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1 and Ab/aptamer reporter molecules linked to cellulase.
2 degrees C) without or with hemicellulase or cellulase.
3 completion without expression of a family 48 cellulase.
4 pectin methylesterase, polygalacturonase and cellulase.
5 e reaction after nitrocellulose digestion by cellulase.
6 ter removing mucilage using the xylanase and cellulase.
7 ere able to strongly enhance the activity of cellulases.
8 n cellulosome chimeras with key cellulosomal cellulases.
9 nding module from CipA in complex with Cel8A cellulases.
10 monooxygenases that enhance the activity of cellulases.
11 lly, which confirmed that these proteins are cellulases.
12 Family 6 cellulases compared to GH Family 7 cellulases.
13 to computationally distinguish them from non-cellulases.
14 ntly increases product binding to processive cellulases.
15 ulases much more strongly than nonprocessive cellulases.
16 used to screen metagenomics data for "true" cellulases.
17 can be accomplished by fungal and bacterial cellulases.
18 re optimal for activity of commercial fungal cellulases.
19 ganism despite the presence of several other cellulases.
20 ollection contains hundreds of highly stable cellulases.
21 icyanide, on nitrocellulose films treated by cellulases.
22 vated temperatures, unlike commercial fungal cellulases.
23 om the performance barriers affecting fungal cellulases.
24 trategy that utilizes multi-catalytic domain cellulases.
25 of a range of glycoside hydrolases including cellulases.
26 t information for the selection of technical cellulases.
27 (6 and 10ppm), xylanase (70 and 120ppm) and cellulase (35 and 60ppm) on the rheological properties o
28 ld (369.23+/-0.11mug) in 1h in comparison to cellulase (359+/-0.30mug) and pectinases (333+/-0.55mug)
30 ctrochemical assay for the total activity of cellulase, a hydrolytic enzyme widely used in food and t
31 f cellulose synthesis in Archaeplastida, and cellulases absent in terrestrial plants as well as the o
32 a comprehensive kinetic model for processive cellulases acting on insoluble substrates to explain thi
33 yet this approach has not been utilized for cellulases acting on their natural substrate, insoluble
41 ited a more generalist phenotype with higher cellulase activity and growth capabilities on different
45 eans of inducing an organism-level change in cellulase activity is to use laboratory adaptive evoluti
50 ourse of evolution concurrent with decreased cellulase activity, increased intracellular ATP concentr
51 to cellulose is known to be proportional to cellulase activity, such that increasing binding affinit
62 loped by pre-treating the stevia leaves with cellulase and adding soluble starch as the glucosyl dono
64 e of 36-45min and the cocktail of pectinase, cellulase and hemicellulase, set at 2% each, gave the be
65 iments are presented that utilize commercial cellulase and laccase enzymes, which are known to modify
66 er, the presence of xylanase, alpha-amylase, cellulase and lipase resulted in bread with greater quan
67 hing to a catalytic site template from a GH9 cellulase and other analyses point to a putative catalyt
68 rs, agitation, liquid/solid (L/S) ratio, and cellulase and protease addition, on extraction yield of
70 xtraction by using three enzymes (pectinase, cellulase and tannase) and an enzymatic blend to increas
71 ndent variables: temperature, pH, pectinase, cellulase and tannase; and a subsequent optimization thr
73 t extracted with carbohydrases, Viscozyme or Cellulase and then hydrolyzed with proteases (Alcalase,
76 60 most upregulated ones that comprised two cellulases and a cellulose synthase was conserved among
78 e enzymes enhance the hydrolytic activity of cellulases and are essential for cost-efficient conversi
80 s identified structural elements that define cellulases and can be used to computationally distinguis
82 al methods are unable to distinguish between cellulases and enzymes with different substrate specific
83 ymes in buffalo rumen metagenome and that of cellulases and hemicellulases in termite hindgut was obs
84 be used for in silico discrimination between cellulases and non-cellulases belonging to GH48 is an om
85 approach supported by experimental studies, cellulases and non-cellulases can be effectively identif
86 work focuses both on improved attributes of cellulases and on the domains of cellulase that have bee
87 robes including Clostridium species organize cellulases and other glycosyl hydrolases into large comp
89 repancies reported for binding constants for cellulases and suggest that product inhibition will vary
91 ability by imaging the distribution of major cellulases and xylanases in Trichoderma reesei using the
93 All of these approaches involve multiple cellulases and, since cellulose is insoluble and microor
94 y Eng-1, Cathepsin S-like cysteine protease, cellulase, and two unknown genes with secretory characte
95 to dabsyl-tagged enzyme substrates to screen cellulases, and for the analysis of plant cell wall hemi
96 ies on the consortium, a 90 kDa, multidomain cellulase, annotated as a member of the TIM barrel glyco
98 lternatively, in certain anaerobic microbes, cellulases are assembled into large multienzymes complex
99 some, CelR also regulates cellulases, while cellulases are controlled by different regulatory sites
101 microorganisms cannot ingest particles, the cellulases are present outside of the cell although they
107 nzymatically responsive to both nuclease and cellulase, as well as small molecules, showing great pot
108 the basis of its ease of use, we expect this cellulase assay platform to be applicable to enzyme scre
109 iently degrades beta-1,4-glucans in in vitro cellulase assays with carboxymethyl-cellulose as substra
111 co discrimination between cellulases and non-cellulases belonging to GH48 is an omega-loop located on
113 tion of expansins for cellulose digestion by cellulases, but only rarely to an extent that is commerc
114 wer binding partition coefficient for fungal cellulases, but surprisingly, it enhanced hydrolytic act
115 duct binding on processive and nonprocessive cellulases by calculating the binding free energy of cel
117 ost cellulolytic bacteria have one family 48 cellulase, C. thermocellum has two, Cel48S and Cel48Y.
