50 results about "Comamonas testosteroni" patented technology

The invention relates to the isolation, sequencing, and recombinant expression of genes encoding either a nitrile hydratase (NHase) or amidase (Am) from Comamonas testosteroni 5-MGAM-4D, where the NHase is useful for catalyzing the hydration of nitriles to the corresponding amides, and the amidase is useful for hydrolysis of amides to the corresponding carboxylic acids. Also provided are transformed host cells containing polynucleotides for expressing the nitrile hydratase or amidase enzymes from Comamonas testosteroni 5-MGAM-4D.

The invention discloses Comamonas testosteroni and application thereof in the synthesizing of 5-hydroxymethyl furoic acid. The Comamonas testosteroni SC1588 is preserved in China Center for Type Culture Collection (CCTCC) on October 13th, 2016, and the preservation number of the Comamonas testosteroni SC1588 is CCTCC No. M2016562. The biological catalyst Comamonas testosteroni SC1588 has the advantages that the Comamonas testosteroni SC1588 has high tolerance to HMF, can catalyze a high-concentration substrate (160mM) to selectively oxidize to synthesize a target product, and yield reaches 98%; high substrate concentration, excellent reaction efficiency and good selectivity are achieved.

A fusion protein of pyrroloquinoline quinone glucose dehydrogenase (PQQGDH) and a cytochrome is disclosed. PQQGDH is, for example, a water-soluble PQQGDH derived from Acinetobacter calcoaceticus. The cytochrome is, for example, an electron transfer domain of quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. The fusion protein of the present invention shows intramolecular electron transfer from PQQ, a redox center, to the cytochrome, which allow construction of a direct electron transfer-type glucose sensor which requires no electron mediators.

The invention discloses a biological modification method of dacron fabrics, mainly comprising the following steps: 1. culturing strains: culturing Comamonas testosteroni in a agarslant solid culture medium for 12-18h under the temperature of 30-37 DEG C, and storing in a refrigerator at the temperature of 4 DEG C; 2. preparing a dacron modified liquid: preparing 6 parts of dacron modified liquid with the terephthalic acid concentration of 1-3g / L (each part is 150ml), respectively filling in a conical flask, and packing and sterilizing for 25min under the temperature of 121 DEG C; 3. modifyingthe dacron fabrics: performing ultraviolet sterilization for 0.5h on 6 parts of dacron fabrics, implanting the Comamonas testosteroni in 3 parts of dacron modified solutions, adding 3 parts of dacronfabrics into the 3 parts of dacron modified liquid respectively, taking the other three parts of dacron fabrics as a reference, performing shake cultivation at the temperature of 30-37 DEG C and withthe revolving speed of 200r / min, and performing catalytic modification on the dacron fabrics; and 4) flushing the fabrics by tap water trickles and distilled water in turn, cleaning the fabrics by ultrasonic and airing.

The invention relates to a method for producing L-alanine by bioconverting L-aspartic acid by a free cell process, which comprises the following steps: bioconverting L-aspartic acid with Comamonas testosteroni HY-08D of self-screened high-yield L-aspartate-beta-decarboxylase (EC 4.1.1.12, ASD or ADL) to produce L-alanine; and filtering, concentrating, crystallizing and drying to obtain the finished L-alanine product. The invention can enhance the production efficiency of L-alanine and lower the production cost.

The present invention relates to one p-nitrobenzene chloride ring opening enzyme gene and its expression product. The gene is from Comamonas testosteroni CNB1 CGMCC No. 1028 strain, has size of 1770 bp, and contains two ORF opening read frames in the same direction of 942 bp and 813 bp separately, separated by 15 bp, coding two different protein products beta-subunit and alpha-subunit. Two beta-subunits and two alpha-subunits constitute one active enzyme molecule. The enzyme can catalyze the ring opening cracking in the 1 and the 6 place of 2-amino phenol and the direct ring opening cracking of p-nitrobenzene chloride. Therefore, the gene may be used in constituting gene engineering bacterian and produce active enzyme for treating sewage containing p-nitrobenzene chloride and similar compound and in biological conversion engineering.