acting on
cellulose and has a maximum throughput of 84 enzyme samples per day when performing the automated FPA. 相似文献
2.
Technologies suitable for the separation and reuse of cellulase enzymes during the enzymatic saccharification of pretreated
corn stover are investigated to examine the economic and technical viability of processes that promote cellulase reuse while
removing inhibitory reaction products such as glucose and cellobiose. The simplest and most suitable separation is a filter
with relatively large pores on the order of 20–25 mm that retains residual corn stover solids while passing reaction products
such as glucose and cellobiose to form a sugar stream for a variety of end uses. Such a simple separation is effective because
cellulase remains bound to the residual solids. Ultrafiltration using 50-kDa polyethersulfone membranes to recover cellulase
enzymes in solution was shown not to enhance further the saccharification rate or overall conversion. Instead, it appears
that the necessary cellulase enzymes, including β-glucosidase, are tightly bound to the substrate; when fresh corn stover
is contacted with highly washed residual solids, without the addition of fresh enzymes, glucose is generated at a high rate.
When filtration was applied multiple times, the concentration of inhibitory reaction products such as glucose and cellobiose
was reduced from 70 to 10 g/L. However, an enhanced saccharification performance was not observed, most likely because the
concentration of the inhibitory products remained too high. Further reduction in the product concentration was not investigated,
because it would make the reaction unnecessarily complex and result in a product stream that is much too dilute to be useful.
Finally, an economic analysis shows that reuse of cellulase can reduce glucose production costs, especially when the enzyme
price is high. The most economic performance is shown to occur when the cellulase enzyme is reused and a small amount of fresh
enzyme is added after each separation step to replace lost or deactivated enzyme. 相似文献
3.
The stability of Penicillium funiculosum cellulase has been investigated under the conditions used for cellulose hydrolysis. Fifty five percent of filter paper activity (FPA) was inactivated on incubation at 50°C for 24 h, whereas there was no loss in endoglucanase and β-glucosidase activity. The addition of 2% polyethylene glycol (PEG) during incubation stabilized the FPA. The influence of pH during fermentation on the thermal stability of the enzyme is discussed. The recovery of enzymes after hydrolysis of bagasse at 50°C was between 8 and 14%. Under the optimal conditions of elution, the recovery of enzyme was 35% ( 1). Increasing the enzyme to the substrate ratio fivefold and presence of PEG during hydrolysis resulted in 80, 83, and 95% recovery of β-glucosidase, FPA, and endoglucanase activity, respectively. Index Entries: Stability; recovery of cellulase P. funiculosum. 相似文献
4.
It is well known that cellulolytic enzymes hardly attack lignocellulose. Hitherto knowledge, however, has not yet fully elucidated the mechanisms of the inhibition; whether it depends on a steric hindrance or protein-binding inhibition. For the purpose of acceleration of enzymatic digestion of lignocellulose biomass, the study was carried out using partially purified cellulase of Meicelase and milled wood lignin from soft or hard wood. Milled wood lignin was prepared from soft wood, Picea jezoensis, or from hard wood, Quercus serrata, by the method of Björkman. Lignin was dissolved in methyl cellosolve, since the solvent has little effect on cellulolytic activities, and enzymic activities were followed with partially purified Meicelase. The results show that cellobiose activities of enzymes from Trichoderma viride are markedly depressed by both lignin of soft and hard wood, and the former lignin inhibits the reaction stronger than the latter. Lignins show no inhibition in the reaction with CMC and debris of filter paper. Liberation of glucose from filter paper by the enzyme in the presence of lignin is also depressed, and addition of cellobiase instead of lignin in the above enzyme reaction shows the delay of time for breakdown of filter paper. This phenomenon indicates that lignin inhibits enzymic decomposition of cellobiose in the degradation pathway of cellulose and accumulated cellobiose gives a feedback function to digestion of fibers of paper. 相似文献
5.
