EC Number   |
Recommended Name  |
Application |
|---|
   1.14.11.45 | L-isoleucine 4-hydroxylase |
synthesis |
double mutant I162T/T182N shows improvements in specific activity, protein expression level, and fermentation titer of 3.2-, 2.8-, and 9.4fold, respectively. L-Isoleucine (228 mM) is completely converted to (2S,3R,4S)-4-HIL with a space-time yield of up to 80.8 g/l and d. With a increase of the substrate loading to 1 M, a high conversion of 91% can also be achieved |
| 1.14.11.45 | L-isoleucine 4-hydroxylase |
synthesis |
dynamic regulation of IDO expression by modified Ile biosensors increases the 4-HIL titer from 24.7 mM to 28.9?74.4 mM and may yield more 4-HIL than the static strain overexpressing IDO by the strong PtacM promoter (69.7 mM). Synergistic modulation of 2-oxoglutarate supply and O2 supply improves the 4-HIL production significantly, and the highest titer achieved is 135.3 mM |
| 1.14.11.45 | L-isoleucine 4-hydroxylase |
synthesis |
improved synthesis of 4-HIL by ribosomal binding site engineering for gene expression in Corynebacterium glutamicum. To supply the cosubstrate 2-oxoglutarate at different levels, the OdhI gene is expressed using the ribosomal binding site sequences. The O2 supply is further enhanced in by overexpressing the Vgb gene. 4-HIL (up to 119.27 mM) is produced in the best strain. The synchronic supply of cosubstrates 2-oxoglutarate and O2 is critical for the high-yield production of 4-HIL |
| 1.14.11.45 | L-isoleucine 4-hydroxylase |
synthesis |
improved synthesis of 4-HIL in an optimized strain of Corynebacterium glutamicum by application of programming adaptive laboratory evolution. The programming evolutionary system contains a Lys biosensor LysG-PlysE and an evolutionary actuator composed of a mutagenesis gene and a fluorescent protein gene. After successive rounds of evolution, mutant strains with significantly increased 4-HIL production and growth performance are obtained. The maximum 4-HIL titer is 152.19 mM, 28.4% higher than the starting strain |
| 1.14.11.45 | L-isoleucine 4-hydroxylase |
synthesis |
in a genome-edited recombinant strain Escherichia coli BL21(DE3) DELTAsucABDeltaaceAK/pET-28a(+)-ido (2DELTA-ido), the bioconversion ratio of L-Ile to 4-HIL is enhanced by about 15% compared to Escherichia coli BL21(DE3)/pET-28a(+)-ido [BL21(DE3)-ido] |
| 1.14.11.45 | L-isoleucine 4-hydroxylase |
synthesis |
recombinant Escherichia coli expressing mutant N126H/T130K or wild-type synthesizes 66.50 mM and 26.09 mM 4-hydroxyisoleucine, respectively, in 24 h |
 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
development of yeast-based bioprocesses to produce lactate from lignocellulosic raw material |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
the enzyme has a commercial significance, as it can be used to produce chiral building blocks for the synthesis of key pharmaceuticals and agrochemicals, optimization of enzyme reaction by engineering to eliminate the substrate inhibition |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
the enzyme might be useful in the production of phenyllactate |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
a lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta) deletion strain is evolved for 2,000 h, resulting in a stable strain with 40:1 ethanol selectivity and a 4.2-fold increase in ethanol yield over the wild-type strain. In a coculture of organic acid-deficient engineered strains of both Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, fermentation of 92 g/liter Avicel results in 38 g/liter ethanol, with acetic and lactic acids below detection limits, in 146 h. engineering is based on a phosphoribosyl transferase (Hpt) deletion strain, which produces acetate, lactate, and ethanol in a ratio of 1.7:1.5:1.0, similar to the 2.1:1.9:1.0 ratio produced by the wild type. The Hpt/Ldh double mutant strain does not produce significant levels of lactate and has a 1.4:1.0 ratio of acetate to ethanol. Similarly, the Hpt/Pta double mutant strain does not produce acetate and has a 1.9:1.0 ratio of lactate to ethanol. The Hpt/Ldh/Pta triple mutant strain achieves ethanol selectivity of 40:1 relative to organic acids |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
