289 results about "Alcohol dehydrogenase" patented technology

The invention discloses an alcohol dehydrogenase mutant and application of the alcohol dehydrogenase mutant in asymmetric synthesis of (S)-6-hydroxy-8-chloro ethyl caprylate with optical purity. The alcohol dehydrogenase or the mutant thereof provided by the invention has extremely high conversion rate and can effectively improve the optical purity of the product. Moreover, based on the mutant, low-cost, efficient and rapid production of single-configuration ethyl 6-hydroxy-8-chloro caprylate can be realized, a multi-configuration mixture is not generated, and the problems of tedious steps, pollution and the like caused by a conventional chemical synthesis method are also avoided.

The present disclosure provides a recombinant yeast host cell for converting a carbohydrate to ethanol and acetone. The recombinant yeast host cell comprises an engineered metabolic pathway to convert acetyl-CoA to acetone, a downregulated native alcohol dehydrogenase (ADH) gene, and a heterologous alcohol dehydrogenase.

The invention relates to the field of biochemical engineering, in particular to an alcohol dehydrogenase mutant and application thereof. The mutant is obtained by mutating alcohol dehydrogenase with an amino acid sequence encoding SEQ ID NO: 4 at one or more sites selected from 62nd, 108th, 130th, 132, 134, 182nd, 206th, 287th, 303th, 313th and 314, and the mutation is that the amino acid at the site is mutated into one of A, G, V, L, I, P, F, Y, W, S, T, C, M, N, Q, D, E, K, R and H. According to the alcohol dehydrogenase mutant and the application of the alcohol dehydrogenase mutant, the feeding amount of substrates is increased; the high conversion rate (gt; 99%) of the substrate is realized; according to the present invention, the new YqjM has the good product ee value (gt; 98%), and it is determined that the YqjM derived from the bacillus subtilis old yellow enzyme (belonging to ketene reductase) has the optimal catalytic activity, such that the good industrial application performance is provided.

The invention discloses a biological catalytic synthesis method of norambrox ether, which comprises the following steps: step 1, starting from trans-nerolidol, carrying out carroll rearrangement reaction to synthesize farnesyl acetone; 2, in the presence of a cofactor, converting farnesyl acetone into high farnesol acetate under catalysis of Bayer-Villiger monooxygenase; step 3, catalyzing the deacetylation of the high-farnesol acetate by using esterase to obtain EE-high-farnesol; and step 4, carrying out enzymatic conversion on farnesol by using the squalene hopaene cyclase mutant to obtain norambrox ether. The transformation process is safe and non-toxic, Bayer-Villiger monooxygenase which is new with a key enzyme, natural co-expressed esterase, alcohol dehydrogenase and squalene and hopaene cyclase mutants matched with the system are used for synergistic transformation, so that not only is the coenzyme for oxidation reaction promoted to be recycled, but also the conversion efficiency is improved; conversion from farnesyl acetone to norambrox ether can be efficiently and specifically catalyzed, and a final product can be directly obtained from a reaction system without separation and purification of an intermediate.

The invention belongs to the field of biology, and particularly relates to a fusion protein for promoting synthesis of 1, 3-propylene glycol and application of the fusion protein. The fusion protein NADPH (Nicotinamide Adenine Dinucleotide Phosphate) dependent alcohol dehydrogenase fusion protein or NADH (Nicotinamide Adenine Dinucleotide Hormone) dependent alcohol dehydrogenase fusion protein disclosed by the invention can be packaged into diol dehydratase and can promote the synthesis of 1, 3-propylene glycol. Experiments prove that the bacillus subtilis has an effect of improving the fermentation performance of the strain.

The invention discloses a medicinal and edible anti-alcoholism composition and a preparation method thereof, and relates to the crossing field of biotechnology and food and medicine, the composition comprises the following components: dried orange peel powder, vitamin C, glutathione, phellinus igniarius extract, polygonatum sibiricum extract, oriental wormwood extract, isatis root extract, schisandra chinensis extract, ginseng powder, lucid ganoderma extract and licorice extract. Silymarin, puerarin, white tomato powder, watermelon powder, fucoidin, tomato powder, mung bean powder, celery powder, turmeric powder, hawthorn fruit powder, honey powder, corn peptide, soybean peptide powder, xanthan gum and stevioside are added. The composition provided by the invention has the effect of increasing the content of ethanol dehydrogenase and acetaldehyde dehydrogenase in blood after drinking, and has the capability of promoting alcohol metabolism.