A new saccharification assay has been devised, in which a continuously buffer-swept membrane reactor is used to remove the solubilized saccharification products, thus allowing high extents of substrate conversion without significant inhibitory effects from the buildup of either cellobiose or glucose. This diafiltration saccharification assay (DSA) can, therefore, be used to obtain direct measurements of the performance of combinations of cellulase and substrate under simulated SSF conditions, without the saccharification results being complicated by factors that may influence the subsequent fermentation step. This assay has been used to compare the effectiveness of commercial and special in-house-producedTrichoderma reeSci. cellulase preparations in the saccharification of a standardized microcrystalline (Sigmacell) substrate and a dilute-acid pretreated lignocellulosic substrate. Initial results strongly suggest that enzyme preparations produced in the presence of the targeted lignocellulosic substrate will saccharify that substrate more effectively. These results call into question the widespread use of the “filter paper assay” as a reliable predictor of enzyme performance in the extensive hydrolysis of substrates that are quite different from filter paper in both physical properties and chemical composition. 相似文献
6.
β-Glucosidase was covalently immobilized alone and coimmobilized with cellulase using a hydrophilic polyurethane foam (Hypol®FHP 2002). Immobilization improved the functional properties of the enzymes. When immobilized alone, the K m for cellobiose of β-glucosidase was decreased by 33% and the pH optimum shifted to a slightly more basic value, compared to the free enzyme. Immobilized β-glucosidase was extremely stable (95% of activity remained after 1000 h of continuous use). Coimmobilization of cellulase and β-glucosidase produced a cellulose-hydrolyzing complex with a 2.5-fold greater rate of glucose production for soluble cellulose and a four-fold greater increase for insoluble cellulose, compared to immobilized cellulase alone. The immobilized enzymes showed a broader acceptance of various types of insoluble cellulose substrates than did the free enzymes and showed a long-term (at least 24 h) linear rate of glucose production from microcrystalline cellulose. The pH optimum for the coimmobilized enzymes was 6.0. This method for enzyme immobilization is fast, irreversible, and does not require harsh conditions. The enhanced glucose yields obtained indicate that this method may prove useful for commercial cellulose hydrolysis. 相似文献
7.
The economics driving biorefinery development requires high value-added products such as cellobiose for financial feasibility.
This research describes a simple technology for increasing cellobiose yields during lignocellulosic hydrolysis. The yield
of cellobiose produced during cellulose hydrolysis was maximized by modification of reaction conditions. The addition of an
inhibitor from the group that includes glucose oxidase, gluconolactone, and gluconic acid during cellulase hydrolysis of cellulose
increased the amount of cellobiose produced. The optimal conditions for cellobiose production were determined for four factors;
reaction time, cellulase concentration, cellulose concentration, and inhibitor concentration using a Box-Behnken experimental
design. Gluconolactone in the cellulase system resulted in the greatest production of cellobiose (31.2%) from cellulose. The
yield of cellobiose was 23.7% with glucose oxidase, similar to 21.9% with gluconic acid. 相似文献
8.
To enhance the conversion of the cellulose and hemicellulose, the corncob pretreated by aqueous ammonia soaking was hydrolyzed
by enzyme complexes. The saturation limit for cellulase (Spezyme CP) was determined as 15 mg protein/g glucan (50 filter paper
unit (FPU)/g glucan). The accessory enzymes (β-glucosidase, xylanase, and pectinase) were supplemented to hydrolyze cellobiose
(cellulase-inhibiting product), hemicellulose, and pectin (the component covering the fiber surfaces), respectively. It was
found that β-glucosidase (Novozyme 188) loading of 1.45 mg protein/g glucan [30 cellobiase units (CBU)/g glucan] was enough
to eliminate the cellobiose inhibitor, and 2.9 mg protein/g glucan (60 CBU/g glucan) was the saturation limit. The supplementation
of xylanase and pectinase can increase the conversion of cellulose and hemicellulose significantly. The yields of glucose
and xylose enhanced with the increasing enzyme loading, but the increasing trend became low at high loading. Compared with
xylanase, pectinase was more effective to promote the hydrolysis of cellulose and hemicellulose. The supplementation of pectinase
with 0.12 mg protein/g glucan could increase the yields of glucose and xylose by 7.5% and 29.3%, respectively. 相似文献
9.