construction of a markerless strain lacking phosphotransacetylase Pta, acetate kinase Ack and lactate dehydrogenase Ldh genes. The gene deletion strain ferments 50 g/liter of cellobiose, with a yield of 0.44 g ethanol per g glucose equivalent substrate and a maximum volumetric productivity of 1.13 g ethanol per liter and h. A system for genetic marker removal allows for enactment of further modifications and creation of strains for industrial applications |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
metabolic engineering of Geobacillus thermoglucosidasius to divert the fermentative carbon flux from a mixed acid pathway, to one in which ethanol becomes the major product, involving elimination of the lactate dehydrogenase and pyruvate formate lyase pathways by disruption of the ldh and pflB genes, respectively, and upregulation of expression of pyruvate dehydrogenase. Strains with all three modifications form ethanol efficiently and rapidly at temperatures in excess of 60°C in yields in excess of 90% of theoretical. The strains also efficiently ferment cellobiose and a mixed hexose and pentose feed |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, a heterologous gene GldA encoding an NAD+-dependent glycerol dehydrogenase is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant enzyme acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
L-nLDH is an efficient catalyst that can be used in the enantioselective reduction of alpha-keto acids to alpha-hydroxy acids |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
coexpression of enzyme and glucose dehydrogenase gene in Escherichia coli efficiently reduces 3,4-dihydroxyphenylpyruvate to L-3,4-dihydroxyphenyllactate with 95.45% isolation yield |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
engineering of Kluyveromyces marxianus to express and coexpress various heterologous LDH enzymes for L-lactic acid production. LDH enzymes originating from Staphylococcus epidermidis (SeLDH, optimal at pH 5.6), Lactobacillus acidophilus (LaLDH, optimal at pH 5.3), and Bos taurus (BtLDH, optimal at pH 9.8) are functionally expressed individually and in combination. A strain co-expressing SeLDH and LaLDH produces 16.0 g/l L-lactic acid, whereas the strains expressing those enzymes individually produces only 8.4 and 6.8 g/l, respectively. This coexpressing strain produces 24.0 g/l L-lactic acid with a yield of 0.48 g/g glucose in the presence of CaCO3 |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
engineering of Kluyveromyces marxianus to express and coexpress various heterologous LDH enzymes for L-lactic acid production. LDH enzymes originating from Staphylococcus epidermidis (SeLDH, optimal at pH 5.6), Lactobacillus acidophilus (LaLDH, optimal at pH 5.3), and Bos taurus (BtLDH, optimal at pH 9.8) are functionally expressed individually and in combination. A strain coexpressing SeLDH and LaLDH produces 16.0 g/l L-lactic acid, whereas the strains expressing those enzymes individually produces only 8.4 and 6.8 g/l, respectively. This coexpressing strain produces 24.0 g/l L-lactic acid with a yield of 0.48 g/g glucose in the presence of CaCO3 |
| 1.1.1.27 | L-lactate dehydrogenase |
synthesis |
production of phenyllactic acid from L-Phe by recombinant Escherichia coli coexpressing L-phenylalanine oxidase and L-lactate dehydrogenase. At optimal conditions (L-Phe 6 g/l, pH 7.5, 35°C, CDW 24.5 g/l and 200 rpm), the recombinant strain produces 1.62 g L-phenylalanine/l with a conversion of 28% from L-Phe |
