Characterization and Structure of the Cellulase Gene of<i>Bacillus subtilis</i>BSE616

Park, Seung-Hwan; Kim, Ha Keun; Pack, M. Y.

doi:10.1080/00021369.1991.10870613

Cited by 3 publications

(3 citation statements)

References 10 publications

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“…Recently the domain organizations of fimgal and bacterial cellulases were summarized (9). An endo-I]-1,4-glucanase gene isolated from a Bacillus subtilis BSE616 had been cloned in Escherichia coil (10) and its gene was characterized (11) previously. The endo-13-1,4-glucanase gene cloned on pBS1, a derivative of amplifiable plasmid pBR322, was expressed effectively in E. coli HB101 to produce the enzyme with 40-fold of original gene source strain of B. subtilis.…”

Section: Similar Results Have Been Accumulated In Bacterial Cellulasementioning

confidence: 99%

Adsorption of Bacillus subtilis endo‐β‐1,4‐glucanase to cellulosic materials

et al. 1997

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Summary: The intact and the trtmcated endo-13-1,4-glucanase expressed in Bacillus megaterium by a B. subtilis gene were purified and its adsorption characteristics to cellulosic materials were investigated. The intact enzyme was purified by affinity towards insoluble cellulose and Mono-Q chromatography. The truncated enzyme was purified by gel filtration and chromatofocusing. The molecular activities of these enzymes towards the soluble substrates were identical. Optimum pH and temperature of these two types of enzyme were same, 5.5 and 60~ respectively. However, the insoluble substrate, Avicel, was hydrolyzed slowly by the intact endoglucanase while the tnmcated endoglucanase did not hydrolyze the Avicel. Isoelectric points of the intact and the trtmcated enzyme were 6.2 and 5.6, respectively. In a Sephadex column the large form of intact endoglucanase was eluted later than the small form of truncated enzyme. Only the intact enzyme was strongly adsorbed to Avicel. The practical maximum adsorption was about 20 mg/g of Avicel at pH 6.0 and 4~

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Section: Similar Results Have Been Accumulated In Bacterial Cellulasementioning

confidence: 99%

Adsorption of Bacillus subtilis endo‐β‐1,4‐glucanase to cellulosic materials

et al. 1997

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“…In addition to isolating cellulolytic microbes, reduction of enzyme production costs and enhancement of cellulase activity have become major areas of research [13]. The cellulase genes of many microorganisms have been cloned and the nucleotide sequences of endo-β-1,4-glucanase genes from several Bacillus strains have been determined [16,18,19,21,23]. The study of cellulolytic enzymes at the molecular level has revealed some of the modular features that contribute to their catalytic activity [22, see review].…”

Section: Introductionmentioning

confidence: 99%

COMPARISON OF NUCLEOTIDE SEQUENCES OF ENDO-Β-1,4-GLUCANASE GENES FROM Bacillus subtilis STRAINS

HWAN¹,

KYOUNG²,

JEONG³

2012

Int J of Biot Appl

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Three Bacillus subtilis strains were isolated from soil, compost and animal waste slurry in Jeju Island, Korea and their endo-β-1,4glucanase genes cloned. Cellulase genes from B. subtilis SL9-9, C5-16 and S52-2 encoded proteins of 480, 470 and 499 amino acid residues, respectively. DNA sequences of the genes were compared with those of other known cellulase genes. The deduced amino acid sequences of the cellulase genes from the isolates matched quite well the modern concepts of multidomain cellulolytic enzymes. The enzymes were composed of three discrete domains: catalytic domains (CD) of glucosyl hydrolase family 5/A2 and interdomain linker and cellulosebinding domains (CBD) of family IIIa. Similar to the modular organization of many Bacillus endoglucanases, the CDs of these enzymes were located in the N-terminal region and CBDs in the C-terminal region.

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“…We have previously cloned an endoglucanase gene of Bacillus subtilis and a Bglueosidase gene of Cellulomonasfimi and determined their nucleotide sequences (Park and Pack, 1986;Park et al, 1991). The studies were further extended to biochemical and microbiological studies using purified endoglucanase from E. coli, B. subtilis and B. megaterium to characterize enzymatic properties as well as to select suitable bacterial host strains for high enzyme production (Lee and Pack, 1987;Kim and Pack, 1988;Lee et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Simultaneous overproduction of extracellular endoglucanase and intracellular ?-glucosidase by genetically engineered Bacillus subtilis

1995

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Simultaneous overproduction of intracellular B-glucosidase and extracellular endoglucanase was attempted by constructing two artificial operon systems comprising the B-glucosidase-endoglueanase gene(BE) or the endoglucanase-B-glucosidase gene(EB) under the control of a strong engineered promoter, BJ27UA88 and expressing them in Bacillus subtilis DB104. Two artificial operon systems contained 30 bp or 5 bp gap between the termination codon of the upstream gene and the SD sequence of the downstream gene, respectively. These operon systems were expressed well in B. subtilis and overproduced the B-glucosidase cell extract as well as the endoglucanase supematant. The level of expression in the operon system was almost the same as that in a single expression system.

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Characterization and Structure of the Cellulase Gene ofBacillus subtilisBSE616

Cited by 3 publications

References 10 publications

Adsorption of Bacillus subtilis endo‐β‐1,4‐glucanase to cellulosic materials

Adsorption of Bacillus subtilis endo‐β‐1,4‐glucanase to cellulosic materials

COMPARISON OF NUCLEOTIDE SEQUENCES OF ENDO-Β-1,4-GLUCANASE GENES FROM Bacillus subtilis STRAINS

Simultaneous overproduction of extracellular endoglucanase and intracellular ?-glucosidase by genetically engineered Bacillus subtilis

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