The present application relates to the technical field of genetic engineering, and provides a monooxygenase mutant, a preparation method and application thereof. The monooxygenase mutant has any one of the amino acid sequences shown in (I) and (II): (I) an amino acid sequence having at least 80% identity with the amino acid sequence shown in SEQ ID NO. 1; and (II) an amino acid sequence obtained by modifying, substituting, deleting, or adding one or several amino acids to the amino acids at 23 to 508 positions of the amino acid sequence shown in SEQ ID NO. 1, the substituting referring to a substitution of 1 to 34 amino acids, wherein the mutant has the activity of monooxygenase.

The present invention relates to a selective process for preparing sulfones from sulfides by enzymatic catalysis, and to a composition comprising a symmetrical sulfide, an oxidoreductase enzyme catalyzing the oxidation of said symmetrical sulfide to symmetrical sulfone; optionally at least one cofactor C of said enzyme E; and an oxidant, which allows in particular the implementation of said process.

Described herein are an immobilized enzyme, and a preparation method therefor and a use thereof. The immobilized enzyme includes activated PEI and an enzyme covalently bonded to the activated PEI, where the enzyme is selected from any one of a transaminase, a ketoreductase, a monooxygenase, an ammonia lyase, an ene-reductase, an imine reductase, an amino acid dehydrogenase and a nitrilase.

The present invention relates to non-naturally occurring polypeptides useful for preparing armodafinil, polynucleotides encoding the polypeptides, and methods of using the polypeptides. The non-naturally occurring polypeptides of the present invention are effective in carrying out biocatalytic conversion of the (i) 2-(benzhydrylsulfinyl)acetamide to (−)-2-[(R)-(diphenylmethyl)sulfinyl]acetamide (armodafinil), or (ii) benzhydryl-thioacetic acid to (R)-2-(benzhydrylsulfinyl)acetic acid, which is a pivotal intermediate in the synthesis of armodafinil, in enantiomeric excess.

Multi-enzyme systems attached to nanoparticles are effective to efficiently and controllably incorporate stable isotopes (such as deuterium) during the synthesis of small molecules. In one example, deuterium is incorporated into (+)-dihydrocarvide using a cascade involving the enzymes (a) pentaerythritol tetranitrate reductase (PETNR) and (b) flavin-dependent cyclohexanone monooxygenase triple variant F249A/F280A/F435A (CHMO.sub.3M).

The invention includes a process of producing methyl methacrylate or derivatives thereof is described. The process includes the steps of converting 2-butanone to methyl propionate using a Baeyer-Villiger monooxygenase, and treating the methyl propionate produced to obtain methyl methacrylate or derivatives thereof. A method of preparing polymers or copolymers of methyl methacrylate or its derivatives is also described.

An eco-compatible method is used to synthesize 2H-HBO optionally substituted at the β-position of the lactone function from LGO or a saturated form of LGO such as dihydrolevoglucosenone (2H-LGO) or LGO hydrate (OH-LGO) via a biocatalytic reaction using a cyclohexanone monooxygenase (CHMO).

Disclosed are a monooxygenase mutant and use thereof. An amino acid sequence of a monooxygenase mutant is an amino acid sequence obtained by mutating an amino acid sequence as shown in SEQ ID NO: 1. Mutation includes at least one of the following mutation sites: site 49, site 60, site 61, site 144, site 145, site 146, site 147, site 167, site 169, site 189, site 246, site 247, site 280, site 284, site 285, site 286, site 287, site 328, site 330, site 332, site 382, site 427, site 428, site 429, site 430, site 431, site 432, site 433, site 434, site 435, site 436, site 438, site 441, site 493, site 494, site 508, site 509, site 510, site 511, site 512, and site 513 sites and the like. The monooxygenase mutant has the advantage of greatly improved stereoselectivity, and the enzyme activity is also improved correspondingly.

Provided is an immobilized enzyme, a preparation method and use thereof. The immobilized enzyme includes an enzyme and an amino resin carrier for immobilizing the enzyme, and the enzyme is selected from any one of the following enzymes: transaminase, ketoreductase, monooxygenase, ammonia-lyase, ene reductase, imine reductase, amino acid dehydrogenase, and nitrilase. The amino resin carrier is an amino resin carrier modified by a cross-linking agent, and the cross-linking agent is a cross-linking agent treated by a polymer. By means of modifying the amino resin carrier with the cross-linking agent treated by the polymer, the enzyme immobilized on the amino resin carrier may easily form a network cross-linking, such that the immobilization effect of the enzyme is more stable, thereby the recycling efficiency of the enzyme is improved.

The present invention relates to a selective process for preparing sulfoxides from sulfides by enzymatic catalysis, and to a composition comprising a symmetrical sulfide, an oxidoreductase enzyme catalyzing the oxidation of said symmetrical sulfide to symmetrical sulfoxide; optionally at least one cofactor C of said enzyme E; and an oxidant, which allows in particular the implementation of said process.