118 esults show for the first time that a single cellulase can be essential for cellulose degradation by
119 y of the extracellular enzymes ligninase and cellulase can be used to track changes in the predominan
121 by experimental studies, cellulases and non-cellulases can be effectively identified within a given
122 Cellulose is the main polymer in biomass and cellulases can hydrolyze it to cellobiose, which can be
125 e find that the two most abundantly secreted cellulases, CBH-1 and CBH-2, depend on distinct ER cargo
126 s a suite of enzymes including endo- and exo-cellulases, CBM33 polysaccharide-monooxygenases, and hem
127 e binding mode, Doc124A directs the appended cellulase, Cel124A, to the surface of C. thermocellum an
128 ynergistic GH9 with the major endoprocessive cellulase Cel48F, but also identify Cel9U as an importan
130 exation and decomplexation of the processive cellulase Cel7A and its insoluble substrate, cellulose.
131 e pre-steady-state regime for the exo-acting cellulase Cel7A using amperometric biosensors and an exp
133 equence is 78% identical to the cellulosomal cellulase Cel9E, was found inactive in the free and comp
135 CBM) 4 Ig fused domain from the cellulosomal cellulase cellobiohydrolase A (CbhA) of Clostridium ther
136 mbination enables quantitative prediction of cellulase chimera thermostability and efficient identifi
137 nt markedly enhanced potential activities of cellulase (CL), beta-glucosidase (BG), lignin peroxidase
138 ands are disrupted by water in nonprocessive cellulase clefts, and the lack of long tunnel-forming lo
140 sLac acted synergistically with a commercial cellulase cocktail to increase glucose production from S
143 could potentially be used to design improved cellulase cocktails, thus lowering the overall cost of b
144 of the biochemically characterized bacterial cellulases come from only a few cellulose-degrading bact
150 which requires neither an edible plant nor a cellulase, could enable crude biomass to be the sole sou
151 onstrate that the small, noncomplexed fungal cellulases deconstruct cell walls using mechanisms that
154 The sole noncellulosomal GH9 (Cel9W) is a cellulase displaying a broad substrate specificity, whos
155 nt within and between twins (e.g., predicted cellulases, dockerins), and transcriptional activities.
156 less severe pretreatment and 300-400% lower cellulase dosages for equivalent product yields using si
157 Understanding the enzymatic mechanism that cellulases employ to degrade cellulose is critical to ef
158 mising approach involves the application of "cellulase-enhancing factors," such as those from the gly
161 enesis to validate these findings on a model cellulase enzyme, an endoglucanase from the thermophilic
165 errogate the requirements for trafficking of cellulase enzymes from the endoplasmic reticulum to the
166 , in which polysaccharides are hydrolyzed by cellulase enzymes into simple sugars and fermented to et
169 he fungus Trichoderma reesei, which secretes cellulase enzymes to hydrolyze lignocellulosic biomass i
170 enzymatic digestion reveals that processive cellulases exploit these defects as initiation sites for
171 enome scale for diverse phenotypes including cellulase expression, isobutanol production, glycerol ut
174 ological perspective due to the diversity of cellulase families, their unique assembly and substrate
175 ves, GH74 was originally considered to be a "cellulase" family, although more recent studies have gen
178 eatly facilitate the engineering of improved cellulases for the large-scale conversion of plant bioma
179 es, and structure of a unique endogenous GH7 cellulase from an animal, the marine wood borer Limnoria
182 cific genomic locus that encodes multidomain cellulases from GH families 9 and 48, which are associat
184 quid tolerance among three distinct family 5 cellulases from Trichoderma viride, Thermogata maritima,
186 lucosidase activity, but efficiently induces cellulase gene expression and cellulolytic activity in t
187 of the clr-2 homolog (clrB) failed to induce cellulase gene expression and lacked cellulolytic activi
188 porters (Delta3betaGDelta2T) does not induce cellulase gene expression in response to cellobiose.
189 ns for both transporters is unable to induce cellulase gene expression in response to crystalline cel
190 lucosidase activity, but efficiently induces cellulase gene expression in the presence of cellobiose,
194 y shows that deletion of the single family 9 cellulase gene in Clostridium phytofermentans prevents g
196 argeted gene disruptions of all 13 predicted cellulase genes showed that only cel5B and cel6A were re
197 verify the importance of a highly expressed cellulase (GH6 family cellobiohydrolase) and the CebR tr
198 , combination of alpha-amylase, xylanase and cellulase had a synergetic effect on the dough rheology.
