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1 degradation of cellulose in the presence of endoglucanase.
2 off-rates, processivity, and synergism with endoglucanase.
3 y 9 of the glycosidases, suggesting it is an endoglucanase.
4 s mixtures of commercially relevant exo- and endoglucanases.
5 s unusual in its abundance of GH5-containing endoglucanases.
6 llulosome as well as the previously reported endoglucanases.
10 raction with CESAs in vitro, suggesting that endoglucanase activity is important for cellulose synthe
11 secrete two beta1,3-glucanases and that Eng1 endoglucanase activity is the predominant factor respons
17 lucanases are functionally equivalent to the endoglucanases and cellobiohydrolases required for other
19 nificant differences between hydrolysis with endoglucanases and cellulase mixtures were observed.
20 ch also comprises a broad range of microbial endoglucanases and endogalactanases, as well as yeast ce
22 PhcA-regulated factors exopolysaccharide I, endoglucanase, and pectin methyl esterase was reduced 10
23 is protein is uncommon for hyperthermophilic endoglucanases, and two of the four domains of the enzym
25 ed in GH7 cellobiohydrolases, but not in GH7 endoglucanases, at the leading glucosyl ring provide the
27 erins, it was also shown that the binding of endoglucanase B (EngB) to CbpA was dependent on the pres
29 d from EcCel5A, a Eubacterium cellulosolvens endoglucanase, bind to a range of beta-glucans but, uniq
30 n of a recoverable, thermoresponsive polymer-endoglucanase bioconjugate that matches the activity of
32 ucture of the catalytic core of the family 5 endoglucanase, Ce15A, from the alkalophilic Bacillus aga
37 f this strategy, we isolated variants of the endoglucanase Cel5A, from the plant-pathogenic fungus Fu
39 ated that three of the 12 predicted beta-1,4 endoglucanases (cel5A, cel5B, and cel45A) and the sole p
41 ural synthetic enzymatic pathway composed of endoglucanase, cellobiohydrolyase, cellobiose phosphoryl
42 omic organization of genes encoding beta-1,4-endoglucanases (cellulases) from the plant-parasitic cys
44 module from the Bacillus sp. 1139 family GH5 endoglucanase, comprising a 191 amino acid protein, has
45 ith additional enzymes, including a family-5 endoglucanase, confirmed the conclusion that to cause cr
46 an unusual family 9 enzyme, is a processive endoglucanase containing a catalytic domain closely link
50 ression of a bacterial gene, celE', encoding endoglucanase E' (EGE'), was investigated in the pancrea
53 I, CBH II) and an internally chain-cleaving endoglucanase (EG), the major components of cellulase sy
54 lso report the identification of two soybean endoglucanases: EGaseA, which acts as a high-affinity li
57 ion of the synergism between randomly acting endoglucanases (EGs) and chain end-specific processive c
59 is study, we enhanced the thermostability of endoglucanase EngB, one component of the cellulase compl
60 t recombinant cellulosomes containing either endoglucanase EngE, endoglucanase EngH, or exoglucanase
61 osomes containing either endoglucanase EngE, endoglucanase EngH, or exoglucanase ExgS bound to mini-C
62 ne in Clostridium cellulovorans that encodes endoglucanase EngL, which is involved in plant cell wall
63 eotide sequence contained reading frames for endoglucanase EngO, a putative response regulator, and a
66 ty assays mapped the distribution pattern of endoglucanase, exoglucanase and xylanase activity throug
68 dation requires a suite of enzymes including endoglucanases, exoglucanases, and beta-glucosidases.
69 uctural analysis of a unique, mixed function endoglucanase from black cottonwood (Populus trichocarpa
71 ese findings on a model cellulase enzyme, an endoglucanase from the thermophilic Pyrococcus horikoshi
73 lostridium cellulovorans (strain ATCC 35296) endoglucanase gene engF has been isolated and sequenced.
78 amylase, the secretion of Trichoderma reesei endoglucanase I (EGI) was not influenced by the YlPMR1 d
79 Our study establishes the important role of endoglucanase in cellulose synthesis and cellulose micro
80 be similar to the xyloglucan-specific fungal endoglucanase inhibitor protein (XEGIP) precursor in tom
83 unique polymer is hydrolyzed by the specific endoglucanase lichenase, but, unlike lichenan and barley
84 other enzymes, strongly suggesting that dual endoglucanase-mannanase activity is widespread in this f
86 portions of ORFs denoted in M. jannaschii as endoglucanase (MJ0555), transketolase (MJ0681), thiamine
87 ly regulated plant genes encoding a beta,1-3 endoglucanase (MtBGLU1), a lectin (MtLEC4), and a cystei
88 onfirmed the conclusion that to cause creep, endoglucanases must cut both xyloglucan and cellulose.
89 the activities of exocellobiohydrolases and endoglucanases needs to be re-appraised in both species.
90 protein CbpA, the exoglucanase ExgS, several endoglucanases of family 9, the mannanase ManA, and the
91 ve 2.5-fold improvement in the display of an endoglucanase on the yeast surface by optimizing multipl
92 hermore, silencing of the elicitor-releasing endoglucanase (PR-2) led to a loss of HR cell death and
93 ogen-secreted apoplastic xyloglucan-specific endoglucanase, PsXEG1, is a focus of this struggle in th
94 1831, Ra2461, and Ra2535) were identified as endoglucanases, releasing predominantly cellobiose and c
98 s the surface, as has been observed in other endoglucanase structures, and is potentially able to acc
99 failed to induce cell wall creep, whereas an endoglucanase that hydrolyzes both xyloglucan and cellul
101 reviously identified plant EGases are E-type endoglucanases that possess signal sequences for endopla
102 tically with a cognate cellobiohydrolase and endoglucanase to completely release, from a cellulosic s
103 icroscopy (AFM) with a stretching device and endoglucanase treatment that induces wall stress relaxat
104 M) with nanogold affinity tags and selective endoglucanase treatments to assess the spatial location
105 ding a serine protease, and engXCA, encoding endoglucanase) was reduced in the rpfA mutant background
106 cellulases and to a single putative beta-1-4 endoglucanase were expressed at high levels relative to
109 rCel7A is a cellobiohydrolase rather than an endoglucanase, with a cellulose-binding tunnel that is m
111 hydrolytic activity of a xyloglucan-specific endoglucanase (XEG) from the fungus Aspergillus aculeatu
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