| 1.1.2.3 | L-lactate dehydrogenase (cytochrome) |
synthesis |
the enzyme is potentially important for bioanalytical technologies for highly selective assays of L-lactate in biological fluids and foods |
| 1.1.3.2 | L-lactate oxidase |
synthesis |
biocascade synthesis of L-tyrosine derivatives by coupling a thermophilic tyrosine phenol-lyase and L-lactate oxidase. o-Phenol derivatives are transformed into the corresponding L-tyrosine derivatives with excellent stereoselectivity and high yields using an efficient one-pot, two-step cascade containing thermophilic tyrosine phenol-lyase mutants from Symbiobacterium toebii and L-lactate oxidase from Aerococcus viridans |
| 1.1.3.2 | L-lactate oxidase |
synthesis |
enzymatic preparation of pyruvate by a whole-cell biocatalyst coexpressing L-lactate oxidase and catalase. Under the optimized transformation conditions, pyruvate is produced at a titer of 59.9 g/l and a yield of 90.8% in a substrate fed-batch process, promising an alternative route for the green production of pyruvate |
| 3.5.2.11 | L-lysine-lactamase |
synthesis |
production of D-alpha-amino-beta-caprolactam and L-lysine as nutrient and food supplement |
| 1.8.4.13 | L-methionine (S)-S-oxide reductase |
synthesis |
enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs |
| 3.5.1.101 | L-proline amide hydrolase |
synthesis |
Escherichia coli cells overexpressing the laaA gene have been demonstrated to be applicable to the S-stereoselective hydrolysis of (R,S)-piperazine-2-tert-butylcarboxamide to produce (S)-piperazine-2-carboxylic acid with high optical purity. Enantiomerically pure piperazine-2-carboxylic acid and its tert-butylcarboxamide derivative are important chiral building blocks for some pharmacologically active compounds such as N-methyl-D-aspartate antagonist for glutamate receptor, cardioprotective nucleoside transport blocker and HIV protease inhibitor |
| 1.14.11.56 | L-proline cis-4-hydroxylase |
synthesis |
coexpression of L-proline cis-4-hydroxylase and N-acetyltransferase Mpr1 from Saccharomyces cerevisiae converting cis-4-hydroxy-L-proline into N-acetyl cis-4-hydroxy-L-proline in Escherichia coli. M9 medium containing L-proline produces more N-acetyl cis-4-hydroxy-L-proline than LB medium containing L-proline. The addition of NaCl and L-ascorbate results in a 2fold increase in N-acetyl cis-4-hydroxy-L-proline production in the L-proline-containing M9 medium |
| 5.3.1.14 | L-rhamnose isomerase |
synthesis |
large scale production of L-mannose from L-fructose by immobilized enzyme |
| 5.3.1.14 | L-rhamnose isomerase |
synthesis |
D-allose production from D-psicose by immobilized enzyme |
| 5.3.1.14 | L-rhamnose isomerase |
synthesis |
L-xylose and L-lyxose production from xylitol using Alcaligenes 701B strain and immobilized L-rhamnose isomerase enzyme |
| 5.3.1.14 | L-rhamnose isomerase |
synthesis |
the enzyme, cross-linked with glutaraldehyde and L-lysine, is used to produce D-allose from D-piscose, which is derived from D-fructose by a recombinant D-tagatose 3-epimerase, in a bioreactor plan, method optimization, overview |
| 5.3.1.14 | L-rhamnose isomerase |
synthesis |
40 g/l L-lyxose is produced from 100 g/l L-xylulose by the enzyme during 60 min, while 25 g/l L-mannose is produced from 100 g/l L-fructose in 80 min |
| 5.3.1.14 | L-rhamnose isomerase |
synthesis |
under optimized conditions of pH 7, 70°C, 1 mM Mn2+, 27 U enzyme/l, and 600 g D-allulose/l, 199 g D-allose/l is produced without byproducts over 2.5 h, with a conversion yield of 33% and a productivity of 79.6 g/l/h |
| 5.1.3.4 | L-ribulose-5-phosphate 4-epimerase |
synthesis |
