195 results about "Aminopeptidase" patented technology

A gram-negative bacterial cell is described that is deficient in a chromosomal gene present in a wild-type such cell which gene shares at least 80% sequence identity with the native sequence of the yfcK gene and encodes an aminopeptidase. Alternatively, a gram-negative bacterial cell is deficient in a chromosomal gene present in a wild-type such cell which gene encodes an aminopeptidase that shares at least 80% sequence identity with the native sequence of aminopeptidase b2324. Either of these types of cells, when comprising a nucleic acid encoding a heterologous polypeptide, produces an N-terminal unclipped polypeptide when it is cultured and the polypeptide recovered, with virtually no N-terminal clipped polypeptide produced as an impurity. Conversely, a method is provided for cleaving an N-terminal amino acid from a polypeptide comprising contacting the polypeptide with an aminopeptidase sharing at least 80% sequence identity with the native sequence of aminopeptidase b2324.

The invention discloses a method for preparing and extracting Bacillus subtilis debittering aminopeptidase by fermentation, which belongs to the technical field of enzyme preparation and food additive. The invention uses the fermentation cylinder production condition of Bacillus subtilis Zj016 to collect fermentation liquor and obtain the product of debittering aminopeptidase by carrying out clarifying, ultrafiltration concentration and salting out on the fermentation liquor. The aminopeptidase produced by the selected Bacillus subtilis Zj016 is exopeptidase which can dissociate amino acid from a polypeptide chain amino terminal. Researched by the laboratory, the aminopeptidase cooperates with alkali protease to hydrolyze soybean protein isolate; the prepared soybean peptide does not have bitterness, and the contents of oligopeptide like dipeptide and tripeptide are higher. Besides, researches on the enzyme lines produced by the Bacillus subtilis show that the Bacillus subtilis only produces circumscribed prolease and does not have the activity of endo protease; moreover, the circumscribed prolease has a stronger hydrolysis capacity to the terminal amino acid with strong hydrophobicity. The research further explains that the invention can reduce or eliminate the bitterness generated during hydrolysis of the soybean protein.

The invention provides aminopeptidase for catalytic synthesis of carnosine, and a preparation method and application thereof. The aminopeptidase has the amino acid sequence shown by SEQ ID NO:2. For the preparation of biological enzymes, firstly, a gene engineering strain of the biological enzymes is built; the biological enzyme gene fragment obtained through full gene synthesis is subjected to linearized plasmid recombination by using restriction enzymes SalI. The built gene-engineered strain is suitable for high-density culture; the exoenzyme is biologically synthesized; solid-liquid separation is performed; ultrafiltration concentration is performed to obtain enzyme liquid; histidine and beta-alanine can be catalyzed in normal-temperature and normal-pressure water solution to efficiently synthesize carnosine; the reaction environment is friendly; the production cost is low; the conversion time is short; the process operation is simple; the reaction system impurity content is low; the post treatment is easy; the wide prospects of large-scale industrial application are realized.

The invention discloses a lactobacillus plantarum (LP-ONLLY) and the application thereof in active fermented milk. The LP-ONLLY is preserved in China General Microbiological Culture Collection Center on December 6, 2004, and the preservation register number is CGMCC NO.1258. The LP-ONLLY has the high aminopeptidase activity, high beta-galactosidase activity and high glucosidase activity, and frozen and dried living bacterium powder is used as an independent leavening agent which can be applied for preparation of the active fermented milk. The active fermented milk contains the high probiotics live bacteria, the live bacteria have the high stability and can supplement probiotics, and the health function of the LP-ONLLY is achieved.

The invention relates to the technical field of deep processing of pigskin, particularly relates to a method for extracting pigskin collagen peptide. The method uses fresh pigskin to serve as a raw material, and a pure biology method is used for obtaining the pigskin collagen peptide. The method for extracting low molecular weight active collagen peptide from the pigskin comprises the following steps of: taking the fresh pigskin to serve as the raw material, firstly conducting outer cutting on collagen in the pigskin by adopting aminopeptidase and carboxypeptidase; separating the collagen from other tissue elements in the pigskin, then the pigskin is in a scattered state, and using endo protease to conduct enzymolysis on protein to enable the protein to form micromolecular protein peptides. Different protein peptides are scientifically selected in different stages, processing steps are optimized, production efficiency is improved, yield of the collagen peptide is promoted, and activity of the collagen peptide is improved.

