The present invention provides solid forms of compounds useful as inhibitors of Acetyl CoA Carboxylase (ACC), compositions thereof, methods of producing the same, and methods of using the same in the treatment of ACC-mediated diseases.

Provided is a humanized monoclonal antibody or an antibody fragment thereof that selectively inhibits the enzymatic activity of vascular endothelial lipase and pharmaceutical compositions containing the same as an active ingredient useful for the treatment of arteriosclerosis or metabolic syndrome.

The disclosure relates to a series of independent human-induced non-transgenic mutations found at one or more of the Lip1 genes of a plant; plants having these mutations in one or more of their Lip1 genes; and a method of creating and finding similar and/or additional mutations of Lip1 by screening pooled and/or individual plants. The plants disclosed herein exhibit decreased lipase activity without having the inclusion of foreign nucleic acids in their genomes. Additionally, products produced from the plants disclosed herein exhibit increased hydrolytic and oxidative stability and increased shelf life without having the inclusion of foreign nucleic acids in their genomes.

The present disclosure provides antisense oligonucleotides, compositions, and methods that target a LIPA intron flanking exon 8, thereby modulating splicing of LIPA pre-mRNA to increase the level of LIPA mRNA molecules having exon 8, e.g., to provide a therapy for Wolman Disease or Cholesteryl Ester Storage Disease. The present disclosure provides an antisense oligonucleotide including a nucleobase sequence at least 70% complementary to a LIPA pre-mRNA target sequence in a 5′-flanking intron, a 3′-flanking intron, or a combination of exon 8 and the 5′-flanking or 3′-flanking intron.

An enzymatic deacidification method for partial glyceride lipase and PUFA-rich oil, comprising the following steps: 1) mixing a polyunsaturated fatty acid (PUFA)-rich oil with a non-polar organic solvent and a short-chain monohydric alcohol, adding an immobilized partial glyceride lipase to carry out an esterification reaction, wherein the partial glyceride lipase is a mutant obtained by mutating the Phe at the 278th position of Lipase SMG1 as Asn; 2) recovering the immobilized enzyme, and recovering the organic solvent and the monohydric alcohol so as to obtain a deacidified PUFA-rich oil. The partial glyceride lipase does not catalyze alcoholysis of triglyceride and like side reactions, has high deacidification efficiency, low reaction temperature, prevents high temperature oxidation of PUFAs, and the immobilized enzyme may be recovered and reused repeatedly, and thus the present invention has good application prospects in industry.

Described herein is an enzyme preparation including component (a): at least one compound according to general formula (I)

##STR00001## wherein R.sup.1 is H; R.sup.2, R.sup.3, R.sup.4 are independently from each other selected from the group consisting of H, linear C.sub.1-C.sub.8 alkyl, and branched C.sub.3-C.sub.8 alkyl, C.sub.6-C.sub.10-aryl, non-substituted or substituted with one or more carboxylate or hydroxyl groups, and C.sub.6-C.sub.10-aryl-alkyl, wherein an alkyl of the C.sub.6-C.sub.10-aryl-alkyl is selected from the group consisting of linear C.sub.1-C.sub.8 alkyl and branched C.sub.3-C.sub.8 alkyl, wherein at least one of R.sup.2, R.sup.3, and R.sup.4 is not H; component (b): at least one enzyme selected from the group consisting of hydrolases (EC 3); and optionally component (c): at least one compound selected from the group consisting of solvents, enzyme stabilizers different from component (a), and compounds stabilizing the enzyme preparation.

A structurally-modified recombinant protein, obtained by a method comprising generating at least one genetic construct comprising a nucleotide sequence coding for the protein comprising a recognition sequence; expressing in a host the at least one genetic construct using a vector comprising the at least one genetic construct; and using a plant-based expression system with the vector to express the protein, the plant-based expression system being a plant or a plant cells suspension; the recognition sequence comprises a sequence Phe-x1-x2-Tyr, wherein Phe is phenylalanine, x1 and x2 are amino acid residues, and Tyr is tyrosine and the plant-based expression system has an inherent enzymatic activity which converts the phenylalanine residue of the recognition sequence into a didehydrophenylalanine residue, producing a structurally-modified recombinant protein; and isolating the protein with the recognition sequence which is a part of the protein, the phenylalanine being converted to a didehydrophenylalanine from the plant-based expression system.

The present disclosure relates to methods and systems for refining grain oil compositions using an esterase enzyme component, water, bleaching processes, and combinations thereof, and related compositions produced therefrom having one or more reduced color values. The present disclosure also relates to methods of using said compositions, e.g., as mineral oil replacements.

The invention relates to a method for generating a preparation of lipase with increased lipolytic activity comprising a step of altering one or more nucleotides in a polynucleotide comprising a first polynucleotide encoding a propeptide operationally linked to a second polynucleotide encoding a lipase, wherein the alteration of one or more nucleotides are made in the first polynucleotide and the alteration independently results in a substitution, an insertion or a deletion in the encoded propeptide amino acid sequence.

The present invention provides an enzymatic method for producing a fatty acid bornyl ester including using borneol and a fatty acid as a substrate for reaction and adding a lipase in a solvent system or a solvent-free system to catalyze the esterification reaction for a period of time to obtain fatty acid bornyl ester. The present method preferably uses fatty acids or their derivatives as acyl donors to prepare fatty acid bornyl esters. By utilizing the characteristics of the substrate, the synthesis process is simple; the reaction efficiency is high; and the content of fatty acid bornyl ester is up to 97%.