improvement of a bacterial L-arabinose utilization pathway consisting of L-arabinose isomerase from Bacillus licheniformis and L-ribulokinase and L-ribulose-5-phosphate 4-epimerase from Escherichia coli after expression of the corresponding genes in Saccharomyces cerevisiae. After adaptation of codon usage, yeast transformants show strongly improved L-arabinose conversion rates. The ethanol production rate from L-arabinose can be increased more than 2.5fold from 0.014 g ethanol per h and g dry weight to 0.036 g ethanol per h and g dry weight and the ethanol yield can be increased from 0.24 g ethanol per g consumed L-arabinose to 0.39 g ethanol per g consumed L-arabinose |
| 1.1.99.32 | L-sorbose 1-dehydrogenase |
synthesis |
the enzyme (SDH) can be used to directly produce 2-keto-L-gulonic acid from L-sorbose with high substrate/product specificity. A platform strain suitable for highthroughput screening of SDH is constructed |
| 1.1.1.103 | L-threonine 3-dehydrogenase |
synthesis |
over-expression of a feedback-resistant threonine operon thrA*BC, with deletion of the genes that encode threonine dehydrogenase tdh and threonine transporters tdcC and sstT, and introduction of a mutant threonine exporter rhtA23 in Escherichia coliMDS42. The resulting strain shows about 83% increase in L-threonine production when cells are grown by flask fermentation, compared to a wild-type Escherichia coli strain MG1655 engineered with the same threonine-specific modifications described above |
| 4.1.2.5 | L-threonine aldolase |
synthesis |
threonine aldolase is a very promising enzyme that can be used to prepare biologically active compounds or building blocks for pharmaceutical industry. Rational design is applied to thermophilic threonine aldolase from Thermotoga maritima to improve thermal stability by the incorporation of salt and disulfide bridges between subunits in the functional tetramer |
| 1.1.1.10 | L-xylulose reductase |
synthesis |
the microalga Chlorella sorokiniana and provide a target for genetic engineering to improve D-xylose utilization for microalgal lipid production |
| 1.1.1.10 | L-xylulose reductase |
synthesis |
potential approach for industrial-scale production of xylitol from hemicellulosic hydrolysate involving the enzyme |
| 1.10.3.2 | laccase |
synthesis |
addition of phenolic and aromatic monomers to growth medium to enhance enzyme production, ferulic acid plus vanillin are most efficient inducers increasing enzyme production up to 10 times |
| 1.10.3.2 | laccase |
synthesis |
Pycnoporus sp. SYBC-L1 is a potential candidate for laccase production |
| 1.10.3.2 | laccase |
synthesis |
owing to their broad substrate range laccases are considered to be versatile biocatalysts which are capable of oxidizing natural and non-natural industrial compounds, with water as sole by-product |
| 1.10.3.2 | laccase |
synthesis |
potential use of the laccase in lignin modification |
| 1.10.3.2 | laccase |
synthesis |
selective biotransformation of aromatic methyl group to aldehyde group in presence of diammonium salt of 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as the mediator |
| 1.10.3.2 | laccase |
synthesis |
the enzyme will serve as a useful tool for enzymatic polymerization of diphenolic compounds such as caffeic acid and ferulic acid |
| 1.10.3.2 | laccase |
synthesis |
synthesis of bioactive 1,4-naphthoquinones. A high yield of naphthoquinones (74.93%) with 1,4-naphthoquinone (60.61%), and its derivative 2-hydroxy-1,4-naphthoquinone (14.32%) is obtained at the optimized reaction conditions |
| 1.10.3.2 | laccase |
synthesis |
synthesis of the C-N polydye at basic pHs |
| 1.10.3.2 | laccase |
synthesis |
the enzyme from Crinipellis sp. synthesizes oxaflavins for redox co-enzymes |
| 1.10.3.2 | laccase |
synthesis |
the enzyme from Pycnoporus cinnabarinus synthesizes 1. benzofuropyroles, which are potent pharmaceutical agents, 2. the pharmaceutical agent 6,7-dihydroxy-2,2-dimethyl-1,3,9-trioxa-fluoren-4-one |
