(by novalidaddress from nurfuerspam.de)
Wed May 5 07:50:02 EST 2010
I would expect some residual activity. Isn't there any information in
the papers of the people who isolated and characterized this nice
On 5 Mai, 11:37, gholamreza ahmadian <gholamrezaahmad... from yahoo.ca>
> Dear All
> I would like to ask a question and I appreciate your any help:
> I am trying to express a betagalactosidase (bgaB) from Geobacillus stearothermophilus in E.coli. bgaB is a thermostable betagalactosidase originally isolated from Geobacillus stearothermophilus. ATCC 7954 , glycosyl hydrolase 42 family. The enzyme catalyses the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.
> It has 3 subunit from N-terminal as : 1- glycosyl hydrolase 42 family domain, -2-non catalytic domain necessary for trimerization and -3- a domain usually found at the C-terminus of beta-galactosidases.
> I would like to know if cloning just domain 1 (glycosyl hydrolase 42 family domain) is functional or other domain like trimerization domain is also necessary for functional expression of enzyme.
> Best Regards
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