The invention provides application of a lactobacillus mucus fermentation strain A21196 in preparation of a product for promoting ethanol metabolism, and belongs to the technical field of microbial preparations. The lactobacillus mucus fermentation strain A21196 has the high-yield ethanol dehydrogenase and acetaldehyde dehydrogenase, and has the effects of reducing the content of ethanol and acetaldehyde in the blood of mice suffering from acute alcoholism and shortening the central nervous inhibition time in vivo. Therefore, the invention provides the application of the fermented lactobacillus mucus strain A21196 in preparation of a product for preventing and / or treating the alcoholic liver injury or the alcoholic liver disease.

The invention discloses a Lactobacillus paracasei grx06 and an application thereof in the aspects of dispelling the effects of alcohol and protecting the liver, the strain number of the Lactobacillus paracasei is grx06, the Lactobacillus paracasei is preserved in the China General Microbiological Culture Collection Center on February 18, 2025, and the preservation number is CGMCC No: 33560. The lactobacillus paracasei obtained by screening in the invention has the capability of producing ethanol dehydrogenase and acetaldehyde dehydrogenase at high yield, and is high in ethanol tolerance. In addition, the traditional Chinese medicine composition has the effects of promoting ethanol metabolism in rats and recovering liver injury. Wide application prospects are realized in the field of anti-alcohol and liver-protecting products.

The invention discloses an enzyme catalytic synthesis method of a luliconazole chiral intermediate, which comprises the following steps: adding a recombinant escherichia coli wet cell for expressing alcohol dehydrogenase, a recombinant escherichia coli wet cell for expressing formate dehydrogenase, a buffer solution, a substrate, a cosolvent, ammonium formate and a coenzyme into a reaction container, reacting at 25-35 DEG C for 2-24 hours, extracting, separating, and carrying out rotary evaporation, thereby obtaining the luliconazole chiral intermediate. The luliconazole chiral intermediate is obtained; the substrate is 2, 2 ', 4'-trichloroacetophenone; the alcohol dehydrogenase is a mutant of AKR3. The method is mild in reaction condition, environmentally friendly, high in regioselectivity and stereoselectivity, high in conversion rate, high in chiral purity, small in enzyme dosage, low in preparation cost and suitable for industrial production.

This invention relates to the field of chicken gizzard lining processing technology, and particularly to an active polypeptide of chicken gizzard lining, its preparation method, and functional products. The preparation method includes the following steps: mixing chicken gizzard lining powder with water and subjecting it to alkaline heat treatment to form a slurry; sequentially adding Bacillus licheniformis alkaline protease, trypsin, and pepsin to the slurry for three separate hydrolysis processes to obtain a hydrolysate; after enzyme inactivation treatment of the hydrolysate, adding Lactobacillus plantarum for fermentation to obtain a fermentation broth; sterilizing the fermentation broth and then filtering it to obtain a fermentation supernatant; sequentially subjecting the fermentation supernatant to membrane filtration, sterilization, and spray drying to obtain the active polypeptide of chicken gizzard lining. The active polypeptide of chicken gizzard lining prepared by the method of this invention exhibits alcohol dehydrogenase activating activity, AGEs inhibitory activity, albumin denaturation inhibitory activity, lipoxygenase inhibitory activity, pancreatic lipase inhibitory activity, and a beneficial bacteria proliferation promoting effect.

The invention discloses ethanol dehydrogenase, recombinant genetically engineered bacteria and application of the ethanol dehydrogenase in asymmetric reduction of prochiral carbonyl compounds, the ethanol dehydrogenase has good biological performance, heterologous expression in Escherichia coli engineering bacteria is achieved, intracellular coenzyme can be directly utilized when whole cells are adopted as a catalyst, and the catalyst has a good application prospect. Zero addition of the coenzyme is realized, the enzyme has the advantages of high activity, high stereoselectivity, wider substrate spectrum and the like, prochiral ketone compounds can be greenly and efficiently catalyzed to be converted into corresponding chiral alcohols, and the problems of low conversion rate, low yield, low e.e. Value, complex reaction process, more byproducts and the like in a traditional chemical method are solved. The ethanol dehydrogenase has good tolerance to isopropanol, and the isopropanol can be used as a hydrogen source to realize the circulation of coenzyme. And the byproduct acetone generated by the enzyme catalytic reaction and the isopropanol remaining in the reaction can be separated and recovered by a technical means, so that the production cost is greatly reduced.

