Ecology, Environment and Conservation Paper

EXPRESSION AND RECOMBINANT PROTEIN PURIFICATION OF PHYCOCYANIN α AND β SUBUNITS FROM ARTHROSPIRA PLATENSIS: ANTIMICROBIAL ACTIVITY

Rachanimuk Hiransuchalert, Kanchana Sittikankaew, Patchari Yocawibun, Maliwan Kutako, Chalee Paiboonkichakul, Sirawut Klinbunga and Narongsak Paunglarp

Abstract

Molecular techniques were used to generate the recombinant C-phycocyanin protein of Atrhrospira platensis via an Escherichia coli expression system. The recombinant c-phycocyanin b-subunit (C-PC/α) exhibited a C-PC/β production rate expressed in insoluble form of pET29a (+)/E. coli BL21-DE3-RIPL with 0.16 mg protein/g cellwet (0.81 μg protein/mlmedium). The corresponding rate of the a-subunit (C-PC/a) expressed in insoluble form of pET32a (+)/E. coli BL21-DE3-RIPL was 9.35 mg protein/g cellwet (25.55 μg protein/mlmedium). The recombinant β-α-subunit (C-PC/βα) had a rate expressed in soluble form of pET29a E. coli BL21-DE3 with 11.59 mg protein/g cellwet (24.68 μg protein/mlmedium). Results show that C-PC/β and C-PC/α were inclusion body proteins, while C-PC/βα was soluble in E. coli BL21-DE3. Recombinant proteins did not exhibit blue-green colors, while low sensitivity to E. coli inhibition occurred in the A. platensis C-PC/β protein (1.53 mm ± 0.06 mm of the inhibition zone). Results suggest that recombinant phycocyanin subunits of A. platensis can be reconstructed via the pET expression vector in E. coli. This approach could be used to generate volumes of this protein.