Abstract
Abstract Cyanophycin granule polypeptide (CGP), a polymer of aspartic acid and arginine, synthesized by cyanophycin synthetase can be converted to polyaspartate which has many industrial applications. Cyanophycin and cyanophycin synthetase from a thermophilic cyanobacterium Chlorogloeopsis fritschii have been studied expecting enzyme from this organism to be thermostable. The organism exhibited best growth in Chu-10 medium at 45 °C. Maximum amount of cyanophycin was observed on 21 d when organism entered into stationary phase. Optimum conditions for cyanophycin synthetase were 30–40 °C and pH 8.0–9.5. The enzyme showed high specificity to aspartic acid and arginine but synthesized polyaspartate when arginine was omitted from the assay mixture. The enzyme activity doubled when Zn2+ were used as cofactor in place of Mg2+. The enzyme exhibited good thermal stability as it showed 66% activity when treated with 45 °C for one hour. Since cyanophycin synthetase formed an industrially valuable molecule polyaspartic acid and showed thermal stability, it has potential applications which needs to be further investigated.
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