Microcrystalline cellulose (MCC) is suspected to be a new adulteration in pasteurized milk in China, yet an efficient method for MCC detection in dairy has not been established. This study presents a novel procedure to detect and estimate MCC in pasteurized milk using dialysis, cellulase hydrolysis, and a reducing sugar assay. The background value of reducing sugar was eliminated by dialysis, and cellulase activity toward MCC was stable in dialyzed milk. A criterion for MCC detection and an empirical formula for MCC estimation were summarized based on the reducing sugar variation after hydrolysis. The detection sensitivity was below 0.5 g/L. Reducing sugar distribution after cellulase-catalyzed hydrolysis was examined by HPLC, and revealed that most of the detected sugar was glucose. This paper describes a practical method for detection of MCC in pasteurized milk that might benefit dairy QC. 相似文献
10.
Glucose is a typical diagnostic marker of diabetes mellitus but it may be also helpful during diagnosis of some types of poisoning, immunological disorder or long-term stress at hospitalized patients. Diagnosis of diabetes mellitus in time is indispensable for prevention of life-threatening complication and so, accurate and easy device for non-invasive and accurate self-diagnosis is necessary. Simple assay based on filter paper with chitosan layer and with immobilized enzymes glucose oxidase and peroxidase and phone camera detection has been proposed for home-care glucose detection in urine. Data were processed in RGB (red–green–blue) color model when blue color channel showed the best sensitivity to changing glucose concentrations. Assay exerted linear regression from 0 to 4 mmol/l and limit of detection was set to be 166 µmol/l. Assay was not influenced by any interfering substances including maltose, sucrose, sorbitol or fructose or by urine matrix substance such as bovine serum albumin, ascorbic acid, uric acid or urea. Measurement of glucose from spiked urine samples reveals also no influence of the matrix on the assay. Long-term stability was measured and filter papers coated by enzymes showed excellent stability for at least 9 weeks without any special treatment or package. In comparison with differently modified filter paper, filter paper with both chitosan and enzymes showed the best sensitivity to changing glucose concentration. In a conclusion, simple (phone camera detection) and fast (3-min reaction) assay for quantitative detection of glucose from urine was optimized. 相似文献
11.
A calorimetric assay procedure for the determination of cellobiose has been developed. The cellobiose is hydrolyzed by β-glucosidase
and the glucose formed is measured calorimetrically by an enzyme thermistor containing co-immobilized glucose oxidase and
catalase. The system was optimized with regard to the arrangement of the enzymes, the pH-dependence of the separate enzymic
steps, and of the total system. By placing the β-glucosidase in a precolumn that could be switched in and out of the flow
through the enzyme thermistor, both cellobiose and glucose present in the sample could be determined. The performance with
standard solutions and with crude samples from cellulose degradation experiments was investigated. 相似文献
12.
In typical fermentations at 45‡C on cellulose/corn steep liquor/ammonium and mineral salts medium, growth of the thermophilic
fungus Talaromyces emersonii increases rapidly up to about 50 h and then decreases, presumably because of cell lysis, sporulation, or both. The accumulation
of cellulase activity follows closely on growth and essentially reaches a maximum at about the same time that cell protein
does. By contrast, two peaks of Β-glucosidase activity are observed, one maximal at about 36 h and the second at about 75
h. Fractionation of culture filtrates showed that the cellulase system is comprised of at least four endoglucanases (EC 3.2.1.4),
four or five exoglucanases (cello-biohydrolase; EC 3.2.1.91), and three types of Β-glucosidase (cellobiase; EC 3.2.1.21).
All are glycoproteins. Indeed, variation in carbohydrate content may account for some of the observed multiplicity of enzyme
forms. Although none of the individual components is active against cellulose, reconstitution experiments show that appropriate
mixtures of each type act synergistically to effect hydrolysis of substrate. In addition to the three extracellular Β-glucosidases
I (M r, 135,000), II (M r, 100,000), and III (M r, 45,700), an intracellular form, IV (M r, 57,600), has been isolated. All exist as single polypeptides. The extracellular forms I and III are most active at 70‡C,
pH 5, and have half-lives under these conditions of 6 and 3 h, respectively. By contrast, the intracellular form (IV) is most
active at 35‡C and is rapidly denatured at higher temperatures. Substrate specificity and other studies provide clues to their
possible roles in vivo. Β-Glucosidase III acts as an exoglucohydrolase by removing glucose residues from cellooligosaccharides
arising from the action of endocellulases. Β-Glucosidase I is the major enzyme involved in cleaving cellobiose and short chain
cellooligosaccharides. In doing so it relieves the inhibition by cellobiose of cellulase action.
