Abstract
Cellulase is a key enzyme for cellulose degradatio n. In order to enhance the efficiency of cellulose degradation, two different cellulase genes were fused and integrated into Lactobacillus genome, and efficiently expressed. Two pairs of primes were designed according to two cellulose genes in GenBank, a peptide containing 10 amid acids was inserted between the two genes. CelL15 and CelL73 were amplified by PCR method, and then fused and cloned into the expression vector pMJ67. The recombinant vector was electrotransferred into Lactobacillus casei. SDS-PAGE analysis showed that the fusion cellulase protein was successfully expressed and secreted into the cell culture supernatant, which was approximately 83 kD. Enzyme activity detection on solid medium indicated that the recombinant Lactobacillus could obviously degrade sodium carboxymethylcellulose in the medium, and the cellulase activity in the supernatant was up to 1.25 U/mL after culture for 36 h.
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