Microbial sucrose isomerases: Producing organisms, genes and enzymes
► Microbial SIs cluster into 5 structural and functional classes. ► The isomaltulose-producing strain “ Protaminobacter rubrum” CBS 574.77 is Serratia plymuthica. ► The trehalulose-producing strain “ Pseudomonas mesoacidophila” MX-45 is Rhizobium sp. ► Each tested SI-producer has a single SI gene an...
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Veröffentlicht in: | Enzyme and microbial technology 2012-01, Vol.50 (1), p.57-64 |
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Zusammenfassung: | ► Microbial SIs cluster into 5 structural and functional classes. ► The isomaltulose-producing strain “
Protaminobacter rubrum” CBS 574.77 is
Serratia plymuthica. ► The trehalulose-producing strain “
Pseudomonas mesoacidophila” MX-45 is
Rhizobium sp. ► Each tested SI-producer has a single SI gene and enzyme. ► Industrial potential may be enhanced by selection for variants that do not catabolize sucrose.
Sucrose isomerase (SI) activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses. All of the known microbial SIs are TIM barrel proteins that convert sucrose without need for any cofactors, with varying kinetics and product specificities. The current analysis was undertaken to bridge key gaps between the information in patents and scientific publications about the microbes and enzymes useful for sucrose isomer production.
This analysis shows that microbial SIs can be considered in 5 structural classes with corresponding functional distinctions that broadly align with the taxonomic differences between producing organisms. The most widely used bacterial strain for industrial production of isomaltulose, widely referred to as “
Protaminobacter rubrum” CBS 574.77, is identified as
Serratia plymuthica. The strain producing the most structurally divergent SI, with a high product specificity for trehalulose, widely referred to as “
Pseudomonas mesoacidophila” MX-45, is identified as
Rhizobium sp.
Each tested SI-producer is shown to have a single SI gene and enzyme, so the properties reported previously for the isolated proteins can reasonably be associated with the products of the genes subsequently cloned from the same isolates and SI classes. Some natural isolates with potent SI activity do not catabolize the isomer under usual production conditions. The results indicate that their industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate. |
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ISSN: | 0141-0229 1879-0909 |
DOI: | 10.1016/j.enzmictec.2011.09.011 |