αa-D-Galactosidases from Thermotoga species
2001
Publisher Summary Based on similarities in primary structure and hydrophobic cluster analyses, αGals have been grouped into three well-conserved families in the general classification of glycosylhydrolases Those from bacteria have been grouped into families 4 and 36 and those of eukaryotic origin into family 27. To date, only α Gals of the hyperthermophilic bacteria Thermotoga maritima ( Tm GalA) and T. neapolitana ( Tn GalA) have demonstrated activity and prolonged stability above 75°. These two enzymes are therefore of considerable interest from a biotechnological standpoint. Potential applications include the high temperature hydrolysis of galactomannans used for well stimulation in the oil and gas industry and oligosaccharide synthesis via glycosyltransferase reactions. Genes encoding both Tm GalA and Tn GalA have been cloned and expressed in Escherichia coli . Although these enzymes are structurally related, they exhibit different biochemical properties in terms of pH optima, activity, and thermostability. This chapter discusses the purification, cloning, and expression of recombinant α Gal from T. neapolitana and T. maritima , in addition to some of their biochemical properties.
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