A method for quantifying cardiolipin in a sample, comprises the steps of: (1) treating the sample with phospholipase D, glycerol kinase, glycerol-3-phosphate oxidase, and peroxidase and (2) measuring the fluorescence intensity, absorbance, or luminescence intensity of a compound generated in step (1) to quantify cardiolipin using a calibration curve obtained beforehand; and a kit for quantifying cardiolipin comprises phospholipase D, glycerol kinase, glycerol-3-phosphate oxidase, and peroxidase.

Disclosed are methods of making a modified lecithin by conducting an enzymatic conversion of a naturally derived lecithin to form a modified lecithin, e.g., having an enhanced level of phosphatidylethanolamine, phosphatidylserine, or a combination thereof. Compositions prepared from the modified lecithin and use to inhibit lipid oxidation are described.

The present disclosure relates to methods, cells, and compositions for producing a product of interest, e.g., a recombinant protein. In particular, the present disclosure provides improved mammalian cells expressing the product of interest, where the cells (e.g., Chinese Hamster Ovary (CHO) cells) have reduced or eliminated activity, e.g., expression, of certain host cell proteins, e.g., enzymes including, but not limited to, certain lipases, esterases, and/or hydrolases.

Engineered phospholipase D mutants are described herein. Also described herein are methods of making engineered phospholipase D mutants. Additionally, methods of using engineered phospholipase D mutants are described.

A method of detecting carboxyalkylpyrrole ethanolamine phospholipids (CAP-EPs) or pentylpyrrole ethanolamine phospholipids (CAP-EPs) in a bodily sample from a subject includes obtaining a bodily sample from a subject suspected of including carboxyalkylpyrrole ethanolamine phospholipids (CAP-EPs) or pentylpyrrole ethanolamine phospholipids (PP-EPs) extracting carboxyalkylpyrrole ethanolamine phospholipids or pentylpyrrole ethanolamine phospholipids from the bodily sample; hydrolyzing carboxyalkylpyrrole or pentylpyrrole ethanolamine phospholipids from the extracted with a phospholipase D to form carboxyalkylpyrrole ethanolamine (CAP-ETN) and pentylpyrrole ethanolamine (PP-ETN) derivatives; and determining the amount of carboxyalkylpyrrole ethanolamine (CAP-ETN) and pentylpyrrole ethanolamine (PP-ETN) by mass spectrometry.

The invention relates to a composition comprising at least one phospholipid-cleaving enzyme. The invention further relates to a method for degumming raw oils using the composition according to the invention and to the use of the composition according to the invention to degum raw oils.

The inventions disclosed herein are a method for quantifying cardiolipin in a sample, comprising the steps of: (1) treating the sample with phospholipase D, glycerol kinase, glycerol-3-phosphate oxidase, and peroxidase and (2) measuring the fluorescence intensity, absorbance, or luminescence intensity of a compound generated in step (1) to quantify cardiolipin using a calibration curve obtained beforehand; and a kit for quantifying cardiolipin comprising phospholipase D, glycerol kinase, glycerol-3-phosphate oxidase, and peroxidase.

The present invention relates to a composition comprising at least one phospholipid-splitting enzyme and at least one protease. The invention further relates to a method for degumming triglyceride-containing compositions by use of the composition according to the invention and to the use of said composition for degumming triglyceride-containing compositions.

The present disclosure relates to methods, cells, and compositions for producing a product of interest, e.g., a recombinant protein. In particular, the present disclosure provides improved mammalian cells expressing the product of interest, where the cells (e.g., Chinese Hamster Ovary (CHO) cells) have reduced or eliminated activity, e.g., expression, of certain host cell proteins, e.g., enzymes including, but not limited to, certain lipases, esterases, and/or hydrolases.

Provided is a method which can produce a target protein while stably maintaining a vector without any special genetic manipulation of host cells and without use of a drug resistance gene or the like. A method for producing a target protein including culturing cells transformed with a vector, the vector containing a gene of the target protein and not containing an antibiotic resistance gene, a recombinase recognition sequence, or a gene essential for cell survival.