199 A new method to determine the activity of cellulase has been developed using a quartz crystal micr
200 The intrinsic processivity (P(Intr)) of cellulases has been shown to be governed by the rate con
201 3 fungal class II cellobiohydrolases (CBH II cellulases) has yielded a collection of highly thermosta
203 catalytic subunits containing cell-adherent cellulases, hemicellulases, xylanases, and other glycosi
206 udies determined the role of rhizobial CelC2 cellulase in different steps of the symbiotic interactio
208 e measured hydrolytic rates of four purified cellulases in small increments of temperature (10-50 deg
210 f all ESTs represent genes encoding putative cellulases, including glycosyl hydrolase family 7 (GH7)
213 ontrast Cel12A, a bifunctional xyloglucanase/cellulase, induced creep with only subtle changes in wal
214 leads to the conclusion that synergism among cellulases is morphology-dependent and governed by the c
221 tive N-glycosylation sites are quite rare in cellulase linkers, while an N-P motif, which strongly di
223 h known activities comprising (carboxymethyl)cellulases, mixed-linkage endo-glucanases, and endo-xylo
224 at enhanced levels of HjCel3A in H. jecorina cellulase mixtures benefit the conversion of cellulose t
227 LPMOs that are present in current commercial cellulase mixtures in part is due to hitherto undetected
230 suggest that cellobiose binds to processive cellulases much more strongly than nonprocessive cellula
231 Overall, this study suggests that marine cellulases offer significant potential for utilization i
234 structural characterization of the action of cellulases on a nano-flat cellulose preparation, which e
237 three enzymes; alpha-amylase, pectinase and cellulase onto amino-functionalized magnetic nanoparticl
238 proach to be amenable to thermophile-derived cellulases or to the separation of multiple species usin
240 tevioside from Stevia rebaudiana leaves with cellulase, pectinase and hemicellulase, using various pa
241 inations of solvent and enzyme, enzyme type (cellulase, pectinase, ss-glucosidase), and hydrolysis ti
244 for reliable computational identification of cellulases precludes their exploration in the genomic da
245 surface ablation mechanism driven by general cellulase processivity, but also excavates extensive cav
246 To provide molecular level insights into cellulase product inhibition, we examine the impact of p
247 ngineering of filamentous fungi for improved cellulase production is hampered by our incomplete knowl
249 of application of alpha-amylase, viscozyme, cellulase, protease and pectinase enzymes to ginger on t
251 Both the development and the application of cellulases require an understanding of the activities of
255 nd the molecular-level implications of pH in cellulase structure, we use a hybrid, solvent-based, con
257 anization resembles the one adopted by other cellulases (such as cellobiohydrolases, for example) tha
258 to biofuels is dependent on highly efficient cellulase systems that produce near-quantitative levels
259 endoglucanase (EG), the major components of cellulase systems, take on distinct roles: EG and CBH II
264 n intermediate strategy, secreting many free cellulases that contain multiple catalytic domains.
265 aori: to join), not directly associated with cellulases, that mediate attachment to cellulose by spec
266 atically (beta-glucuronidase/arylsulphatase, cellulase), the compounds separated on a reversed phase
268 allinity substrates making it the only known cellulase to function well on highly crystalline cellulo
270 ondition obtained was: liquid to solid (LS), cellulase to xylanase and enzymes to matter ratios of 22
271 y, we show that prior action of LPMO enables cellulases to attack otherwise highly resistant crystall
272 r 2 CBMs, from both bacterial and eukaryotic cellulases to identify conserved characteristics potenti
275 alpha- and gamma-tocopherols in hot-air and cellulase treated rice bran were remained unchanged.
277 n of the lignocellulosic residue followed by cellulase treatment and conversion to ethanol at a high
279 with the sensitivity of their directions to cellulase treatment, indicates they most likely reflect
283 and and the cellobiose product in processive cellulase tunnels and the additional stabilization from
285 to D-lactate (50 degrees C and pH 5.0), the cellulase usage could be reduced to 1/3 that required fo
286 of the structural and dynamic features that cellulases utilize to bind a single strand of crystallin
287 demonstrate how the synergistic activity of cellulases was enhanced by altering the hydrogen bond ne
289 Gal), endo-1,4-beta-D-glucanase (EGase), and cellulase were monitored during growth and ripening of S
291 o effect on product binding in nonprocessive cellulases, whereas it significantly increases product b
293 ndustrially important GH Family 7 processive cellulases with free energy perturbation/replica-exchang
294 are the Cel7A linker with linkers from other cellulases with sequence-based tools to predict disorder
296 Family 7 enzymes from other genera and other cellulases within T. reesei may not be as disordered, wa
299 med the biochemical activities of a GH5-GH10 cellulase-xylanase and a GH11-CE4 xylanase-esterase.
300 xylanase under five different combinations (cellulase/xylanase: 50/0, 50/25, 50/50, 25/50, and 0/50