Amino Acid Sequence and Stereoselective Hydrolytic Reaction of an Endo-1,4-<i>β</i>-glucanase from a<i>Bacillus</i>Strain

Hitomi, Jun; Hatada, Yuji; Kawaminami, Shunro; Kawai, Shuji; Ito, Susumu

doi:10.1271/bbb.61.2004

Cited by 5 publications

(1 citation statement)

References 15 publications

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“…Phylogenetic analysis was performed using the PHYLIP v.3.5c software package (Felsenstein 1993) and employed a Bacillus sp. EGase (Hitomi et al 1997) as the nominated out-group. Tree topology and evolutionary distances were estimated by the maximum parsimony method and also by neighbour-joining using Kimura distances.…”

Section: Protein Sequence Analysis and Phylogenymentioning

confidence: 99%

A causal role for ethylene and endo‐β‐1,4‐glucanase in the abscission of red‐raspberry (Rubus idaeus) drupelets

Iannetta¹,

Wyman

Neelam

et al. 2000

Physiologia Plantarum

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During raspberry (Rubus ideaus L. cv Glen Clova) fruit ripening, endo‐β‐1,4‐glucanase (EGase; EC 3.2.1.4) specific activity (per g fresh weight) increases approximately 15‐fold. Highest activity was associated with the surfaces of the receptacles where the weakening abscission zones are located. Immunoblotting using antibodies raised against a bean abscission‐EGase (ab.‐EGase) identified a single protein of Mr 52 kDa that was present only in ripe fruit and was most prominent in the receptacle. Using reverse transcription‐polymerase chain reaction (RT‐PCR), two 497‐bp partial putative EGase clones were obtained from ripe receptacle mRNA (termed RI‐EGL1 and 2) which share 53% amino acid identity. The more abundant RI‐EGL1 was used to obtain its full length clone from a ripe receptacle cDNA library. The deduced amino acid sequence of RI‐EGL1 was similar to other ab.‐EGase sequences (ca 67%) and contained the conserved motifs present in all E2‐class EGases. Northern analysis revealed that RI‐EGL1 expression was limited to ripe‐fruit receptacles. Application of the ethylene antagonist 1‐methylcyclopropene (1‐MCP) to green fruits indicated that endogenous ethylene accelerates raspberry abscission and increases both EGase activity and RI‐EGL1 expression.

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Section: Protein Sequence Analysis and Phylogenymentioning

confidence: 99%

A causal role for ethylene and endo‐β‐1,4‐glucanase in the abscission of red‐raspberry (Rubus idaeus) drupelets

Iannetta¹,

Wyman

Neelam

et al. 2000

Physiologia Plantarum

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Molecular characterization of a β-1,4-endoglucanase from an endophytic Bacillus pumilus strain

Lima

Quecine

Fungaro

et al. 2004

Appl Microbiol Biotechnol

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Endophytes comprise mainly microorganisms that colonize inner plant tissues, often living with the host in a symbiotic manner. Several ecological roles have been assigned to endophytic fungi and bacteria, such as antibiosis to phytopathogenic agents and plant growth promotion. Nowadays, endophytes are viewed as a new source of genes, proteins and biochemical compounds that may be used to improve industrial processes. In this study, the gene EglA was cloned from a citrus endophytic Bacillus strain. The EglA encodes a beta-1,4-endoglucanase capable of hydrolyzing cellulose under in vitro conditions. The predicted protein, EglA, has high homology to other bacterial cellulases and shows a modular structure containing a catalytic domain of the glycosyl hydrolase family 9 (GH9) and a cellulose-binding module type 3 (CBM3). The enzyme was expressed in Escherichia coli, purified to homogeneity, and characterized. EglA has an optimum pH range of 5-8, and remarkable heat stability, retaining more than 85% activity even after a 24-h incubation at pH 6-8.6. This characteristic is an important feature for further applications of this enzyme in biotechnological processes in which temperatures of 50-60 degrees C are required over long incubation periods.

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Molecular and biochemical characterization of Ba-EGA, a cellulase secreted by Bacillus sp. AC-1 from Ampullaria crosseans

Zhang

Yin

et al. 2007

Appl Microbiol Biotechnol

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A novel gene (Ba-ega) of Bacillus sp. AC-1, encoding an endoglucanase (Ba-EGA), was cloned and expressed in Escherichia coli. Ba-ega, containing a 1,980-bp open reading frame (ORF), encoded a protein of 659 amino acids and had a molecular mass of 74.87 kDa. Ba-EGA was a modular enzyme composed of a family-9 glycosyl hydrolase catalytic module (CM9) and a family-3 carbohydrate-binding module (CBM3). To investigate the functions of the CBM3 and CM9, a number of truncated derivatives of Ba-EGA were constructed, and all were active. The catalytic module (rCM9) alone was less stable at high temperature than the recombinant Ba-EGA (rBa-EGA). The temperature stability for the complex of rCM9 and rCBM3 was still lower than rBa-EGA, but higher than rCM9 alone. These observations indicated the existence of a non-covalent interaction between CM9 and CBM3 that might strengthen the stability of CM9. However, this interaction is not strong enough to mimic the protective effect of the CBM in the wild-type enzyme.

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Amino Acid Sequence and Stereoselective Hydrolytic Reaction of an Endo-1,4-β-glucanase from aBacillusStrain

Cited by 5 publications

References 15 publications

A causal role for ethylene and endo‐β‐1,4‐glucanase in the abscission of red‐raspberry (Rubus idaeus) drupelets

A causal role for ethylene and endo‐β‐1,4‐glucanase in the abscission of red‐raspberry (Rubus idaeus) drupelets

Molecular characterization of a β-1,4-endoglucanase from an endophytic Bacillus pumilus strain

Molecular and biochemical characterization of Ba-EGA, a cellulase secreted by Bacillus sp. AC-1 from Ampullaria crosseans

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