The present invention relates to a polypeptide having lipase activity wherein the polypeptide when aligned with the polypeptide according to SEQ ID NO: 1, comprises at least an amino acid substitution L410X and optionally one or more amino acid substitutions chosen from S365Q, S365N, L413M, G414A, G414S, G414V, G414T, V534L and V534l, wherein the 10 numbering of amino acid position(s) is/are defined with reference to SEQ ID NO: 1. The invention further relates to a process for preparing a product comprising an oil or fat comprising bringing an intermediary form of the product comprising oil or fat into contact with a polypeptide as disclosed herein and the use of a polypeptide as disclosed herein to saturated fatty acids in an oil or fat.

The present invention relates to a lipase-producing strain and application thereof. The strain is classified and named Bacillus subtilis CS1802, with a preservation number of CCTCC NO: M2018262. The strain can be used to produce vitamin A palmitate through whole-cell transformation of vitamin A and palmitic acid. The Bacillus subtilis CS1802 of the present invention is derived from traditional natural fermented food and is a microorganism generally recognized as safe. The strain can be easily cultured and preserved. The highest content of vitamin A palmitate obtained through whole-cell transformation of vitamin A and palmitic acid is 15.35 mg/L. The highest transformation efficiency is 76.75%. The strain provides a new path for enzymatic synthesis of vitamin A palmitate and has important application prospects.

The present invention relates to an enzymatic process for preparation of optically pure enantiomers of homopropargylic alcohol compounds of formula I, which are useful intermediates for the synthesis of Halichondrin B and analogs. wherein, P is H or an alcohol protecting group, n is an integer ranging from 0-12.

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The present invention relates to an enzymatic process for preparation of optically pure enantiomers of homopropargylic alcohol compounds of formula I, which are useful intermediates for the synthesis of Halichondrin B and analogs. wherein, P is H or an alcohol protecting group, n is an integer ranging from 0-12.

##STR00001##

Bioactive coatings that are stabilized against inactivation by weathering are provided including a base associated with a chemically modified enzyme, and, optionally a first polyoxyethylene present in the base and independent of the enzyme. The coatings are optionally overlayered onto a substrate to form an active coating facilitating the removal of organic stains or organic material from food, insects, or the environment.

Bioactive coatings that are stabilized against inactivation by weathering are provided including a base associated with a chemically modified enzyme, and, optionally a first polyoxyethylene present in the base and independent of the enzyme. The coatings are optionally overlayered onto a substrate to form an active coating facilitating the removal of organic stains or organic material from food, insects, or the environment.

The present disclosure discloses a method for increasing the usage efficiency of a lipase in the enzymatic reaction, belonging to the technical field of food processing. In the present disclosure, the peroxide value of raw materials required for enzymatic synthesis of a structured lipid is reduced by a distillation method or an adsorption method, and then the raw material and a lipase undergo catalytic reaction to synthesize the structured lipid, so as to maintain the activity of the lipase and increase the reuse rate of the enzyme. The distillation method includes deodorization and molecular distillation. The present disclosure provides a method for manufacturing a structured lipid by a high efficiency and low-cost enzymatic synthesis, addressing to the issues such as large enzyme consumption, expansive cost, low enzyme utilization rate in the traditional industrial production. Therefore, the method provided by the present disclosure has certain development potential and practical significance.

In alternative embodiments, provided are compositions and methods for making a chimeric polypeptide comprising an S-layer polypeptide and a heterologous polypeptide or peptide. In alternative embodiments, the compositions and methods comprise recombinantly engineering a methylotrophic or methanotrophic bacteria to recombinantly express a chimeric polypeptide comprising an S-layer polypeptide and a heterologous polypeptide or peptide. Also provided are compositions and methods for displaying or immobilizing proteins on a methanotrophic S-layer. In alternative embodiments, provided are compositions and methods comprising recombinant methylotrophic or methanotrophic bacteria comprising assembled or self-assembled recombinant or isolated chimeric S-layer polypeptides. In alternative embodiments, provided are compositions and methods using recombinant methylotrophic or methanotrophic bacteria, optionally a Methylomicrobium alcaliphilum, optionally a M. alcaliphilum sp. 20Z, for ectoine ((4S)-2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid), for the production or synthesis of a protein, e.g., an ectoine, or an enzyme, e.g., a lipase.

In alternative embodiments, provided are compositions and methods for making a chimeric polypeptide comprising an S-layer polypeptide and a heterologous polypeptide or peptide. In alternative embodiments, the compositions and methods comprise recombinantly engineering a methylotrophic or methanotrophic bacteria to recombinantly express a chimeric polypeptide comprising an S-layer polypeptide and a heterologous polypeptide or peptide. Also provided are compositions and methods for displaying or immobilizing proteins on a methanotrophic S-layer. In alternative embodiments, provided are compositions and methods comprising recombinant methylotrophic or methanotrophic bacteria comprising assembled or self-assembled recombinant or isolated chimeric S-layer polypeptides. In alternative embodiments, provided are compositions and methods using recombinant methylotrophic or methanotrophic bacteria, optionally a Methylomicrobium alcaliphilum, optionally a M. alcaliphilum sp. 20Z, for ectoine ((4S)-2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid), for the production or synthesis of a protein, e.g., an ectoine, or an enzyme, e.g., a lipase.

The present invention concerns an enzymatic process for the preparation of an ingredient comprising 1,3-Olein-2-palmitin (OPO), the most abundant triglyceride present in human breast milk. This is achieved by using immobilized lipase from Ther-momyces lanuginosis for producing 1,3-olein-2-palmitin (1,3-Dioleate-2-palmitate-glycerol) using as substrate tripalmitin or triglycerides enriched in palmitic acid at SN-2 position by first alcoholysis in presence of C3 to C5 alcohol (butanol, pentanol, isopropanol) to produce 2-monopalmitin which is purified by selective crystallization at decreased temperature, followed by esterification using the same lipase and oleic acid.