Patent classifications
C12Y204/01001
Preparation of glucan-based shell-core structure carrier material and its application thereof
The present invention discloses a glucan-based shell-core structure carrier material and preparation and application thereof, and belongs to the technical field of modern food processing. Spherical hyperbranched water-soluble amylum grains are used as the raw material, and an enzymatic grafting and chain extending process is adopted for treatment to modify the surfaces of water-soluble glucan molecules into a firm shell structure with densely cumulated crystal structures, and form the glucan-based carrying material with the shell-core structure of which an inner core cavity has an amorphous state and an outer shell layer has a crystalline state. The adopted spherical hyperbranched water-soluble amylum grains have wide sources of raw materials and are not limited by producing areas and seasons; the preparation has simple and convenient steps, easy operation, controllable reaction conditions, relatively low cost and basically no pollution to the environment; and the prepared product can effectively protect, deliver and release functional nutritional components, can be applied to multiple fields of food, medicine, chemicals for daily use and the like, and has great market prospects and broad economic benefits.
NOVEL PSICOSE-6-PHOSPHATE PHOSPHATASE, COMPOSITION FOR PRODUCING PSICOSE INCLUDING SAID ENZYME, METHOD FOR PRODUCING PSICOSE USING SAID ENZYME
The present application relates to a psicose-6-phosphate phosphatase comprising motif A and motif B, a composition for producing D-psicose comprising the enzyme, and a method for producing D-psicose using the enzyme.
RECOMBINANT YEAST HOST CELL EXPRESSING AN HYDROLASE
The present disclosure concerns a recombinant yeast host cell exhibiting higher stability and, in some embodiments, higher fermentation performance. The recombinant yeast host cell stability has a limited ability to express an hydrolase during its propagation phase. In return, this limits the cleavage of a yeast cellular component during or after propagation which may be detrimental to the stability and/or fermentation performances. The recombinant yeast host cell expresses a heterologous hydrolase under the control of a heterologous promoter (for limiting the expression of the heterologous hydrolase during propagation and favoring the expression of the heterologous hydrolase during fermentation).
Enzymatic production of D-allulose
The current disclosure provides a process for enzymatically converting a saccharide into allulose. The invention also relates to a process for preparing allulose where the process involves converting fructose 6-phosphate (F6P) to allulose 6-phosphate (A6P), catalyzed by allulose 6-phosphate 3-epimerase (A6PE), and converting the A6P to allulose, catalyzed by allulose 6-phosphate phosphatase (A6PP).
ADENO-ASSOCIATED VIRUS VARIANT CAPSIDS AND METHODS OF USE THEREOF
Provided herein are variant adeno-associated virus (AAV) capsid proteins having one or more modifications in amino acid sequence relative to a parental AAV capsid protein, which, when present in an AAV virion, confer increased infectivity of one or more types of muscle cells as compared to the infectivity of the muscle cells by an AAV virion comprising the unmodified parental AAV capsid protein. Also provided are recombinant AAV virions and pharmaceutical compositions thereof comprising a variant AAV capsid protein as described herein, methods of making these rAAV capsid proteins and virions, and methods for using these rAAV capsid proteins and virions in research and in clinical practice, for example in, e.g., the delivery of nucleic acid sequences to one or more muscle cells for the treatment of muscle disorders and diseases.
Alpha-glucose-1-phosphate synthesis from sucrose and glucan synthesis using glucan phosphorylases
Reactions are disclosed herein comprising water, alpha-glucose-1-phosphate (alpha-G1P), an acceptor molecule, and an alpha-1,4-glucan phosphorylase. Novel alpha-1,4-glucan phosphorylase enzymes are also disclosed. Additional disclosures herein regard sucrose phosphorylase enzymes and methods of use thereof to produce alpha-G1P.
ENZYMATIC PRODUCTION OF HEXOSES
Disclosed herein are methods of producing hexoses from saccharides by enzymatic processes. The methods utilize fructose 6-phosphate and at least one enzymatic step to convert it to a hexose.
IMMOBILIZED ENZYME COMPOSITIONS FOR THE PRODUCTION OF HEXOSES
The invention relates to immobilized enzyme compositions for the preparation of a hexose. Hexoses include, for example, tagatose, psicose, fructose, allose, mannose, galactose, altrose, talose, sorbose, gulose, idose, and inositol. The invention also relates to an enzymatic process for preparing a hexose from a saccharide by contacting a starch derivative with an immobilized enzyme composition of the invention.
ADENO-ASSOCIATED VIRUS VARIANT CAPSIDS AND METHODS OF USE THEREOF
Provided herein are variant adeno-associated virus (AAV) capsid proteins having one or more modifications in amino acid sequence relative to a parental AAV capsid protein, which, when present in an AAV virion, confer increased infectivity of one or more types of muscle cells as compared to the infectivity of the muscle cells by an AAV virion comprising the unmodified parental AAV capsid protein. Also provided are recombinant AAV virions and pharmaceutical compositions thereof comprising a variant AAV capsid protein as described herein, methods of making these rAAV capsid proteins and virions, and methods for using these rAAV capsid proteins and virions in research and in clinical practice, for example in, e.g., the delivery of nucleic acid sequences to one or more muscle cells for the treatment of muscle disorders and diseases.
ENZYMATIC PRODUCTION OF D-ALLULOSE
The current disclosure provides a process for enzymatically converting a saccharide into allulose. The invention also relates to a process for preparing allulose where the process involves converting fructose 6-phosphate (F6P) to allulose 6-phosphate (A6P), catalyzed by allulose 6-phosphate 3-epimerase (A6PE), and converting the A6P to allulose, catalyzed by allulose 6-phosphate phosphatase (A6PP).