Patent classifications
C12P19/44
Processing biomass
Biomass (e.g., plant biomass, animal biomass, microbial, and municipal waste biomass) is processed to produce useful products, such as food products and amino acids.
IMPROVED PRODUCTION OF SYMMETRICAL BOLAFORM SOPHOROSIDES
The present invention relates to the field of microbial production of novel biosurfactants. More specifically, the present invention discloses the usage of a fungal strain such as the yeast Starmerellabombicola having a dysfunctional CYP52M1 cytochrome P450 monooxygenase and a dysfunctional FAO1 fatty alcohol oxidase for producing high amounts of so-called “symmetrical bolaform sophorosides” where both sophorose moieties are attached through a terminal glycosidic linkage to the hydrophobic linker. In addition, the present invention further discloses that the latter yeast can also be used to produce alkyl sophorosides and symmetrical bolaform glucosides.
IMPROVED PRODUCTION OF SYMMETRICAL BOLAFORM SOPHOROSIDES
The present invention relates to the field of microbial production of novel biosurfactants. More specifically, the present invention discloses the usage of a fungal strain such as the yeast Starmerellabombicola having a dysfunctional CYP52M1 cytochrome P450 monooxygenase and a dysfunctional FAO1 fatty alcohol oxidase for producing high amounts of so-called “symmetrical bolaform sophorosides” where both sophorose moieties are attached through a terminal glycosidic linkage to the hydrophobic linker. In addition, the present invention further discloses that the latter yeast can also be used to produce alkyl sophorosides and symmetrical bolaform glucosides.
PROCESS FOR THE PREPARATION OF HALO-SUBSTITUTED TRIFLUOROACETOPHENONES
The invention relates to a process for the preparation of a compound of formula I (I), wherein R.sub.1 is hydrogen, fluoro or chloro; which process comprises a) reacting a compound of formula II (II), wherein R.sub.1 is hydrogen, fluoro or chloro; with a nitration agent to the compound of formula (III), wherein R.sub.1 is hydrogen, fluoro or chloro; and b) reacting the compound of formula III with chlorine gas at temperature from 180° C. to 250° C. to the compound of formula I.
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PROCESS FOR THE PREPARATION OF HALO-SUBSTITUTED TRIFLUOROACETOPHENONES
The invention relates to a process for the preparation of a compound of formula I (I), wherein R.sub.1 is hydrogen, fluoro or chloro; which process comprises a) reacting a compound of formula II (II), wherein R.sub.1 is hydrogen, fluoro or chloro; with a nitration agent to the compound of formula (III), wherein R.sub.1 is hydrogen, fluoro or chloro; and b) reacting the compound of formula III with chlorine gas at temperature from 180° C. to 250° C. to the compound of formula I.
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Production of Steviol Glycosides in Recombiant Hosts
The invention relates to recombinant microorganisms and methods for producing steviol glycosides and steviol glycoside precursors.
Production of Steviol Glycosides in Recombiant Hosts
The invention relates to recombinant microorganisms and methods for producing steviol glycosides and steviol glycoside precursors.
Glycoconjugate synthesis
The invention relates to a method for producing a glycoconjugate comprising an oligosaccharide part covalently linked to a non-sugar moiety selected from the group consisting of amino acids, peptides, proteins, lipids, longer alkyl groups, polyethylene glycols, α,β-unsaturated amido group and polyvinyl alcohols, using a genetically modified cell.
Glycoconjugate synthesis
The invention relates to a method for producing a glycoconjugate comprising an oligosaccharide part covalently linked to a non-sugar moiety selected from the group consisting of amino acids, peptides, proteins, lipids, longer alkyl groups, polyethylene glycols, α,β-unsaturated amido group and polyvinyl alcohols, using a genetically modified cell.
Quantitative control of sialylation
The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations were found to exhibit sialidase enzymatic activity, particularly a variant of human sialyltransferase (hST6Gal-I) with a truncation deletion involving the first 89 N-terminal amino acids of the respective wild-type polypeptide. A fundamental finding documented in the present disclosure is that there exists a variant of this enzyme which is capable of catalyzing transfer of a glycosyl moiety as well as hydrolysis thereof. Thus, disclosed is a specific exemplary variant of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variant of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.