Compositions and methods for converting at least one glucosinolate to an isothiocyanate using Bacillus subtilis 839, Bacillus subtilis CO4_4, Pediococcus pentosaceus M3_H01, and/or Pediococcus pentosaceus M2_H12, or active variants thereof, are provided. Conversion of glucosinolates, such as glucoraphanin, to isothiocyanates, such as sulforaphane, leads to the stimulation of the Nrf2/Keap pathway and phase II enzymes, providing chemoprotective and anti-inflammatory effects. Accordingly, provided herein are compositions comprising Bacillus subtilis 839, Bacillus subtilis CO4_4, Pediococcus pentosaceus M3_H01, and/or Pediococcus pentosaceus M2_H12, or active variants thereof, for administration to subjects for increasing isothiocyanate (e.g., sulforaphane) production, increasing the expression of genes regulated by the Nrf2 transcription factor, including phase II enzymes, decreasing inflammation, and treating or preventing an inflammatory disorder or a cancer. The composition can comprise at least one glucosinolate or a plant, plant part or an extract thereof comprising glucosinolate(s).

A monooxygenase having an amino acid sequence obtained by mutation of the amino acid sequence shown in SEQ ID NO:2 is disclosed. The use of the monooxygenase of the present invention in production of chiral sulfoxide-based drugs has advantages including mild reaction conditions, environmental friendliness, high yield, high optical purity of products, less peroxide products, and the like, and therefore the monooxygenase in the present invention has a good industrial application prospect in the production of proton pump inhibitors for the treatment of gastric ulcers.

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.

Non-naturally occurring microorganisms are provided that produce taurine and/or taurine precursors, e.g., hypotaurine, sulfoacetaldehyde, or cysteate, utilizing exogenously added enzyme activities. Methods of producing taurine and/or taurine precursors in microbial cultures, and feed and nutritional supplement compositions that include taurine and/or taurine precursors produced in the microbial cultures, such as taurine- and/or taurine precursor-containing biomass, are also provided.

Non-naturally occurring microorganisms are provided that produce taurine and/or taurine precursors, e.g., hypotaurine, sulfoacetaldehyde, or cysteate, utilizing exogenously added enzyme activities. Methods of producing taurine and/or taurine precursors in microbial cultures, and feed and nutritional supplement compositions that include taurine and/or taurine precursors produced in the microbial cultures, such as taurine- and/or taurine precursor-containing biomass, are also provided.

Metabolites produced by a microorganism using more particularly oxaloacetate as substrate or co-substrate upstream in the biosynthesis pathway. There is indeed a need in the art for transformed, in particular recombinant, microorganisms having at least an increased ability to produce oxaloacetate, thus allowing an increased capacity to produce oxaloacetate-derived amino acids and amino acid derivatives, the oxaloacetate-derived amino acids and amino acid derivatives being termed oxaloacetate derivatives. The solution is the use of a genetically modified yeast including many modifications as described in the present text.

Waste gas mixtures produced and used in industry may contain harmful sulphurous compounds. The present disclosure provides a method for treatment of gas mixtures contaminated with harmful sulphurous compounds by using microorganisms capable of degrading said harmful sulphurous compounds which involves controlling nitrate levels in the medium in which microbiological conversion of harmful sulphurous compounds takes place at high levels.

Waste gas mixtures produced and used in industry may contain harmful sulphurous compounds. The present disclosure provides a method for treatment of gas mixtures contaminated with harmful sulphurous compounds by using microorganisms capable of degrading said harmful sulphurous compounds which involves controlling nitrate levels in the medium in which microbiological conversion of harmful sulphurous compounds takes place at high levels.

An engineered microbe that contains a designed platform for the conversion of one-carbon substrates to chemical products is described. The designed platform embodies a new metabolic architecture that consolidates carbon fixation, central metabolism, and product synthesis into a single pathway. This is made possible by the key finding that 2-hydroxyacyl-CoA lyase, an enzyme in the α-oxidation pathway, is capable of catalyzing the C—C bond formation between formyl-CoA and aldehydes of different chain lengths, allowing for the elongation of the carbon backbone of said aldehyde by one-carbon units. These novel microbes present an opportunity for the production of chemicals from single-carbon feedstocks such as carbon dioxide, carbon monoxide, formate, formaldehyde, methanol or methane.

An engineered microbe that contains a designed platform for the conversion of one-carbon substrates to chemical products is described. The designed platform embodies a new metabolic architecture that consolidates carbon fixation, central metabolism, and product synthesis into a single pathway. This is made possible by the key finding that 2-hydroxyacyl-CoA lyase, an enzyme in the α-oxidation pathway, is capable of catalyzing the C—C bond formation between formyl-CoA and aldehydes of different chain lengths, allowing for the elongation of the carbon backbone of said aldehyde by one-carbon units. These novel microbes present an opportunity for the production of chemicals from single-carbon feedstocks such as carbon dioxide, carbon monoxide, formate, formaldehyde, methanol or methane.