The invention relates to a method for preparing leucine aminopeptidase through the fermentation of bacillus subtilis engineering bacteria, belonging to the technical field of enzymic preparations and food additives. The method is characterized in that the enzyme powder of the leucine aminopeptidase is obtained by using the fermentation production of the bacillus subtilis engineering bacteria and carrying out extraction operations such as flocculation, filtration sterilization, ultrafiltration and concentration, and freeze drying on fermentation liquor, and the basic enzymology characteristics of the prepared leucine aminopeptidase are studied. According to the method, the bacillus subtilis engineering bacteria PMA5-SAP for the high yield of the leucine aminopeptidase, which is structured on the basis of the wild bacillus subtilis engineering bacteria zj016, is further optimized in the fermentation process, the enzyme activity of the leucine aminopeptidase produced in a 7L-fermentation tank is substantially increased by adopting strategies such as the pretreatment of a culture medium, the adjustment of culture medium components, the control of dissolved oxygen level and the like, and the level of enzymes produced through fermentation is increased from 7000U/L (unit for enzyme activity) to about 200000U/L.

The invention provides an intensive antitumor medicament, namely bestatin deanol ester, a preparation method and application thereof. The bestatin deanol ester not only can effectively inhibit ectopic expression of aminopeptidase N activity, but also greatly improve the water solubility of the parent drug bestatin of the bestatin deanol ester, has slow release effect, is more excellent than the parent drug bestatin either from healing effect or preparation, and has wide application. Particularly, the invention mainly relates to the following three aspects: (1) design and synthesis of the bestatin deanol ester; (2) N'N deanol which is a micromolecule fragment, can be connected with other medicaments containing carboxyl, improves the pharmacokinetic property of the medicaments, and improves water solubility; and (3) a method for synthesizing an ester substance to which the invention relates with wide application and mild condition.

Peptide inhibitors of dipeptidyl-aminopeptidase type IV (DP-IV) are provided. The peptide inhibitors have an isomeric purity of about 96–99 percent. The peptide inhibitors include one or more amino acids covalently coupled to boroproline moiety. The compounds are useful as DP-IV inhibitors, in vivo and in vitro.

The invention relates to an antibacterial and antiviral mask and a preparation method thereof. The antibacterial and antiviral mask sequentially comprises an antibacterial layer, a bacteria dissolvinglayer and an antiviral layer from outside to inside, wherein the antiviral layer comprises aminopeptidase, and the aminopeptidase is derived from streptomyces nitro. According to the antibacterial and antiviral mask, aminopeptidase from streptomyces nitro is selected as an antiviral agent, so that the antibacterial and antiviral mask has the advantages of being high in antiviral property, safe and environmentally friendly; the antibacterial and antiviral mask has lasting antibacterial and antiviral capacity, the antibacterial and antiviral effects are thorough, and secondary infection of bacteria and viruses is effectively avoided; and the preparation method of the antibacterial and antiviral mask has the advantages of simplicity in operation, low cost, easiness in implementation, environmental friendliness and the like.

The invention relates to the technical field of food processing and microbial fermentation, in particular to aspergillus oryzae ZA184 and use thereof in soy sauce brewing. The aspergillus oryzae ZA184can increase the pH of koji, enhance the activity of the koji enzymes (such as neutral protease, alkaline protease, leucine aminopeptidase and glutaminase), and improve the contents of amino nitrogen, total nitrogen and glutamic acid in soy sauce, so that the flavor and quality of the soy sauce is improved, the fermentation cycle can be significantly shortened, and the production efficiency is improved.

