Enzymatic properties, crystallization, and deduced amino acid sequence of an alkaline endoglucanase from Bacillus circulans

A high-isoelectric-point (p I), alkaline endo-1,4-β-glucanase (Egl-257) of Bacillus circulans KSM-N257 was purified to homogeneity and crystallized. The purified enzyme hydrolyzed carboxymethyl cellulose (CMC) with optima of pH 8.5 and 55 °C. The molecular mass was 43 kDa, and the p I was pH 9.3. Th...

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Vydáno v:	Biochimica et Biophysica Acta (BBA) - General Subjects Ročník 1570; číslo 3; s. 174 - 180
Hlavní autoři:	Hakamada, Yoshihiro, Endo, Keiji, Takizawa, Shuichi, Kobayashi, Tohru, Shirai, Tsuyoshi, Yamane, Takashi, Ito, Susumu
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Netherlands Elsevier B.V 15.04.2002 Elsevier BV
Témata:	Amino Acid Sequence Bacillus Bacillus - enzymology Base Sequence Carboxymethylcellulose Sodium Carboxymethylcellulose Sodium - metabolism Cellulase Cellulase - chemistry Cellulase - genetics Cloning Crystallization Crystallography, X-Ray Family 8 Glycosyl hydrolase Hydrogen-Ion Concentration Hydrolysis Isoelectric Point Lichenase Molecular Sequence Data Molecular Weight Open Reading Frames Protein Conformation Sequence Alignment aa Cloning nt Crystallization Glycosyl hydrolase PAGE Egl Cellulase Family 8 Bacillus Lichenase CMC p I PCR
ISSN:	0304-4165, 0006-3002, 1872-8006
On-line přístup:	Získat plný text
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