30 results about "Levanase activity" patented technology

Isolated polynucleotides encoding polypeptides having the activity of enzymes in the mevalonate pathway are provided. These sequences are useful for recombinantly producing isoprenoid compounds, such as carotenoids, in particular zeaxanthin. Expression vectors, cultured cells, and methods of making isoprenoid compounds are also provided.

The present invention relates to a novel polypeptide having the enzymatic activity of conversion of methylglyoxal to lactic acid in a single step (known as glyoxalase III activity), a polynucleotide having a nucleotide sequence encoding such polypeptide and uses thereof.The invention relates to the modulation of the glyoxalase III activity in a microorganism by varying the expression level of the polynucleotide coding for such polypeptide.The invention also relates to the production of commodity chemicals, especially 1,2-propanediol, acetol, and lactic acid by fermenting microorganisms wherein their glyoxalase III activity is modulated.

A preparation method conducive to enhancing enzymatic activity of cellulase includes the steps of preparing a first inducer, preparing preculture hyphae, producing enzymes by a single strain, feeding a second inducer, and producing enzymes by co-culture strains. Main ingredients of the first inducer and the second inducer are cellulose and lactose, respectively. The enzymatic activity of the cellulase produced is enhanced by induction of cellulose and lactose and co-culture of Trichoderma and Aspergillus.

This invention discloses a kind of method of producing genetic engineering immobilized enzyme N-glycoamidase (PNGase). The N-glycoamidase is fused with yeast agglutination factor by the genetic engineering technique, Anchor it to the surface of methanol nutrition type yeast cell and get a kind of immobilized N-glycoamidase using cells as carrier. In this method, the activity of the enzyme during immobilizing process will not decrease. The produced immobilized enzymes have high stability and can use repeatedly. The method also leaves out purification and reduces the cost. The N-glycoamidase can be widely used in extracting oligosaccharide chain which has biological function from farm product remains (egg yolk powder, milk)

The invention discloses an application of a novel fructosidase coding gene. Fructosidase has the amino acid sequence shown as SEQ.ID NO:1 in a sequence table. The coding gene has the nucleotide sequence shown as SEQ.ID NO:2 in the sequence table. The fructosidase originates from Lactobacillus plantarum, compared with fructosidase originating from other sources, the enzyme has the enzymatic activity of decomposing FOS (fructooligosaccharides) and freeing fructose radicals from the FOS as well as the inulinase activity and levanase activity; lactic acid bacteria without the capability of utilizing the FOS can have the capability of utilizing the FOS when the enzyme is heterogeneously expressed in the other lactic acid bacteria.

Recombinant processes are provided whereby additional genes are introduced into E. coli which have been genetically engineered to produce PHA so that the improved strains produce PHA homopolymers and copolymers directly from diols. In preferred embodiments, PHAs containing 4-hydroxybutyrate monomers are produced directly from 1,4-butanediol; PHAs containing 5-hydroxyvalerate are produced from 1,5-pentanediol; PHAs containing 6-hydroxyhexanoate (6HH) are produced from 1,6-hexanediol; PHAs containing 3-hydroxypropionate are produced from 1,3-propanediol; PHAs containing 2-hydroxypropionate (lactate) are produced from 1,2-propanediol (propylene glycol); PHAs containing 2-hydroxyethanoate (glycolate) are produced from 1,2-ethanediol (ethylene glycol). Genes encoding these same enzyme activities can be introduced or their expression amplified in wild type PHA producers to improve the production of PHA homopolymers and copolymers directly from diol and other alcohol feedstocks. The PHA polymers are readily recovered and industrially useful as polymers or as starting materials for a range of chemical intermediates.

The invention relates to a method for screening and testing activity of a lysine propionylation removal enzyme and a butyrylation removal enzyme. The basis thought of the method is that: lysine propionylation or butyrylation modification degree of a substrate can be reflected by the sensitivity of the substrate to the catalysis removal enzyme. The method comprises the following steps of: a, lysine propionylation substrate polypeptide marked with releasable signal substances; b, the lysine propionylation removal enzyme; and c, a detection method for distinguishing the modification lysine propionylation polypeptide from corresponding non-modification polypeptide. The method can be used for screening modification removal enzymes and testing the activity of the enzymes, and also can screen substrates influencing the activity of the enzymes to be further used in quick diagnosis of several diseases.

The invention relates to thermophilic long-chain alkyl aldehyde dehydrogenase in an n-alkane end degradation process of thermophilic denitrified bacillus and a crystal structure thereof. A molecular clone method is utilized, so that a target gene is cloned into escherichia coli (E. coli) so as to be heterologously expressed. A purified product of aldehyde dehydrogenase is obtained through a protein purification method. A crystal of the aldehyde dehydrogenase, which is suitable for diffraction, is obtained through a hanging droplet crystallization method. The crystal structure of the aldehyde dehydrogenase is analyzed by utilizing an X-ray diffraction method. The results show that the aldehyde dehydrogenase contains a characteristic ALDH fold which is formed by three structural domains. Site-specific mutagenesis is carried out on conserved residues on an enzyme activity part, and the influence of the conserved residues on enzyme activity is proved through wild type of the enzyme and enzyme activity experiment of the mutant thereof. The results can comprehensively reflect space conformation of the enzyme, and provide theoretical guidance for further researching relation between structures and functions of the aldehyde dehydrogenase, and improving the degradation activity of the enzyme.