The present invention relates to the field of microbial fermentation technology, and in particular to a Pediococcus pentosaceus ZKPp0412, Pueraria lobata fermentation liquid and their application in preparing alcohol sobering and liver protecting products. Pediococcus pentosaceus )ZKPp0412 was deposited in the General Microbiology Center of the China Microbiological Culture Collection Administration on June 21, 2023, with the deposit number CGMCC No.27674, and the deposit address is No. 3, Yard No. 1, Beichen West Road, Chaoyang District, Beijing. The Pueraria lobata fermentation liquid prepared by fermenting the Pueraria lobata extract by this strain has a lower pH and a higher number of viable bacteria, and can promote the activity of alcohol dehydrogenase and acetaldehyde dehydrogenase in vitro. In vivo experiments have verified that the Pueraria lobata fermentation liquid has the effect of sobering up and sobering up drunk mice, and can effectively inhibit alcohol-induced liver enlargement / liver damage.

The present invention discloses a method for synthesizing rasagiline in a microfluidic field. The method is based on a double enzyme hydrogenation cascade reaction, which efficiently converts racemic alcohol into enantiomeric amines, realizes the direct synthesis of chiral amines, and has high atom economy and reaction efficiency. Racemic 1-indanol is completely oxidized to generate 1-indanone by alcohol dehydrogenase catalysis, and the cofactor NADP+ is reduced to NADPH to provide the required reducing power for subsequent reactions; using ( R )-selective reductive amino enzyme catalyzes the reductive amination reaction of 1-indanone to generate the target product rasagiline. The present invention adopts a dual enzyme synergistic catalytic strategy to successfully achieve the efficient conversion from racemic alcohol to chiral amine, has the advantages of mild reaction conditions, green sustainability, high product yield and optical purity, and provides a new efficient, economical and environmentally friendly way for the synthesis of rasagiline.

The invention discloses an Escherichia coli endogenous alcohol dehydrogenase EcYjgB mutant and application thereof. The mutant is obtained by performing any one of the following mutations (a) to (c) on Escherichia coli endogenous alcohol dehydrogenase EcYjgB as shown in SEQ ID NO.1: (a) mutating serine at the 200th site into arginine; (b) the serine at the 199th site is mutated into aspartic acid, and the serine at the 200th site is mutated into arginine; and (c) the serine at the 199th site is mutated into aspartic acid, the serine at the 200th site is mutated into arginine, and the asparagine at the 240th site is mutated into tryptophan. The mutant is used for efficiently catalyzing reduction of HMF or furfural to respectively synthesize BHMF and furfuryl alcohol, so that the purposes of improving the production efficiency, reducing the production cost and improving the environmental effect are achieved.

The invention relates to a method for producing vanillin from natural lignocellulose biomass through co-culture of pichia pastoris, which comprises the following steps: respectively constructing a xylan hydrolysis recombinant strain (for releasing ferulic acid) and a vanillin synthesis recombinant strain (for converting ferulic acid) to realize conversion production from a natural xylan substrate to vanillin. In order to reduce the generation of by-products, 15 genes for coding aldehyde dehydrogenase (ALDRs), alcohol dehydrogenase (ADHs) and aldehyde ketoreductase (AKRs) are further knocked out from the vanillin synthesis recombinant strain, so that the vanillin can be further converted into the by-product vanillic acid, thereby improving the yield and purity of the vanillin.

The invention discloses an alcohol dehydrogenase mutant with high yield of nootkatone and a preparation method of the alcohol dehydrogenase mutant, alcohol dehydrogenase from alpinia oxyphylla is subjected to site-specific mutagenesis, and the mutagenesis is at least one of S197V, M144C and L196A. The alcohol dehydrogenase mutant provided by the invention has high catalytic activity, and the yield of nootkatone prepared by using the mutant M144C / L196A / S197V to catalyze nocardanol can reach 99%, which is 4.32 times that of an original enzyme; the alcohol dehydrogenase mutant is simple in production process, mild in reaction condition, environment-friendly in production process, beneficial to industrial production of nootkatone and wide in application prospect.

Disclosed in the present invention is a method for synthesizing indigo and derivatives thereof by means of dual-enzyme cascade catalysis, comprising: using an aminophenethyl alcohol compound (I) as a substrate to generate indigo and derivatives (III) thereof by means of a reaction catalyzed by alcohol dehydrogenase and flavin-containing monooxygenase. The present invention is convenient to operate, reduces the use of cofactors, and has high yield and good industrial application prospects in biocatalytic preparation of indigo and derivatives thereof.