The intracellular form, Β-glucosidase IV, may have a dual role. By virtue of its transferase activity it may convert incoming
cellobiose to the active inducer of cellulase synthesis, whereas by cleaving cellobiose to glucose (hydrolase action) it provides
energy for the cell and a repressor of cellulase formation. Four endocellulases have been purified to apparent homogeneity
as judged by electrophoresis. Preliminary results show that they all have M r values of about 70,000 and pI values less than 4. However, they differ from one another in carbohydrate content, thermal
stability, and affinity for substrate. The complete cellulase system is most active at pH 4.2, 60–65‡C, and retains about
80% of its original activity after 5 d incubation at 60‡C, pH 5.
Avicel and filter paper most effectively induce synthesis of the complete cellulase system, as measured by the ability of
culture filtrate to digest filter paper. Cotton, Solka floc, and α-cellulose are also effective inducers, as are “wastes”
such as newspaper, straw, and beet pulp. Little or no cellulase synthesis is evident when lactose, cellobiose, or glucose
replaces cellulose in growth media. From a practical viewpoint we find that saccharification of beet pulp is most readily
achieved by using enzyme (i.e., culture filtrate) obtained by growing the organism on medium containing beet pulp as the source
of cellulose. Of the various strains of Talaromyces emersonii investigated for cellulase production, we found CBS 814.70 to be the best, yielding approx. 0.5 IU/mL of culture filtrate.
By medium optimization and genetic manipulation we have isolated a number of mutants of this strain giving 2 IU/mL or more
and enzyme productivities of 20–25 IU/L/h. Xylanase, arabinogalactanase, and pectinase activities have also been detected
in culture filtrates of the organism when grown on beet pulp. Various lignocellulosic materials, including cotton, Solka floc,
Avicel, filter paper, newspaper, and straw, can be degraded by the enzyme system. However, much of our effort has been directed
to investigation of the saccharification of beet pulp since it is available in large quantities at central locations and because
its lignin content is low. About 85% of the dry weight of this material is accounted for by cellulose, hemicellulose, and
pectin in roughly equal proportions. Culture filtrates effect significant saccharification of pulp as measured by the release
of reducing sugars or of glucose. Ball-milling the pulp prior to incubation with enzyme effects considerable improvement in
the extent of digestion. Alkali or peracetic acid pretreatment of the ball-milled substrate facilitates enzymic hydrolysis
even further. Good results are also obtained when unmilled pulp is (a) pretreated with pectinase prior to incubation with
normal culture filtrates or (b) incubated with more concentrated culture filtrates with good pectinase activity. Under suitable
conditions, 80% hydrolysis of beet pulp polysaccharides was achieved in 5 d at 60‡C, pH 5. 相似文献
13.
The filamentous fungus Sclerotinia sclerotiorum produces beta-glucosidases in liquid culture with a variety of carbon sources, including cellulose (filter paper), xylan, barley straw, oat meal, and xylose. Analysis by native polyacrylamide gel electrophoresis (PAGE) followed by an activity staining with the specific chromogenic substrate, 5-bromo 4-chloro 3-indolyl beta-1,4 glucoside (X-glu) showed that two extracellular beta-glucosidases, designated as beta-glu1 and beta-glu2, were in the filter paper culture filtrate. Only one enzyme designated as beta-glu x was revealed by the same method in the xylose culture filtrate. Beta-glu1 and beta-glu2 were purified to homogeneity. The purification procedure consist of a common step of anion-exchange chromatography on DEAE-Sepharose CL6B, both high-performance liquid chromatography (HPLC) anion-exchange and gel filtration columns for beta-glu1 and only HPLC gel filtration for beta-glu2. Beta-glu1 has a molecular mass of 196 kDa and 96.5 kDa, as estimated by gel filtration and sodium dodecyl sulfate (SDS)-PAGE, respectively, suggesting that the native enzyme may consist of two identical subunits. The same analysis showed that beta-glu2 is a monomeric protein with an apparent molecular mass of about 76.5 kDa. Beta-glu1 and beta-glu2 hydrolyses PNPGlc and cellobiose, with apparent Km values respectively for PNPGlc and cellobiose of 0.1 and 1.9 mM for beta-glu1 and 2.8 and 8 mM for beta-glu2. Both enzymes exhibit the same temperature and pH optima for PNPGlc hydrolysis (60 degrees C and pH 5.0). beta-glu1 was stable over a pH range of 3-8 and kept 50% of its activity after 30 min of heating at 60 degrees C without substrate. It was further characterized by studying the effect of some cations and various reagents on its activity. 相似文献
14.
