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- W2379319733 abstract "The recombinant protein composed of human β defensin 3 and des-pGlu -brazzein (hBD3-Bra) expressed heterologously by the engineered strain Escherichia coli BL21 - pET-hBD3-Bra was purified and its activity was analyzed, as well as its lactose inductive conditions were optimized. The purified hBD3 - Bra showed weak antimicrobial activity and tasted little sweet. After cleaved by thrombin, the released recombinant hBD3 had high antimicrobial activity and the des-pGlu1-Brazzein was 600 times sweeter than sucrose. The influences of three factors, lactose concentration, inductive time and inductive temperature, on strain growth and yield of hBD3-Bra were analyzed. The results indicated that the strain growth was inhibited by higher lactose concentration (P 0.01), however, the interested protein expression was not affected by 0.5%～5.0% of lactose (P 0.05). Biomass was improved along with time increase(P 0.01), while the interested protein yield did not increase obviously (P 0.05). Both strain growth and interested protein expression were influenced by temperature (P 0.01), the optimal temperature for strain growth was 30 ～32℃ and for interested protein expression 30 ℃. As an inducer, Lactose was as good as IPTG (P 0.05)." @default.
- W2379319733 created "2016-06-24" @default.
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- W2379319733 date "2008-01-01" @default.
- W2379319733 modified "2023-09-25" @default.
- W2379319733 title "Purification and Activity Analysis of a Fusion Protein of Human β Defensin 3 and Plant des-pGlu1-Brazzein and Optimization of Lactose Inductive Conditions" @default.
- W2379319733 hasPublicationYear "2008" @default.
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