The invention discloses a genetically engineered probiotic composition for expressing ADH (adenosine dihydrogenase) and ALDH (aldehyde dehydrogenase) and application of the genetically engineered probiotic composition in hangover alleviating and liver protection. The genetically engineered probiotic composition (such as EcN.1917-ADH and EcN.1917-ALDH) is constructed by introducing genes of alcohol dehydrogenase (ADH, NCBI (National Center for Biotechnology Information) Gene ID: 855349) and acetaldehyde dehydrogenase (ALDH, NCBI Gene ID: 855206) of saccharomyces cerevisiae into probiotics (such as escherichia coli). The engineering bacterium shows remarkable ethanol, acetaldehyde and endurance capacity in an in-vitro experiment, and the ethanol degradation rate is remarkably higher than that of a wild type strain; a mouse drunkenness model verifies that drunkenness and death caused by drinking can be reduced through pretreatment, drunkenness tolerance time is remarkably prolonged, and movement coordination disorder caused by alcohol can be improved. The strain can effectively promote alcohol metabolism and relieve alcoholic liver injury, and a new candidate strain is provided for development of a hangover-alleviating and liver-protecting viable bacterial preparation.

The invention relates to a preparation method of D-panthenol. The preparation method comprises the following steps: (1) carrying out mixed reaction on DL-pantoic acid lactone and D-pantoic acid lactone hydrolase, extracting, and separating a water phase to obtain D-pantoic acid; (2) mixing the D-pantoic acid with a compound enzyme auxiliary agent for reaction to obtain D-pantoic acid lactone; (3) mixing the D-pantoic acid lactone with beta aminopropanol for reaction to obtain D-panthenol crude product slurry; (4) purifying the D-panthenol crude product slurry to obtain D-panthenol; the compound enzyme auxiliary agent comprises esterase, carbonyl reductase, alcohol dehydrogenase and alcohol nitrile enzyme. According to the method disclosed by the invention, the esterase, the carbonyl reductase, the alcohol dehydrogenase and the alcohol nitrile enzyme act synergistically to catalyze an esterification reaction in D-pantoic acid molecules and promote the D-pantoic acid molecules to form a lactone structure, so that side reactions are reduced, the efficiency of the esterification reaction of the D-pantoic acid is improved, and finally, the yield and the purity of the D-panthenol are improved.

The invention discloses an alcohol dehydrogenase mutant for high yield of tea flavor ketone and application of the alcohol dehydrogenase mutant in a one-pot method. The mutant is A182L or A182L / V214T. The alcohol dehydrogenase mutant has high catalytic activity on 4-hydroxyisophorone, and the yield of tea flavor ketone prepared by catalysis of the mutant A182L / V214T can reach 97% and is 3.73 times that of an original enzyme; the alcohol dehydrogenase mutant has high catalytic activity of synthesizing the tea aroma ketone through one-pot catalysis of isophorone, and the yield of the tea aroma ketone obtained through direct oxidation of isophorone by jointly using the mutant A182L / V214T and a cytochrome P450BM3 monooxygenase mutant can reach 92%; the alcohol dehydrogenase mutant has the advantages of simple production process, mild reaction conditions and environment-friendly production process, is beneficial to the industrial production of the tea flavor ketone, and has wide application prospects.

The invention discloses an ethanol dehydrogenase mutant and an application of the ethanol dehydrogenase mutant in synthesis of symmetric chiral diol. The ethanol dehydrogenase mutant is obtained by carrying out single mutation or multiple mutations on amino acids at 74th, 187th, 210th, 211th and 352th sites of an ethanol dehydrogenase amino acid sequence as shown in SEQ ID NO.2 from Candida orbiculata Co. The invention further discloses a preparation method of the ethanol dehydrogenase mutant, and the preparation method comprises the following steps: carrying out single mutation or multiple mutations on the amino acids at the 74th, 187th, 210th, 211th and 352th sites of the ethanol dehydrogenase amino acid sequence as shown in SEQ ID NO.2. Alcohol dehydrogenase is utilized to catalyze prochiral symmetric diketone to synthesize symmetric chiral diol, the method is high in substrate concentration, high in stereoselectivity, mild in reaction, simple in operation process, environment-friendly and more suitable for industrial amplification production, and the problems that in the prior art, the substrate concentration is not high, the reaction condition is violent, the reaction process is complex and difficult to control, and the production cost is low are solved. And the method is not environment-friendly enough, and the like.