The invention relates to novel compounds of formula (I): H2N-CH(R1)-CH2-S-S- CH2-CH(R2)-CONH-R5, wherein R1 is a hydrocarbon chain, phenyl or benzyl radical, methylene radical substituted by a 5 or 6 atom heterocycle; R2 is a phenyl or benzyl radical, a 5 or 6 atom aromatic heterocycle, methylene group substituted by a 5 or 6 atom heterocycle; R5 is a CH(R3)-COOR4 radical, wherein R3 is hydrogen, an OH or OR group, a saturated hydrocarbon group, a phenyl or benzyl radical and OR4 is hydrophile ester, or 5 or 6 membered heterocycle comprising several heteroatoms selected from a group consisting of nitrogen, sulphur and oxygen, with at least two nitrogene atoms, wherein said heterocycle is substitutable by an alkyl C1-C6, phenyl or benzyl radical.; The use of the inventive compounds in the form of drugs, a pharmaceutical composition comprising said compounds, a pharmaceutically acceptable excipient, the use in conjunction of at least one type of cannabinoid derivative for potentiating the analgesic and antidepressant effect of the novel compounds of formula (I) and/or morphine or the derivatives thereof are also disclosed.

Disclosed herein are fungal nucleic acid sequences that encode novel polypeptides. Also disclosed are polypeptides encoded by these nucleic acid sequences, as well as derivatives, variants, mutants, or fragments of the aforementioned polypeptide, polynucleotide, or antibody. The novel leucine aminopeptidase (LAP) and other amino- and carboxypeptidases polypeptides, referred to herein as EXOX nucleic acids and proteins of the invention are useful in a variety of medical, research, and commercial applications.

The invention relates to bacillus subtilis DFS01 and application thereof. The collection number of the strain is CDMCC NO. 60294. Compared with the existing known bacillus subtilis strain, the bacillus subtilis DFS01 is remarkably characterized in that (1) the strain has high enzyme production activity, the produced proteases comprise keratinase, carboxypeptidase and aminopeptidase which can withstand the temperature of 100 DEG C compared with proteases produced by ordinary bacillus subtilis strains, the content of bitter peptides produced by decomposing the proteases is low, and a fermentation product has very strong flavor and very high livestock palatability; (2) the strain has the characteristic of high intestinal cell adhesion capability, and the adhesion rate is up to 62.78 percent.

The invention discloses a method for improving the stability of liquid aminopeptidase and an application of the aminopeptidase, which belong to the technical field of enzymic preparations and food additives. The invention relates to an extracting process of bacillus subtilis Zj016 liquid aminopeptidase to improve the stability of the liquid aminopeptidase and an application of the aminopeptidase in deep hydrolysis of soy isolated protein. The bacillus subtilis Zj016 liquid aminopeptidase is centrifuged, clarified, concentrated, desalinized, deposited by alcohol and redissolved to obtain the liquid aminopeptidase; the liquid aminopeptidase can keep stable by controlling the pH condition and/or the additive; the aminopeptidase can carry out deep hydrolysis on a substrate of the soy isolated protein to generate a small peptide and amino acid with higher content and has a combined application potential with a plurality of incision enzymes, thereby having wide application prospect in food processing of protein raw materials.

The invention provides mature peptide of a myotis brandti leukotriene A4 hydrolase inhibitor Motistin and an application of the mature peptide, and belongs to the technical field of biological medicine. The amino acid sequence of the mature peptide is shown as SEQ ID NO: 2. The invention discovers for the first time that the mature peptide of Motistin can inhibit the hydrolase activity of LTA4H without affecting the aminopeptidase activity of LTA4H. The mature peptide of Motistin can target LT44H, can inhibit the recruitment of immune cells and the generation of inflammatory mediators by inhibiting the hydrolase activity of LTA4H, and also has the function of inhibiting the generation of inflammatory cytokines IL6, TNF <alpha> and IL1<beta> caused by virus and bacterial lipopolysaccharide.The mature peptide has the potential of becoming an effective drug for inhibiting inflammation.

The invention belongs to the field of biochemical engineering, and particularly relates to a preparation method and an application of a near-infrared fluorescent molecular probe NF-O-Leu for detectingleucine aminopeptidase (LAP). The structural general formula of the compound NF-O-Leu is as shown in the specification, R1, R2, R3, R4, R5 and R6 are introduced substituent groups and can be used foradjusting electronic effects of the fluorescent probe, so that fluorescence of the fluorescent probe is changed. According to the near-infrared fluorescent molecular probe NF-O-Leu, near-infrared fluorescent dyes NF-OH and LAP receptor units (leucine residues) are bridged together by para-aminobenzoic acid (PABA), the target near-infrared fluorescent molecular probe NF-O-Leu is synthesized and used for specifically monitoring LAP activity in vitro and in vivo, and trace LAP in living cells is successfully tracked and detected.