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Bioproduction of d-Tagatose from d-Galactose Using Phosphoglucose Isomerase from Pseudomonas aeruginosa PAO1

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Abstract

Pseudomonas aeruginosa PAO1 phosphoglucose isomerase was purified as an active soluble form by a single-step purification using Ni-NTA chromatography that showed homogeneity on SDS-PAGE with molecular mass ∼62 kDa. The optimum temperature and pH for the maximum isomerization activity with d-galactose were 60 °C and 7.0, respectively. Generally, sugar phosphate isomerases show metal-independent activity but PA-PGI exhibited metal-dependent isomerization activity with aldosugars and optimally catalyzed the d-galactose isomerization in the presence of 1.0 mM MnCl2. The apparent Km and Vmax for d-galactose under standardized conditions were calculated to be 1029 mM (±31.30 with S.E.) and 5.95 U/mg (±0.9 with S.E.), respectively. Equilibrium reached after 180 min with production of 567.51 μM d-tagatose from 1000 mM of d-galactose. Though, the bioconversion ratio is low but it can be increased by immobilization and enzyme engineering. Although various l-arabinose isomerases have been characterized for bioproduction of d-tagatose, P. aeruginosa glucose phosphate isomerase is distinguished from the other l-arabinose isomerases by its optimal temperature (60 °C) for d-tagatose production being mesophilic bacteria, making it an alternate choice for bulk production.

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  1. P. D. Patel Institute of Applied Sciences, Charotar University of Science and Technology, Changa, 388 421, Gujarat, India

    Manisha J. Patel, Arti T. Patel, Rekha Akhani, Samir Dedania & Darshan H. Patel

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Patel, M.J., Patel, A.T., Akhani, R. et al. Bioproduction of d-Tagatose from d-Galactose Using Phosphoglucose Isomerase from Pseudomonas aeruginosa PAO1. Appl Biochem Biotechnol 179, 715–727 (2016). https://doi.org/10.1007/s12010-016-2026-7

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