The invention discloses 10-hydroxydecanoic acid as well as a preparation method and application thereof, and belongs to the technical field of cosmetics, Candida lipolytica is taken as a fermentation thallus, the Candida lipolytica contains alkane monooxygenase (CYP450), alcohol dehydrogenase (ADH), fatty alcohol oxidase (FAO) and fatty aldehyde dehydrogenase (FALDH), amplification and activation are performed on the Candida lipolytica in a seed culture medium, and the Candida lipolytica is obtained. The method comprises the following steps: inoculating a seed solution into a liquid culture medium, enabling a strain to adapt to a culture environment in advance, reducing strain death caused by environmental mutation after inoculation, inoculating the seed solution into the liquid culture medium, culturing until OD600 is 45-55, realizing high-density enrichment of the strain, being beneficial to increasing the content of CYP450, ADH, FAO and FALDH, adding decane and Tween 80, and enabling the Tween 80 to be capable of increasing the permeability of a cell membrane and increasing the reaction rate, the CYP450 is used for catalyzing decane to carry out hydroxylation, and ADH, FAO and FALDH are used for carrying out oxidation, so that the high-purity 10-hydroxydecanoic acid is obtained.

The application discloses a method for synthesizing high-concentration furfuryl alcohol by using a double-enzyme coupling method, and the method comprises the following steps: mixing alcohol dehydrogenase freeze-dried bacterial powder and glucose dehydrogenase freeze-dried bacterial powder to serve as a catalyst, using furfural as a substrate, using glucose as a co-substrate, using NADP + or NAD + as a coenzyme, using a buffer solution with a pH value of 4-9 as a reaction medium to form a reaction system, and reacting completely under the condition of 20-50 DEG C and 400 rpm, then separating and purifying the reaction liquid to obtain furfuryl alcohol. The biological catalytic system is suitable for furfural with a concentration higher than 500 mM, and 100% conversion of 500 mM can be realized within 10 hours. The substrate continuous flow process is further used to eliminate the inhibition of aldehyde substrates on the biological catalyst, the concentration of the product can reach 1500 mM, and the highest space-time yield can reach 235 g / (L.d).

The invention discloses a Stemphylium alcohol dehydrogenase as well as a coding gene and application thereof, and relates to the technical field of microbial genetic engineering. The alcohol dehydrogenase is any one of (1), (2) and (3): (1) SvADH1 protein, the amino acid sequence of which is as shown in SEQ ID NO.3; (2) carrying out substitution, deletion and / or addition of one or more amino acid residues on the amino acid sequence of the SvADH1 protein to obtain a protein which has more than 70% of identity with the SvADH1 protein and is related to cross-linked solanol A redox; and (3) a fusion protein obtained by connecting a protein tag to the N terminal or / and C terminal of (1) or (2). Research finds that overexpression of the coding gene of the alcohol dehydrogenase in Stemphylium cystosum can significantly improve the yield of the interlinked solanol A, so that a new direction is provided for developing the interlinked solanol A from microorganisms.

The invention relates to the technical field of genetic engineering, in particular to a recombinant microorganism and application thereof in preparation of glycine. The application comprises the following steps: producing glycine by adopting the recombinant microorganism; the recombinant microorganism comprises an enzyme combination and / or a nucleic acid molecule combination. The enzyme combination comprises threonine aldolase, ethanol dehydrogenase and isopropanol dehydrogenase; the threonine aldolase comprises an amino acid sequence as shown in SEQ ID NO. 1. The nucleic acid molecule combination is used for encoding the enzyme combination. According to the invention, threonine aldolase, ethanol dehydrogenase and isopropanol dehydrogenase are converted into microorganisms, and the constructed recombinant microorganisms can be used for decomposing threonine to produce glycine; and a specific system formed by specific isopropanol dehydrogenase, ethanol dehydrogenase and isopropanol dehydrogenase can also have a relatively high conversion rate under the condition of no addition of pyridoxal phosphate (PLP), and has important significance and economic value.

