High-level production of hyperthermophilic cellulase in the Bacillus brevis expression and secretion system.
A hyperthermophilic cellulase derived from Pyrococcus horikoshii was successfully produced with the Bacillus brevis host-vector system. The production of the recombinant enzyme was increased about 20-fold (to a level of 100 mg per liter) by the insertion of certain amino acid such as alanine and peptides like AEEAADP between the carboxyl end of signal peptide and the N-terminus of the mature cellulase. These recombinant cellulases had the same characteristics as that of the cellulase expressed in Escherichia coli.
Kashima
Yasuhiro
Y
Special Division for Human Life Technology, National Institute of Advanced Industrial Science and Technology (AIST Kansai), Osaka, Japan.
Udaka
Shigezo
S
D000409:Alanine / Q000235:genetics; D001407:Bacillus / Q000201:enzymology / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002480:Cellulase / Q000235:genetics* / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D005786:Gene Expression Regulation; D010455:Peptides / Q000235:genetics; D010957:Plasmids / Q000235:genetics; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D010455:Peptides; D011994:Recombinant Proteins; D002480:Cellulase; D000409:Alanine