| 1.10.3.2 | laccase |
synthesis |
the enzyme from Trametes hirsute synthesizes polyanniline |
| 1.10.3.2 | laccase |
synthesis |
the enzyme from Trametes versicolor synthesizes 1. polycatechol, a valuable polymer used as a chromatographic resin and in the formation of thin films for biosensors, 2. benzofuranones for medicinal chemistry, 3. poly allylamine with high antioxidant potential, 4. dyes used in hair dyeing, 5. benzoquinones used as intermediates in pharmaceuticals, 6. phenazine and phenoxazinone chromopheres for synthetic dyes |
| 1.10.3.2 | laccase |
synthesis |
the enzyme from Trametes villosa synthesizes benzofurans with antimicrobial and anti-inflammatory activities |
| 1.10.3.2 | laccase |
synthesis |
the enzyme from Ustilago maydis synthesizes polymers of quercitin and kampferol with improved antioxidant properties of the polymers compared to the monomers |
| 1.1.1.77 | lactaldehyde reductase |
synthesis |
fermentation of L-rhamnose, L-fucose and D-fucose to a mixture of 1,2-propanediol, acetone, H2, CO2 and ethanol |
| 3.2.1.140 | lacto-N-biosidase |
synthesis |
synthesis of Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc, i.e. lacto-neotetraose |
| 3.4.21.96 | Lactocepin |
synthesis |
optimisation of enzymatic hydrolysis of beta-casein to produce the angiotensin-I-converting enzyme (ACE) inhibitory peptides. Under optimal conditions (enzyme-to-substrate ([E]/[S]) ratio (w/w) of 0.132 and pH of 8.00 at 38.8°C), the ACE inhibitory activity of hydrolysates is 72.06% and the total peptides is 11.75 mg/ml. The resulting hydrolysates have higher thermal stability than beta-casein and show an increase in the free sulfhydryl content compared with raw beta-casein |
| 5.4.99.7 | Lanosterol synthase |
synthesis |
engineering ERG7 for producing biological active agents is promising |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
synthesis of L-selenomethionine from 2-oxo-4-methylselenobutanoate |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
conversion of ammonia or urea into essential amino acids, L-Leu, L-Val, and L-Ile, using artificial cells containing an immobilized multienzyme system that consists of EC 1.1.1.1, EC 1.4.1.9, EC 3.5.1.5 and dextran-NAD+ |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
production of L-Leu, L-Val and L-Ile by artificial cells containing a glucose dehydrogenase and leucine dehydrogenase |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
preparation of (S)-1-cyclopropyl-2-methoxyethanamine, a key chiral intermediate for the synthesis of a corticotropin releasing factor-1 (CRF-1) receptor antagonist, by a chemoenzymatic route using leucine dehydrogenase. Synthesis of (S)-1-cyclopropyl-2-methoxyethanamine starting from methylcyclopropyl ketone. Permanganate oxidation of the ketone gives cyclopropylglyoxylic acid, which is converted to (S)-cyclopropylglycine by reductive amination using leucine dehydrogenase from Thermoactinomyces intermedius, recombinantly expressed in Escherichia coli, with NADH cofactor recycling by formate dehydrogenase from Pichia pastoris |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
coexpression with Bacillus megaterium glucose dehydrogenase in Escherichia coli for the production of L-tert-leucine. A decagram preparation of L-tert-leucine is performed at a substrate concentration of 0.6 M in 1 l scale with 99% conversion after 5.5 h, resulting in 80.1% yield and > 99% enantiomeric excess |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
coexpression with NAD+-dependent FDH from Candida boidinii in Escherichia coli for synthesis of L-tert-leucine. In a continuous feeding process, at an overall substrate concentration up to 1.5 M, both conversion and enantiomeric excess of >99% and space-time yield of 786 g/l/d are achieved |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
