Abstract: Pseudomonas chlororaphis NRRL B-30761 produces monorhamnolipids with predominantly 3-hydroxydodecenoyl-3-hydroxydecanoate (C12:1-C10) or 3-hydroxydodecanoyl-3-hydroxydecanoate (C12-C10) as the lipid moiety under static growth conditions. The cloning and sequencing of three genes and proteins involved in the biosynthesis of monorhamnose-lipid (R1L) is described. Expression of two of these genes, i.e., rhlA and rhlB, together in P. chlororaphis NRRL B-30761 increases R1L production by at least 10-fold. Also the generation of a recombinant P. chlororaphis NRRL B-30761 capable of synthesizing dirhamnose-lipid (R2L) is described. Characterization of R1L and R2L produced by the recombinant P. chlororaphis NRRL B-30761 is also described.

Abstract: The isolation and characterization of a glucosyltransferase gene from Candida bombicola is disclosed. Use of the glucosyltransferase enzyme for the production of glucosylated sterol and hydroxyl-fatty acid substrates is also disclosed. This enzyme has broad-specificity and is useful for the production of sophorolipids both in-vivo and in-vitro.

Abstract: Pseudomonas chlororaphis NRRL B-30761 produces monorhamnolipids with predominantly 3-hydroxydodecenoyl-3-hydroxydecanoate (C12:1-C10) or 3-hydroxydodecanoyl-3-hydroxydecanoate (C12-C10) as the lipid moiety under static growth conditions. The cloning and sequencing of three genes and proteins involved in the biosynthesis of monorhamnose-lipid (R1L) is described. Expression of two of these genes, i.e., rhlA and rhlB, together in P. chlororaphis NRRL B-30761 increases R1L production by at least 10-fold. Also the generation of a recombinant P. chlororaphis NRRL B-30761 capable of synthesizing dirhamnose-lipid (R2L) is described. Characterization of R1L and R2L produced by the recombinant P. chlororaphis NRRL B-30761 is also described.

Abstract: The isolation and characterization of a glucosyltransferase gene from Candida bombicola is disclosed. Use of the glucosyltransferase enzyme for the production of glucosylated sterol and hydroxyl-fatty acid substrates is also disclosed. This enzyme has broad-specificity and is useful for the production of sophorolipids both in-vivo and in-vitro.

Abstract: A sophorolid produced by a method involving reacting a compound of formula I with a compound of formula II wherein R1 and R2 are H, C1-C18 alkyl, C3-C18 alkenyl, C3-C10 cycloalkyl, phenyl, or C1 through C18 acyl or alkoxycarbonyl, R1 and R2 are not both acyl, R3 is H, CH3, CH2-phenyl, CH2—C6H4—OH, CH2CO2H, CH2CH2CO2H, CH(CH3)2, CH2CH(CH3)2, CH(CH3)CH2CH3, CH2OH, CH(CH3)OH, CH2CH2CH2CH2NH2, CH2CH2CONH2, CH2CONH2, CH2—C3N2H3(histidine), CH2CH2CH2NHC(NH)NH2, CH2CH2SCH3, R2 and R3 may be joined in a ring, R4 is H, C1-C18 alkyl, C3-C18 alkenyl, C3-C10 cycloalkyl, or phenyl, n is 0-6, R5 and R6 are H, C1-C18 alkyl, C3-C18 alkenyl, C3-C10 cycloalkyl, or phenyl, and X is C1-C18 alkyl or C1-C18 alkenyl; optionally followed by acidolytic (treating with an acid) or hydrogenolytic deprotection (treating with a hydrogenolysis catalyst) which removes one of the groups R1 or R2 and replaces it with hydrogen.

Abstract: A sophorolid produced by a method involving reacting a compound of formula I with a compound of formula II wherein R1 and R2 are H, C1-C18 alkyl, C3-C18 alkenyl, C3-C10 cycloalkyl, phenyl, or C1 through C18 acyl or alkoxycarbonyl, R1 and R2 are not both acyl, R3 is H, CH3, CH2-phenyl, CH2—C6H4—OH, CH2CO2H, CH2CH2CO2H, CH(CH3)2, CH2CH(CH3)2, CH(CH3)CH2CH3, CH2OH, CH(CH3)OH, CH2CH2CH2CH2NH2, CH2CH2CONH2, CH2CONH2, CH2—C3N2H3(histidine), CH2CH2CH2NHC(NH)NH2, CH2CH2SCH3, R2 and R3 may be joined in a ring, R4 is H, C1-C18 alkyl, C3-C18 alkenyl, C3-C10 cycloalkyl, or phenyl, n is 0-6, R5 and R6 are H, C1-C18 alkyl, C3-C18 alkenyl, C3-C10 cycloalkyl, or phenyl, and X is C1-C18 alkyl or C1-C18 alkenyl; optionally followed by acidolytic (treating with an acid) or hydrogenolytic deprotection (treating with a hydrogenolysis catalyst) which removes one of the groups R1 or R2 and replaces it with hydrogen.