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Comprehensive Summary: The biochemical property and functional identification of three recombinant glycosyltransferases, including β‐1,4‐rhamnosyltransferase (Cps8R), β‐1,4‐galactosyltransferase (Cps8J) and α‐2,3‐sialyltransferase (Cps8K) involved in the biosynthesis of the tetrasaccharide repeating unit of serotype VIII capsular polysaccharide (CPS) of Group B Streptococci (GBS), were systematically investigated. Subsequently, these recombinant enzymes were employed for one‐pot three‐enzyme efficient synthesis of the tetrasaccharide repeating unit of GBS serotype VIII CPS using the chemically synthesized Glcα‐PP‐(CH2)11‐OPh as the starting substrate in a satisfying yield of 87%. [ABSTRACT FROM AUTHOR]

The enzymatic activity and function of a new α‐1,3‐glucosyltransferase, Cps18CU, derived from Streptococcus pneumoniae serotype 18C was identified for the first time using the enzymatically synthetic disaccharide Rhaβ1,4‐Glcα‐PP‐O(CH2)11‐OPh as the acceptor substrate. Further investigation on substrate specificity revealed that Cps18CU exhibited broad toleration toward various NDP‐Glc donors and also accepted such disaccharide acceptor containing Rhaβ1,4‐Glc moiety in structure. Finally, Cps18CU was employed into a one‐pot two‐enzyme reaction system, furnishing trisaccharide Glcα1,3‐Rhaβ1,4‐Glcα‐PP‐O(CH2)11‐OPh in an 81 % yield. [ABSTRACT FROM AUTHOR]