The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme including the capability of reducing 5-((4S)-2-oxo-4-phenyl (1,3-oxazolidin-3-yl))-1-(4-fluorophenyl) pentane-1,5-dione to (4S)-3-[(5S)-5-(4-fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize the intermediate (4S)-3-[(5S)-5-(4-fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one in a process for making Ezetimibe.

The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize chiral compounds.

The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize chiral compounds.

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.

The present disclosure relates to compositions and methods for producing stereoisomerically pure aminocyclopropanes.

Provided herein, in some embodiments, are artificial ribosomes that synthesize nonribosomal peptides, polyketides, and fatty acids with full control over peptide sequence. Also provided herein are methods for programmed synthesis of nonribosomal peptides, polyketides, and fatty acids. In particular, provided herein are methods for scalable synthesis of a wide range of antibacterial, antifungal, antiviral, and anticancer compounds.

Primary leachate is used as a plant growth stimulant. A fermentation medium is fermented with a microbial culture in a bioreactor to produce a primary leachate comprising microorganisms derived from the microbial culture and/or naturally occurring microorganisms. The primary leachate is isolated from the bioreactor, diluted with water, and used to irrigate plants to reduce bacterial diversity and stimulate beneficial microorganisms in the rhizosphere around the plants. The fermentation medium may be organic waste, preferably food waste. A secondary leachate may also be used as a plant growth stimulant. The primary leachate is used to culture black soldier fly larvae with a substrate in a secondary processing bioreactor under suboptimal culture conditions, thereby producing secondary leachate. Melanin is extracted therefrom by acid precipitation. The secondary leachate is then diluted with water and used to irrigate plants, reducing bacterial diversity and stimulating beneficial microorganisms in the rhizosphere around the plants.

Primary leachate is used as a plant growth stimulant. A fermentation medium is fermented with a microbial culture in a bioreactor to produce a primary leachate comprising microorganisms derived from the microbial culture and/or naturally occurring microorganisms. The primary leachate is isolated from the bioreactor, diluted with water, and used to irrigate plants to reduce bacterial diversity and stimulate beneficial microorganisms in the rhizosphere around the plants. The fermentation medium may be organic waste, preferably food waste. A secondary leachate may also be used as a plant growth stimulant. The primary leachate is used to culture black soldier fly larvae with a substrate in a secondary processing bioreactor under suboptimal culture conditions, thereby producing secondary leachate. Melanin is extracted therefrom by acid precipitation. The secondary leachate is then diluted with water and used to irrigate plants, reducing bacterial diversity and stimulating beneficial microorganisms in the rhizosphere around the plants.

A ketoreductase mutant and use thereof are provided. The amino acid sequence of the ketoreductase mutant is an amino acid sequence obtained by mutation of the amino acid sequence shown in SEQ ID NO: 1, wherein the mutation at least comprises one of the following mutation sites: position 6, position 94, position 96, position 117, position 144, position 156, position 193, position 205, position 224, position 176, position 85 and position 108; alternatively, the amino acid sequence of the ketoreductase mutant has a mutation site in a mutated amino acid sequence and an amino acid sequence having 80% or more homology with the mutated amino acid sequence.

A ketoreductase mutant and use thereof are provided. The amino acid sequence of the ketoreductase mutant is an amino acid sequence obtained by mutation of the amino acid sequence shown in SEQ ID NO: 1, wherein the mutation at least comprises one of the following mutation sites: position 6, position 94, position 96, position 117, position 144, position 156, position 193, position 205, position 224, position 176, position 85 and position 108; alternatively, the amino acid sequence of the ketoreductase mutant has a mutation site in a mutated amino acid sequence and an amino acid sequence having 80% or more homology with the mutated amino acid sequence.