The invention relates to a method of testing the activity of a potentially active substance to inhibit the enzymatic activity of phospholipase A2. The invention relates notably to a method wherein it comprises a) placing the potentially active substance in the presence with the phospholipase A2; a substrate which is a phospholipid, comprising at least one fatty acid in the form of an ester, the fatty acid is preferably a long chain having between 15 and 22 carbon atoms, this fatty acid preferably being unsaturated or poly-unsaturated, the substrate being capable of releasing at least one fatty acid during its hydrolysis; b) measuring the enzymatic activity of the phospholipase A2, notably comprising detecting the presence of the fatty acid and eventually its quantitative determination. The use of this test method notably enables identifying and selecting an active principle capable of inhibiting the enzymatic activity of phospholipase A2.

Methods of treating mitochondrial fatty acid b-oxidation and / or transport disorders arising from mutant proteins in the mitochondrial fatty acid β-oxidation and transport metabolic pathways in patients are provided. The methods modulate the mitochondrial fatty acid β-oxidation pathway at the last step so that the product of the mutant protein accumulates and stabilizes the mutant protein and / or the substrate(s) / product(s) of the down stream reactions accumulate and possibly bind to allosteric sites on the mutant protein to stabilize it. Trimetazidine pharmacodynamics function as such in the β-oxidation pathway. Further, a synergistic effect is observed where trimetazidine and PPARδ agonist combination enhanced enzyme activity and presence significantly more than either alone.

Recombinant processes are provided whereby additional genes are introduced into E. coli which have been genetically engineered to produce PHA so that the improved strains produce PHA homopolymers and copolymers directly from diols. In preferred embodiments, PHAs containing 4-hydroxybutyrate monomers are produced directly from 1,4-butanediol; PHAs containing 5-hydroxyvalerate are produced from 1,5-pentanediol; PHAs containing 6-hydroxyhexanoate (6HH) are produced from 1,6-hexanediol; PHAs containing 3-hydroxypropionate are produced from 1,3-propanediol; PHAs containing 2-hydroxypropionate (lactate) are produced from 1,2-propanediol (propylene glycol); PHAs containing 2-hydroxyethanoate (glycolate) are produced from 1,2-ethanediol (ethylene glycol). Genes encoding these same enzyme activities can be introduced or their expression amplified in wild type PHA producers to improve the production of PHA homopolymers and copolymers directly from diol and other alcohol feedstocks. The PHA polymers are readily recovered and industrially useful as polymers or as starting materials for a range of chemical intermediates.

It was involved in separating L-amino acid oxidase from the snake venom of Agkistrodonhalysussuriensis. Through two steps of colum chromatography (i.e. heparin fast flow and qsepherose fast flow) L-amino acid oxidase was separated and purified from the snake toxin of Gloydius ussuriensis. Not including transfer between concentrating and buffer system. It could avoid the influence of freezing and the pH value change to enzyme activity. The method was found to be simple, rapid and convenient. The ratio of recovery was high.

The invention relates to a quick detection method of dihydrogen-flavanol4-reductase / leucocyanidin reductase and anthocyanin reductase in tea tree, which can solve the problems of the prior technique of complicated operation in enzymatic activity detection method, high cost, long detection time. The quick detection method comprises: preparing an enzyme extracting-solution, measuring the protein content in enzyme extracting-solution and enzymatic activity, wherein the enzymatic activity is detected by detecting the consumption of the reduction type nicotinamide adenine dinucleotide phosphate solution (NADPH) and the vitamine C is added into the reaction system to reduce the interference of the substrate DHM and CYA on enzymatic activity detection. The quick detection method using ultraviolet spectrophotometer has features of simple method, low cost, short detection time of 15-25 minutes; environmental protection, safety, no need of noxious organic solvent, higher detection accuracy due to continuous detection of the changed enzymatic activity.

The invention relates to a C-type β-glucosidase mutant and its expression plasmid and recombinant bacteria, in particular to a C-type β-glucosidase mutant with significantly improved enzyme activity and a construction method thereof, belonging to biological engineering Technical field; The present invention carries out site-directed mutation on the β-glucosidase derived from Taiwan termites, and changes the lysine K at the 170th position into serine S and tryptophan W respectively, and the phenylalanine F at the 182nd position is methionine M, the amino acid histidine H at the 252nd position becomes asparagine N, and is respectively expressed as Glu1C-K170S, Glu1C-K170W, Glu1C-F182M, Glu1C-H252N; the obtained mutant of the present invention Enzyme activity has improved respectively 5.2 times, 2.05 times, 2.9 times, 2.1 times compared with before mutation; The application of biocatalytic technology provides a favorable basis for industrial application, can better meet the requirements of social production, and has broad market prospects.