A device with direct sampling, dilution, and sample loading has been utilized to couple a vertically hanging immobilized cellulase bioreactor with a high-performance liquid chromatography system to make a successful on-line analysis of the 3 major carbohydrate products: glucose, xylose, and cellobiose in the cellulase hydrolysate. The coupled analysis system for successive on-line monitoring of the enzymatic hydrolysis of paper cellulose was stable over a period of 96 h. A comparative study involving 4 different quantification methods for the 3 carbohydrates was conducted. The internal standard calibration method with on-line dilution was observed to be the best procedure in terms of accuracy, precision, limit of detection, and systematic error reduction. With this method, the analysis for glucose had 99.9% accuracy, RSD below 2.4%, and a 2.1 ppm detection limit. Matrix matching was found important in the preparation of standard calibration curves with refractive index detection. 相似文献
15.
A commercialized cellulase from Trichoderma reesei has been successfully immobilized by using calcium alginate gel in our laboratory. The waste paper cellulose was hydrolyzed with a special design of the reactor to form a vertically hanging immobilized cellulase under the optimum conditions of pH 4.0 and 45 °C. Glucose, cellobiose and xylose are the major hydrolysis products. The glucose production from the hydrolysis with the vertically hanging immobilized cellulase was about 1.73‐fold better than the freely suspended immobilized cellulase. The average diameter of the immobilized cellulase pellets was 4.190 ± 0.291 mm. UV light irradiation deactivates the activity of the immobilized cellulase. The advantage of the vertically hanging immobilized cellulase reactor is an easy recycle and reuse of the immobilized cellulase. Washing and soaking the recycled immobilized cellulase with distilled water for one day can restore its activity to a small extent. Overall, the application of the hanging immobilized cellulase reactor for waste paper cellulose hydrolysis is successful. 相似文献
16.
The cellulase system of Bacillus circulans F-2 effectively hydrolyzed carboxymethyl cellulose (CMC), xylan, avicel, cellobiose, filter paper, cotton, and p-nitrophenyl-Β-D-cellobioside, and the crude enzyme produced mainly glucose from digestion of avicel. Two major and one minor
peaks of enzyme activities were eluted on DEAE ion-exchange chromatography, and designated cellulase complex I(C-I) and complex
II(C-II) for the two major peaks, and cellulase-III for a minor peak. C-I and C-II were further purified on gel filtration
column of a TSK-Gel SW G3000 ×L. The molecular masses of C-I and C-II were estimated to be about 669 and 443 kDa, respectively.
Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the C-I and C-II complexes showed that the C-I complex
was present as a multiple protein complex, consisting of at least five CMCases and two xylanases, and that the C-II complex
was consisted of at least three CMCase and four xylan ases. C-I showed high activities of cellohydrolase, CMCase, xylanase,
and Β-glucosidase, whereas C-II showed high activities of CMCase, xylanase, avicelase, and Β-glucosidase. The outstanding
property of the C-II was its high hydrolytic activity toward filter paper, a highly resistant substrate against enzymatic
degradation. However, cellulaseIII showed only strong avicelase activity. These results indicated that the cellulase system
of the strain exists as multiple complex forms. 相似文献
17.