formation of a bifunctional enzyme complex consisting of leucine dehydrogenase (LDH) and formate dehydrogenase from Candida boidinii via a miniscaffoldin for production of L-tert-leucine. Ninety-one grams of L-tert-leucine per liter with an enantiomeric purity of 99% e.e. can be obtained |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
high-throughput screening method for L-tert-leucine synthesis and directed evolution strategy to engineer LeuDH for improved efficiency of L-tert-leucine synthesis |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
production of L-2-aminobutanoate from L-threonine via overexpression of L-threonine deaminase from Escherichia coli, L-leucine dehydrogenase from Bacillus cereus, and formate dehydrogenase from Pseudomonas sp. in Escherichia coli with formate as a cosubstrate for NADH regeneration. 30 mol L-threonine are converted to 29.2 mol L-2-aminobutanoate with 97.3 % theoretical yield and with a productivity of 6.37 g/l/h at 50 l |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
enzyme cascade from threonine to synthesis of L-2-aminobutanoate. In this cascade, the threonine deaminase is used for threonine to 2-oxobutanoate, then LeuDH mutant and formate dehydrogenase are used for synthesis of L-2-aminobutanoate. Under optimized conditions, 1 M threonine is catalyzed by whole cells of Escherichia coli harboring the enzymes in 12 h in sodium phosphate buffer to the optically pure L-2-aminobutanoate with a yield of 99% and ee above 99% |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
enzyme coupled with recombinant formate dehydrogenase is used to catalyze trimethylpyruvic acid through reductive amination to generate enantiopure L-tert-leucine. Using a fed-batch feeding strategy, up to 0.8 M of trimethylpyruvate is transformed to L-tert-leucine, with an average conversion rate of 81% and L-tert-leucine concentration of 65.6 g/l |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
in Escherichia coli expressing IvlA, mutant K72A, formate dehydrogenase, under optimized conditions 150 g L-threonine is transformed to 121 g L-2-aminobutanoate in 5 l fermenter with 95% molar conversion rate, and a productivity of 5.04 g/l and h |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
production of L-tert-leucine by a fusion enzyme of leucine dehydrogenase and glucose dehydrogenase with a rigid peptide linker (GDH-R3-LeuDH). Compared with the free enzymes, both the environmental tolerance and thermal stability of GDH-R3-LeuDH is improved. The fusion structure accelerates the cofactor regeneration rate and maintains the enzyme activity. The space-time yield of L-tert-leucine synthesis by GDH-R3-LeuDH whole cells is up to 2136 g/l/day in a 200 ml scale system under the optimal conditions (pH 9.0, 30°C, 0.4 mM of NAD+ and 500 mM of substrate including trimethylpyruvic acid and glucose) |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
production of L-tert-leucine. A coupled reaction comprising LeuDH with glucose dehydrogenase of Bacillus amyloliquefaciens results in substrate inhibition at high trimethylpyruvate concentrations (0.5 M), which is overcome by batch-feeding of the substrate. The total turnover number and specific space-time conversion of 0.57 M substrate increases to 11400 and 22.8 mmol per h and l and g, respectively |
| 1.4.1.9 | leucine dehydrogenase |
synthesis |
production of L-valine in Escherichia coli on the base of the aminotransferase B-deficient strain V1 by introducing one chromosomal copy of the Bcd gene or the IlvE gene. The Bcd-possessing strain exhibits 2.2fold higher L-valine accumulation (up to 9.1 g/l) and 2.0fold higher yield (up to 35.3%) under microaerobic conditions than the IlvE-possessing strain |
| 3.4.11.1 | leucyl aminopeptidase |
synthesis |
production of polyketide antibiotics |
