ISSN:
1432-072X
Keywords:
α-Amylase
;
Z. mobilis
;
Secretion
;
Expression
;
Transfer
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The gene from Bacillus licheniformis coding for a thermostable α-amylase was subcloned into the broad-host-range plasmid pKT210 in Escherichia coli. The recombinant plasmid pGNB6 was transferred into Zymomonas mobilis ATCC 31821 by conjugation. Plasmid pGNB6 was stably maintained in E. coli and unstable in Z. mobilis. The amylase gene was expressed in Z. mobilis at a lower level (25%) than in E. coli and regulation of enzyme biosynthesis was different in the host cells. Almost all the α-amylase activity was recovered in the culture medium of Z. mobilis. This enzyme localization seemed to be the result of protein secretion rather than cell lysis. Integration of the amylase gene into a cryptic plasmid of Z. mobilis was observed. The amylase gene was still expressed, although at a lower level, and the α-amylase activity, associated with a protein of molecular mass 62,000 daltons, was immunologically identical in Z. mobilis, E. coli and B. licheniformis.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00249071
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