8 results about "Cold adapted" patented technology

The invention discloses exo-type alginate lyase VsAly7C as well as a recombinant strain and application of the exo-type alginate lyase VsAly7C. The amino acid sequence of the exo-alginate lyase is as shown in SEQ ID No.4, and the nucleotide sequence for coding the amino acid sequence is as shown in SEQ ID No.1. The suitable reaction temperature of the exo-alginate lyase is 24-28 DEG C, and the exo-alginate lyase has high stability at 0-20 DEG C, so that the exo-alginate lyase can effectively degrade a substrate at low temperature, and belongs to cold-adapted alginate lyase. The exo-type alginate lyase has the capability of degrading alginate, polyG and polyM, the degradation mode is exo-type, and a final degradation product is unsaturated alginate trisaccharide and has NaCl dependence. The invention further constructs a recombinant vector and a recombinant thallus containing the exo-alginate lyase VsAly7C coding gene, and a good foundation can be provided for industrial application and production of unsaturated alginate oligosaccharides.

The invention discloses an influenza A virus Vero cell cold adapted strain Vca-CPD and application thereof, and relates to the field of biotechnology and vaccinology. The preservation number of the Vca-CPD provided by the invention is CCTCC (China Center For Type Culture Collection) NO: V202585. The strain is mainly obtained by performing codon pair optimization on PB2, PA and NP genes. In-vivo and in-vitro experiments prove that the replication ability of the strain in human cells and mammal models is obviously weakened, and the safety is improved; meanwhile, an organism can be induced to generate high-level and specific serum protective antibodies and respiratory mucosa sIgA antibodies. In addition, the virus yield of the strain in production of stromal cells is equivalent to that of a parent strain, and the strain shows good production applicability.

The invention provides a composite biological enzyme ceramic odor removal block for a refrigerator and a preparation method of the composite biological enzyme ceramic odor removal block. The composite biological enzyme ceramic odor removal block for the refrigerator comprises a porous ceramic carrier and a composite biological enzyme loaded on the porous ceramic carrier, the composite biological enzyme is prepared from a composite biological enzyme stock solution, lipase, protease and formaldehyde dehydrogenase according to a mass ratio of 4: 3: (1-2), and the composite biological enzyme comprises cold-adapted oxidoreductase, low-temperature chitinase and mycose; the surface of the porous ceramic carrier is modified by a silane coupling agent, and the interior of the porous ceramic carrier has gradient pore size distribution of 10-0.1 mu m. Through the synergistic effect of the biological enzyme compound system and the ceramic carrier, efficient mineralization decomposition of peculiar smell molecules is achieved, meanwhile, the safety standard of food contact materials is met, and the problems of low-temperature inactivation, secondary pollution and frequent replacement in the prior art are solved.

This invention discloses a method for screening thermosensitive UDG rational mutation sites based on strain culture temperature. The method first divides strains into heat-tolerant and cold-adapted groups according to temperature thresholds based on the culture temperature of the strain preservation database, constructing corresponding UDG sequence sets and three-dimensional structure sets. Then, a first candidate mutation site set is generated through multiple sequence alignment and amino acid distribution difference analysis. A second candidate mutation site set is generated through rigid body alignment and functional protection rules under a unified coordinate system. Finally, multiple-source indicators such as structural dispersion, contact and salt bridge networks, and kinetic coupling are calculated for the second candidate mutation site set. Combined with effect-safety dual-dimensional scoring, spatial clustering, and cross-validation of the first candidate mutation site set, a preferred mutation site set is output. This invention achieves a systematic transformation from temperature ecotags to engineered sites, improving the reproducibility and interpretability of site screening without requiring a large-scale mutation library.

This invention discloses the application of the OsCAX1a gene in the breeding of cold-adapted rice varieties, belonging to the field of plant genetic engineering. The amino acid sequences of the two different spliceosome translation proteins encoded by the OsCAX1a gene are shown in SEQ ID NO.1 and SEQ ID NO.2, respectively, and the CDS sequences are shown in SEQ ID NO.3 and SEQ ID NO.4, respectively. This invention reveals that OsCAX1a is a negative regulator of rice cold stress adaptation. Knocking out the OsCAX1a gene inhibits rice growth and development in the early stages, but as the heading stage lengthens and the plant enters the low-temperature growth period, the mutant exhibits significantly better cold adaptation, ultimately manifested in an increased number of tillers and increased grain yield per plant. By selecting varieties with low expression levels of this gene or by mutating the gene through gene editing, superior cold-adapted rice varieties tolerant to low-temperature stress can be cultivated, showing promising application prospects.

This invention discloses a cold-adapted xylose isomerase mutant, its preparation method, and its applications. Compared to the amino acid sequence of the wild-type xylose isomerase shown in SEQ ID NO: 1, the cold-adapted xylose isomerase mutant has a mutation at position 30, where alanine is replaced with glycine. This invention obtains a cold-adapted xylose isomerase mutant through rational design guided by ΔΔG on a heat-sourced xylose isomerase. This cold-adapted xylose isomerase mutant exhibits significantly enhanced activity at the fermentation temperature of *Saccharomyces cerevisiae*.

The invention discloses an endo-type alginate lyase VsAly7B-CM with high activity as well as a recombinant strain and application of the endo-type alginate lyase VsAly7B-CM. The amino acid sequence of the endo-type alginate lyase is as shown in SEQ ID NO.5, and the nucleotide sequence for coding the amino acid sequence is as shown in SEQ ID NO.4. The invention further discloses a preparation method of the endo-type alginate lyase. The endo-type alginate lyase has a suitable reaction temperature of 20-30 DEG C and good stability at a temperature of 0-30 DEG C, so the endo-type alginate lyase can effectively degrade a substrate at a low temperature and belongs to a cold-adapted alginate lyase. The endo-type alginate lyase has the degradation capacity on alginate, polyG and polyM, the degradation mode is endo-type, and final degradation products are unsaturated disaccharide, trisaccharide, tetrasaccharide and pentasaccharide and have NaCl dependence. The invention further constructs a recombinant vector and a recombinant thallus containing the coding gene of the catalytic structural domain VsAly7B-CM of the incision type alginate lyase VsAly7B, and a good basis can be provided for industrial application and production of alginate oligosaccharide.

The present disclosure provides compositions and methods for manufacturing and obtaining a live attenuated Influenza vaccine (LAIV) composition that can be delivered intranasally to provide protection against influenza virus infection. Said LAIV strains are based on cold adapted, temperature sensitive and attenuated phenotypes of master donor viruses (MDVs) containing the surface glycoprotein genes of the wild type pandemic or seasonal influenza strains. Also, said LAIV strains are further adapted to grow in MDCK cells (Madin Darby canine kidney cells). The use of eggs is avoided in large scale vaccine manufacturing. The purification process is devoid of chromatography steps. The said LAIV composition includes one or more live attenuated influenza vaccine virus and is devoid of polymers and surfactants.