| 3.4.11.1 | leucyl aminopeptidase |
synthesis |
production of alpha-amino acids, which are intermediates in the synthesis of antibiotics, injectables, food and feed additives |
| 4.2.2.16 | levan fructotransferase (DFA-IV-forming) |
synthesis |
synthesis of di-D-fructose-2,6':2',6 dianhydride |
| 4.2.2.16 | levan fructotransferase (DFA-IV-forming) |
synthesis |
development of a di-D-fructofranosyl-2,6':2',6-anhydride production system with single culture of Bacillus subtilis directly from sucrose. This system can avoid the purification procedure of levan in which organic solvent is used for precipitation. The levan fructotransferase gene is cloned from Arthrobacter nicotinovorans GS-9 and expressed in levan producing Bacillus subtilis 168. LFTase activity is detected in the culture supernatant of the transformant with maximal activity of 0.062 U/ml after 15.5 h post induction. Then sucrose is added as substrate and incubated. About 78 h after addition of sucrose, 20.5 g/l of di-D-fructofranosyl-2,6':2',6-anhydride is produced from 139.3 g/l of sucrose consumed. The yield of di-D-fructofranosyl-2,6':2',6-anhydride from sucrose is 14.7 wt.% |
| 4.2.2.16 | levan fructotransferase (DFA-IV-forming) |
synthesis |
enzymatic production of ascorbic acid 2-fructoside, that can be applied to cosmetics, food products, and pharmaceuticals |
| 3.2.1.65 | levanase |
synthesis |
protection from aging |
| 3.2.1.65 | levanase |
synthesis |
paper industry |
| 3.2.1.65 | levanase |
synthesis |
synthesis of various products such as ethanol or aceton-butanol |
| 3.2.1.65 | levanase |
synthesis |
commercial production of ultra-high-fructose syrups |
| 3.2.1.65 | levanase |
synthesis |
the enzyme is used for simultaneous saccharification and fermentation of inulin to 2,3-butanediol. A fed-batch simultaneous saccharification and fermentation yields 103.0 g/liter 2,3-butanediol in 30 h, with a high productivity of 3.4 g/liter/h |
| 3.2.1.65 | levanase |
synthesis |
the enzyme is uzilized for production of beta2-6 fructose oligosaccharides (levan-type FOS) through a sequential reactionwith levan produced from sucrose by bacterial levansucrases, method development, overview |
| 2.4.1.10 | levansucrase |
synthesis |
immobilization of recombinant free levansucrase on magnetite leads to production of low molecular weight levan, increased thermal stability of the enzyme |
| 2.4.1.10 | levansucrase |
synthesis |
enzyme is an important biocatalyst for production of fructose homopolymers, potential usage in bioindustrial fields |
| 2.4.1.10 | levansucrase |
synthesis |
production of the artificial sweetener, lactosucrose |
| 2.4.1.10 | levansucrase |
synthesis |
D-glucose acts as an inhibitor of the transfructosylation reaction, Candida cacaoi selectively removes glucose from the reaction medium, the decrease of glucose concentration by yeast in the medium by 16-19% results in the increased degree of levan polymerisation (by 6 to 9%) and efficiency of levan synthesis (by 9 to 11%) |
| 2.4.1.10 | levansucrase |
synthesis |
the enzyme is useful in levan production for application in the food and pharmaceutical industry |
| 2.4.1.10 | levansucrase |
synthesis |
levansucrase Lsc3 of Pseudomonas syringae pv. tomato has very high catalytic activity and stability making it a promising biotechnological catalyst for FOS and levan synthesis |
| 2.4.1.10 | levansucrase |
synthesis |
the enzyme is interesting for levan production due to its ability to directly use the free energy of cleavage of non-activated sucrose to transfer the fructosyl group to a variety of acceptors including monosaccharides (exchange), oligosaccharides (fructooligosaccharides synthesis) or a growing fructan chain (polymer synthesis). Levansucrase from Bacillus amyloliquefaciens is a promising biocatalyst for the synthesis of beta-(2-6)-linked-fructose-based carbohydrates (fructooligosaccharides, oligolevans, levans) targeting specific structures and functional properties |
