Abstract
In an attempt to mine cyanobacterial genes of potential biotechnological applications, the hypothetical protein All4894 of Anabaena PCC7120, following cloning, heterologous expression, purification and biochemical analysis, revealed the presence of a thermostable β-glucosidase. The glycosylated protein showed apparent molecular mass of ~18.0 kDa, while the purified enzyme depicted activity over wide pH (2.0–9.0) range and 85% stability up to 100 °C. All4894 encoding fascilin-1 domain showed higher specific activity to natural substrate cellobiose (Km = 0.75 mM and Vmax = 0.416 mMmin−1 mg−1) as compared to p-nitrophenyl-β-D-glucopyranoside. Quantitative reverse transcription polymerase chain reaction analysis (qRT-PCR) of all4894 revealed 4.0 to 16.0 fold elevated transcript under salinity, heat, arsenic, cadmium, UV-B and butachlor. The ectopic expression of All4894 in E. coli BL21 (DE3) reaffirmed its stress management capability. In view of the multiple functional attributes i.e. cell adhesion and abiotic stress tolerance All4894 may be regarded as “moonlighting protein” having a novel biomolecule for biotechnological applications including bioethanol production.
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