C12P19/44

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.

METHOD FOR THE BIOSYNTHESIS OF DIOSMIN AND/OR HESPERIDIN IN A MICROORGANISM

The present invention relates to a recombinant microorganism which is modified to be capable of producing diosmin and hesperidin and to the use thereof for producing diosmin and/or hesperidin.

ENHANCED PRODUCTION OF RHAMNOLIPIDS USING AT LEAST TWO CARBON SOURCES
20210403969 · 2021-12-30 ·

Provided is a method for improving the yield of rhamnolipids comprising culturing in medium containing a triglyceride containing oil and sweetener as a carbon source.

ENHANCED PRODUCTION OF RHAMNOLIPIDS USING AT LEAST TWO CARBON SOURCES
20210403969 · 2021-12-30 ·

Provided is a method for improving the yield of rhamnolipids comprising culturing in medium containing a triglyceride containing oil and sweetener as a carbon source.

Recombinant Production of Steviol Glycosides

Recombiant microorganisms, plants, and plant cells are disclosed that have been engineered to express recombinant genes encoding UDP-glycosyltransferases (UGTs). Such microorgansims, plants, or plant cells can produce steviol glycosides, e.g., Rebaudioside A and/or Rebaudioside D, which can be used as natural sweeteners in food products and dietary supplements.

Recombinant Production of Steviol Glycosides

Recombiant microorganisms, plants, and plant cells are disclosed that have been engineered to express recombinant genes encoding UDP-glycosyltransferases (UGTs). Such microorgansims, plants, or plant cells can produce steviol glycosides, e.g., Rebaudioside A and/or Rebaudioside D, which can be used as natural sweeteners in food products and dietary supplements.

RECOMBINANT MICROBIAL SYSTEM FOR DIRECTED EVOLUTION OF GLYCOCINS AND METHOD OF PREPARATION THEREOF
20210395728 · 2021-12-23 ·

The present invention relates to a recombinant microbial system for generation of neo-glycocins, a substrate and to co-evolve its glycosyltransferase enzyme. The recombinant microbial system comprises a gene cassette A encoding for microbial O- and S-glycosyltransferase and its suitable acceptor substrate in conjugation with a cleavable dual affinity tag under the control of two independent inducible promoters. The gene cassette is expressed in a microbial host such as E. coli for the co-expression of glycosyltransferase and its suitable acceptor substrate. The invention further discloses method for production and bioactivity guided screening of O- and or S-neo-glycocins using the recombinant microbial system. The system provides optimized construct design, and methods for high yield production of glycocins and neo-glycocins for downstream applications.

RECOMBINANT MICROBIAL SYSTEM FOR DIRECTED EVOLUTION OF GLYCOCINS AND METHOD OF PREPARATION THEREOF
20210395728 · 2021-12-23 ·

The present invention relates to a recombinant microbial system for generation of neo-glycocins, a substrate and to co-evolve its glycosyltransferase enzyme. The recombinant microbial system comprises a gene cassette A encoding for microbial O- and S-glycosyltransferase and its suitable acceptor substrate in conjugation with a cleavable dual affinity tag under the control of two independent inducible promoters. The gene cassette is expressed in a microbial host such as E. coli for the co-expression of glycosyltransferase and its suitable acceptor substrate. The invention further discloses method for production and bioactivity guided screening of O- and or S-neo-glycocins using the recombinant microbial system. The system provides optimized construct design, and methods for high yield production of glycocins and neo-glycocins for downstream applications.

Sucrose phosphorylase mutant with improved enzyme activity and construction method thereof and use thereof

The disclosure relates to a sucrose phosphorylase mutant with improved enzyme activity, and construction method thereof and use thereof, and belongs to the technical field of genetic engineering. The amino acid sequence of the mutant of the disclosure is as shown in SEQ ID NO: 1. The mutant of the disclosure is based on sucrose phosphorylase derived from Leuconostoc mesenteroides, and subjected to site-directed mutagenesis to improve the enzyme activity of sucrose phosphorylase. The mutant is expressed in Corynebacterium glutamicum and used as a whole cell catalyst to produce 2-O-α-D-glycerol glucoside. At a 5 L fermentation tank level, a large quantity of 2-O-α-D-glycerol glucoside can be produced efficiently in a short time, which is conducive to expanding the prospect of industrial application of sucrose phosphorylase for the production of 2-O-α-D-glycerol glucoside and realizing its large-scale industrial application.

IMMUNOTHERAPEUTIC POTENTIAL OF MODIFIED LIPOOLIGOSACCHARIDES/LIPID A
20210381015 · 2021-12-09 ·

Embodiments of the disclosure provide for unique lipooligosaccharide/lipid A-based mimetics for use as adjuvants. Methods of generating lipooligosaccharide/lipid A-based mimetics are provided that utilize recombinantly engineered bacteria to produce the mimetics, including, for example, addition of one or more particular enzymes such as acyltransferases, deacylases, phosphatases, or glycosyltransferases.