The invention belongs to the technical field of microorganisms, and particularly relates to lactobacillus paracasei BL19 and application thereof to preparation of products with functions of dispelling effects of alcohol and protecting liver. The lactobacillus paracasei BL19 is preserved in the China General Microbiological Culture Collection Center (CGMCC), and the preservation number of the lactobacillus paracasei BL19 is CGMCC No.34368. The lactobacillus paracasei BL19 is named as Lactobacillus paracasei BL19. The lactobacillus paracasei BL19 provided by the invention has relatively strong alcohol tolerance, alcohol degradation capability and relatively high activity of promoting alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH); the lactobacillus paracasei BL19 has the advantages that the lactobacillus paracasei BL19 has good anti-alcohol and anti-liver effects and strong capacity of protecting alcoholic injury liver cells, so that the anti-alcohol and anti-liver effects can be comprehensively achieved from multiple dimensions, and in addition, the lactobacillus paracasei BL19 has strong acid resistance and bile salt resistance, also has strong tolerance to simulated gastrointestinal fluid and has important application value in the fields of anti-alcohol and anti-liver products and the like.

The present invention discloses a method for synthesizing hydroxytyrosol by multi-enzyme cascade, comprising: 1) preparing a hydroxytyrosol product by using 3,4-dihydroxybenzaldehyde, L-threonine, sodium formate, NAD + As raw material, L-threonine transaldolase, alcohol dehydrogenase, and formate dehydrogenase are used to catalyze the synthesis of L-threo-3-(3,4-dihydroxyphenyl)serine; 2) L-threo-3-(3,4-dihydroxyphenyl)serine is used as substrate, glucose, NAD + Hydroxytyrosol is synthesized through a cascade catalysis of phenylserine dehydratase, α-ketoacid decarboxylase, aldehyde reductase, and glucose dehydrogenase. The synthesis method provided by the present invention achieves a hydroxytyrosol yield of >99% and a space-time yield of 0.88 g / L / h, currently the highest, showing great potential for industrial application and suitable for further promotion and application.

The present invention discloses a method for biocatalytic conversion of β-ionol to prepare dihydro-β-ionone, belonging to the technical field of bioengineering. In the present invention, β-ionol is used as a substrate, and short-chain alcohol dehydrogenase NaSDR and enoate reductase AaDBR1 are added for reaction. The reaction temperature is 25-60 °C, the pH is 4.0-11.0, and the reaction time is 0.5-3 h to obtain β-ionone. The present invention uses short-chain alcohol dehydrogenase and enoate reductase for cascade reaction, establishes a process for in vitro one-pot biopreparation of dihydro-β-ionone using β-ionol as a substrate, and realizes the regeneration and self-circulation of NADPH, thus creating a new method for highly efficient and low-cost biosynthesis of dihydro-β-ionone.

The invention relates to the technical field of biological engineering and biological catalysis, in particular to two alcohol dehydrogenase mutants and application thereof. The invention discloses a pair of alcohol dehydrogenase mutants CpAR2-M3 (F85A / F192L / E209A) and CcPAR-M1 (V158L) with opposite stereoselectivity, wherein the corresponding amino acid sequences of the alcohol dehydrogenase mutants CpAR2-M3 (F85A / F192L / E209A) and CcPAR-M1 (V158L) are respectively shown as SEQ ID No.5 and SEQ ID No.6. The invention further discloses a preparation method of the alcohol dehydrogenase mutants. The method can be applied to asymmetric reduction of hemiacetal compounds, synthesis of corresponding key intermediate axial chiral biaryl benzyl alcohol compounds with complementary stereoselectivity is achieved, the highest yield can reach 95%, the highest stereoselectivity can reach 99% e.e., and the method is suitable for industrial production. A green, efficient and high-stereoselectivity synthesis strategy is provided for subsequent enantiocomplementary synthesis of the compounds.

A recombinant methanol utilization pathway deficient methylotrophic yeast (Mut−) host cell which is engineered: a) by one or more genetic modifications to reduce expression of a first and a second endogenous gene compared to the host cell prior to said one or more genetic modifications, wherein i. the first endogenous gene encodes alcohol oxidase 1 (AOX1) comprising the amino acid sequence identified as SEQ ID NO:1 or a homologue thereof, and ii. the second endogenous gene encodes alcohol oxidase 2 (AOX2) comprising the amino acid sequence identified as SEQ ID NO:3 or a homologue thereof, and b) by one or more genetic modifications to increase expression of an alcohol dehydrogenase (ADH2) gene compared to the host cell prior to said one or more genetic modifications, wherein the ADH2 gene encodes an alcohol dehydrogenase (ADH2).