The effects of long-chain fatty alcohols (LFAs) on the enzymatic hydrolysis of crystalline cellulose by two commercial Trichoderma reesei cellulase cocktails (CTec2 and Celluclast 1.5L) were studied. It was found that n-butanol inhibited the enzymatic hydrolysis, but n-octanol, n-decanol and n-dodecanol had strong enhancement on enzymatic hydrolysis of crystalline cellulose in the buffer pH range from 4.0 to 6.0. LFAs can increase the hydrolysis efficiency of crystalline cellulose from 37 to 57 % at Celluclast 1.5L loading of ten filter paper units (FPU)/g glucan. LFAs have similar enhancement on the enzymatic hydrolysis of crystalline cellulose mixed with lignin or xylan. The enhancement of LFAs increased with the decrease of the crystallinity index. LFAs not only enhanced the high-solid enzymatic hydrolysis of lignocellulose, but also improved the rheological properties of high-solid lignocellulosic slurries by decreasing the yield stress and complex viscosity. Meanwhile, LFAs can improve the enzymatic hydrolysis of cellobiose to glucose, especially at low cellulase loading. 相似文献
18.
The use of the intensive mass transfer reactor (IMTR) for enzymatic saccharification of cellulose, where the reaction mixture
is intensively stirred by ferromagnetic particles (FMP), enhances the process rate and productivity drastically. The most
significant enhancement of the process was observed when microcrystalline cellulose was used as a substrate. A concentration
of sugars up to 5% was obtained after 1 h of cellulose hydrolysis using a cellulase activity level of 2 filter paper units
(FPU)/mL (20 FPU/g substrate). In the hydrolysis of two types of industrial cellulosic wastes, the enhancement effects were
less pronounced. Parameters related to the IMTR design, such as the shape, dimensions, and mass of FMP, as well as the magnetic
field strength, strongly affected the process of hydrolysis. Among various kinds of FMP tested, the most efficient were found
to be cylindrical particles (0.25 x 4 mm). In general, the hydrolysis rate enhanced when the magnetic field strength increased
from 26,000 to 64,000 A/m. An optimal FMP loading existed at each level of the field strength. Hydrolyzates obtained in the
IMTR under the action of Trichoderma reesei and Penicillium verruculosum cellulases contained glucose and cellobiose as soluble products, cellobiose being predominant (> 50%). Only when a high level
of extra Β-glucosidase was added to the IMTR (10 CBU/mL), did glucose made up more than 90% of the products. Owing to extreme
shear conditions in the IMTR, significant enzyme inactivation took place. 相似文献
19.
A cellulase production process was developed by growing the fungi Trichoderma reesei and Aspergillus phoenicis on dairy manure. T. reesei produced a high total cellulase titer (1.7 filter paper units [FPU]/mL, filter paper activity) in medium containing 10 g/L
of manure (dry basis [w/w]), 2 g/L KH 2PO 4, 2 mL/L of Tween-80, and 2mg/L of CoCl 2. However, β-glucosidase activity in the T. reesei-enzyme system was very low. T. reesei was then cocultured with A. phoenicis to enhance the β-glucosidase level. The mixed culture resulted in a relatively high level of total cellulase (1.54 FPU/mL)
and β-glucosidase (0.64 IU/mL). The ratio of β-glucosidase activity to filter paper activity was 0.41, suitable for hydrolyzing
manure cellulose. The crude enzyme broth from the mixed culture was used for hydrolyzing the manure cellulose, and the produced
glucose was significantly ( p<0.01) higher than levels obtained by using the commercial enzyme or the enzyme broth of the pure culture T. reesei. 相似文献
20.
A quantitative approach was taken to determine the inhibition effects of glucose and other sugar monomers during cellulase
and β-Glucosidase hydrolysis of two types of cellulosic material: Avicel and acetic acid-pretreated softwood. The increased
glucose content in the hydrolysate resulted in a dramatic increase in the degrees of inhibition on both β-Glucosidase and
cellulase activities. Supplementation of mannose, xylose, and galactose during cellobiose hydrolysis did not show any inhibitory
effects on β-Glucosidase activity. However, these sugars were shown to have significant inhibitory effects on cellulase activity
during cellulose hydrolysis. Our study suggests that high-substrate consistency hydrolysis with supplementation of hemicellulose
is likely to be a practical solution to minimizing end-product inhibition effects while producing hydrolysate with high glucose
concentration. 相似文献
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