| 4.2.3.32 | levopimaradiene synthase |
synthesis |
increase of levopimaradiene synthesis in Escherichia coli by amplification of the flux toward isopentenyl diphosphate and dimethylallyl diphosphate precursors and reprogramming the rate-limiting downstream pathway by generating combinatorial mutations in geranylgeranyl diphosphate synthase and levopimaradiene synthase. The most productive pathway, combining precursor flux amplification and mutant synthases, confers approximately 2600fold increase in levopimaradiene levels. A maximum titer of approximately 700 mg/l is obtained by cultivation in a benchscale bioreactor |
| 4.2.3.32 | levopimaradiene synthase |
synthesis |
the development of yeast strains carrying the engineered Erg20p, which support efficient isoprenoid production, e.g. by abietadiene synthase, and can be used as a dedicated chassis for diterpene production or biosynthetic pathway elucidation. The design developed can be applied to the production of any GGPP-derived isoprenoid and is compatible with other yeast terpene production platforms, method overview |
| 3.2.1.73 | licheninase |
synthesis |
the unusually resistance against inactivation by heat, ethanol or ionic detergents makes the enzyme highly suitable for industrial application in the mashing process of beer brewing |
| 3.2.1.73 | licheninase |
synthesis |
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% |
| 3.2.1.73 | licheninase |
synthesis |
over-expression in Pichia pastoris, with a yield of about 1000 U/ml in a 3.7 l fermentor |
| 3.2.1.73 | licheninase |
synthesis |
upon expression in Pichia pastoirs as active extracellular beta-1,3-1,4-glucanase, the recombinant protein is secreted predominantly into the medium and comprises up to 85% of the total extracellular proteins and reaches a protein concentration of 9.1 g/l with an activity of 55,300 U/ml in 5-l fermentor culture |
| 3.2.1.73 | licheninase |
synthesis |
analysis of fermentation conditions for beta-1,3-1,4-glucanase production under solid-state fermentation. Under the optimized fermentation conditions, viz. oatmeal as sole carbon source, 5% (w/w) peptone as sole nitrogen source, initial moisture of 80% (w/w), initial culture pH of 5.0, incubation temperature of 50°C and incubation time of 6 days, the highest beta-1,3-1,4-glucanase activity of 20025 U/g dry substrate is achieved. The addition of the purified beta-1,3-1,4-glucanase in mash obviously reduces its filtration time (24.6%) and viscosity (2.61%) |
| 3.2.1.73 | licheninase |
synthesis |
expression of mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in Bacillus subtilis to maximal extracellular activity of 4840.4 U/ml |
| 3.2.1.73 | licheninase |
synthesis |
immobilization of enzyme on porous silica using glutaraldehyde. Enzyme activity decreases sharply at high concentrations of glutaraldehyde. Immobilized protein is stable over a wide range of pH and can be stored long term at 4°C. After 10 cycles, the enzyme retains 42% of its initial catalytic activity |
| 3.2.1.73 | licheninase |
synthesis |
the enzyme can be used in the production of anti-hypercholesterolemic agents |
| 1.11.1.14 | lignin peroxidase |
synthesis |
evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control |
| 1.11.1.14 | lignin peroxidase |
synthesis |
immobilization of enzyme by entrapping in xerogel matrix of trimethoxysilane and proplytetramethoxysilane to maximum immobilization efficiency of 88.6%. The free and immobilized enzymes have optimum pH values of 6 and 5 while optimum temperatures are 60°C and 80°C, respectively. Immobilization enhances the activity and thermo-stability potential significantly and immobilized enzyme remains stable over broad pH and temperature range |
