Abstract: The present invention provides a method for producing sesaminol or sesaminol glucosides comprising: reacting a protein with a substrate sesaminol glycoside having at least one glycosidic bond, and catalyzing the hydrolysis of the glycosidic bond; wherein, the protein is selected from the group consisting of the following (1) to (3): (1) a protein composed of the amino acid sequence SEQ ID NO: 1; (2) a protein composed of the amino acid sequence formed by deletion, substitution, insertion and/or addition of one or more amino acids in the amino acid sequence SEQ ID NO:1, wherein the protein has the activity of catalyzing the hydrolysis of the glycosidic bond; (3) a protein composed of an amino acid sequence having an sequence identity of more than 60% compared with the amino acid sequence of SEQ ID NO: 1, wherein the protein has the activity of catalyzing the hydrolysis of the glycosidic bond.

Abstract: The present invention provides an application of genistein and its phosphate ester derivative for treating or preventing diseases mediated by the cannabinoid receptor type 1 (CB1 receptor) in an individual. The present invention also provides a pharmaceutical composition for treating or preventing CB1 receptor-mediated diseases, comprising an effective amount of genistein and its phosphate ester derivative.

Abstract: The present invention provides a coupled enzyme system, comprises: a first enzyme, comprising a polyphenol phosphorylation synthetase; a second enzyme, which is ATP regeneration enzyme; and a substrate, being phosphorylated by the first enzyme. The coupled enzyme system of the present invention integrates polyphenol phosphorylation synthetase with ATP regeneration enzyme so that the polyphenol phosphorylation synthetase is used to phosphorylate polyphenol and the ATP regeneration enzyme regenerate ATP from AMP. Therefore, the present invention not only improves the water-solubility and bioavailability of the phenolic phytochemicals but also significantly reduces ATP consumption, presenting the potential of enzymatic systems in the production of polyphenol monophosphates.

Abstract: An isolated or engineered polypeptide, a microorganism comprising a nucleic acid sequence encoded by the polypeptide, and a method for synthesizing a polyphenolic phytochemicals phosphate derivative using the polypeptide or the microorganism are provided. The polypeptide having a homologous protein sequence that is more than 70% identical to the polyphenol phosphorylation synthetase (SEQ ID NO: 13) comprises a conserved domain which sequentially comprises: an ATP-binding domain, which includes active catalytic sites of Lys27, Arg102, and Glu282; a substrate-binding domain, which includes a conserved motif of DDHHFYIDAMLDAKAR (SEQ ID NO: 14), and includes active catalytic sites ofAsp627, His629, and His630; and a phosphorylated histidine catalytic domain, which includes His795 based on SEQ ID NO: 13.

Abstract: The present invention provides a method for treatment or prevention of a disease associated with a decrease in bone mass comprising administering to a subject in need of such treatment a composition comprising an effective amount of genistein phosphate conjugate. The present invention also provides a method of improving bone architecture and bio-mechanical strength of bone comprising administering to a subject in need of such treatment of a composition comprising an effective amount of genistein phosphate conjugate. The present invention administering to a subject in need of such treatment a composition comprising an effective amount of genistein phosphate conjugate can effectively increase the oral bioavailability so as to reduce the symptoms and the risk of complications of menopausal women, increase bone mineral content, bone density and bio-mechanical strength of bone, and slow down osteoporosis.

Abstract: The present invention is related to a biotransformation process, effected by means of an isolated polypeptide possessing benzopyrone phosphate synthetase activity, and also a microorganism comprising a nucleic acid sequence that encodes the polypeptide, for the preparation of phosphate-conjugated derivatives of benzopyrone compounds. The hydrophilic property of the benzopyrone compounds is enhanced after catalyzed by the benzopyrone phosphate synthetase of the present invention.

Abstract: The present invention provides a method for treatment or prevention of a disease associated with a decrease in bone mass comprising administering to a subject in need of such treatment a composition comprising an effective amount of genistein phosphate conjugate. The present invention also provides a method of improving bone architecture and bio-mechanical strength of bone comprising administering to a subject in need of such treatment of a composition comprising an effective amount of genistein phosphate conjugate. The present invention administering to a subject in need of such treatment a composition comprising an effective amount of genistein phosphate conjugate can effectively increase the oral bioavailability so as to reduce the symptoms and the risk of complications of menopausal women, increase bone mineral content, bone density and bio-mechanical strength of bone, and slow down osteoporosis.

Abstract: The present invention is related to a biotransformation process, effected by means of an isolated polypeptide possessing benzopyrone phosphate synthetase activity, and also a microorganism comprising a nucleic acid sequence that encodes the polypeptide, for the preparation of phosphate-conjugated derivatives of benzopyrone compounds. The hydrophilic property of the benzopyrone compounds is enhanced after catalyzed by the benzopyrone phosphate synthetase of the present invention.

Abstract: The present invention discloses a lectin, which is isolated from a plant belonging to the family Caricaceae. The lectin of the present invention includes a first subunit having a molecular weight of 38 kDa and a second subunit having a molecular weight of 40 kDa, wherein the lectin has a molecular weight in a range from 750 to 850 kDa and has a binding specificity to N-acetylgalactosamine and lactose.