Phosphate sugar isomerases and their potential for rare sugar bioconversion
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MINIREVIEW Phosphate sugar isomerases and their potential for rare sugar bioconversion Soo-Jung Kim1, Yeong-Su Kim2*, and Soo-Jin Yeom3* 1 Department of Integrative Food, Bioscience and Biotechnology, Chonnam National University, Gwangju 61186, Republic of Korea 2 Wild Plants Industrialization Research Division, Baekdudaegan National Arboretum, Bonghwa 36209, Republic of Korea 3 School of Biological Sciences and Technology, Chonnam National University, Gwangju 61186, Republic of Korea
(Received Apr 29, 2020 / Revised May 26, 2020 / Accepted May 27, 2020)
Phosphate sugar isomerases, catalyzing the isomerization between ketopentose/ketohexose phosphate and aldopentose/ aldohexose phosphate, play an important role in microbial sugar metabolism. They are present in a wide range of microorganisms. They have attracted increasing research interest because of their broad substrate specificity and great potential in the enzymatic production of various rare sugars. Here, the enzymatic properties of various phosphate sugar isomerases are reviewed in terms of their substrate specificities and their applications in the production of valuable rare sugars because of their functions such as low-calorie sweeteners, bulking agents, and pharmaceutical precursor. Specifically, we focused on the industrial applications of D-ribose-5-phosphate isomerase and D-mannose-6-phosphate isomerase to produce D-allose and L-ribose, respectively. Keywords: biocatalyst, phosphate sugar isomerase, rare sugar, substrate specificity, bioconversion Introduction Rare sugars have recently attracted attention owing to their potential applications in the food, pharmaceutical, and nutritional industries, such as low-calorie sweeteners and bulking agents (Levin et al., 1995; Livesey and Brown, 1996; Levin, 2002; Matsuo et al., 2002; Matsuo and Izumori, 2004; Beerens et al., 2012), immunosuppressants in allogenic orthotopic liver transplantation (Hossain et al., 2000), and potential inhibitors of various glycosidases (Muniruzzaman et al., 1996), ischemia/reperfusion injury of liver (Hossain et al., *For correspondence. (Y. S. Kim) E-mail: [email protected]; Tel.: +82-54679-2740; Fax: +82-54-679-0636 / (S. J. Yeom) E-mail: [email protected]. kr; Tel.: +82-62-530-1911; Fax: +82-62-530-2199 Copyright G2020, The Microbiological Society of Korea
2004), and segmented neutrophil production without other detrimental clinical effects (Murata et al., 2003). Rare sugars have been generally produced by chemical synthesis; however, this method has numerous disadvantages, such as harsh reaction conditions (e.g., alkaline), multi-reaction steps, formation of chemical waste, complex purification steps, and by-product formation (Yoon et al., 2009a). As an alternative, biocatalysts including ketose epimerases, aldose isomerases, aldose reductases, and oxido-reductases, have been used to overcome these disadvantages of chemical production. Among these enzymes, isomerases have been used mainly to produce rare sugars through the interconversion
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