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Isolation and Characterization of Novel Lactic Acid Bacterium for Efficient Production of L (+) - Lactic Acid from Xylose by M.A. Abdel-Rahman; Y. Tashiro; T. Zendo; K. Sonomoto is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## S347 selected. Using this motif, beta-galactosidase, which is active only in tetrameric form, was functionally displayed on the surface of Bacillus subtilis spore. The surface localization of beta-galactosidase was verified by enzymatic assay of purified spore, protease accessibility test and FACS analysis of spore expressing beta-galactosidase. While Bacillus subtilis spore wall integrity, examined by lysozyme and heat treatments, was slightly affected by the incorporation of CotE-LacZ fusion protein, it was not affected by the incorporation of CotG-lacZ fusion. Other enzymes such as streptavidin, lipase (lipB) of Bacillus subtilis and GFP UV were also successfully displayed using cotE and cotG motifs, and its possible application in various biotechnological fields will be discussed.

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Author

M.A. Abdel-Rahman; Y. Tashiro; T. Zendo; K. Sonomoto

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0168-1656)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)