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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Purification and characterization of a new endo-1,4-beta-D-glucanase from Beltraniella portoricensis.

A new endoglucanase, designated BCE1, produced by Beltraniella portoricensis, was purified from the culture supernatant. The N-terminal amino acid sequence suggests that BCE1 belongs to family 45 glycoside hydrolase (family 45 endoglucanase). The molecular mass of BCE1 was found to be 40 kDa by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH for the carboxymethyl cellulase (CMCase) activity of BCE1 was 4.5, and the optimum temperature was 55 degrees C. Among family 45 endoglucanases, RCE1 and RCE2 from Rhizopus oryzae, PCE1 from Phycomyces nitens, and EGL3 and EGL4 from Humicola grisea, BCE1 was most resistant to anionic surfactant and oxidizing agent. These results indicate that BCE1 might prove to be a useful enzyme in the detergent industry.[1]

References

  1. Purification and characterization of a new endo-1,4-beta-D-glucanase from Beltraniella portoricensis. Baba, Y., Shimonaka, A., Koga, J., Murashima, K., Kubota, H., Kono, T. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
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