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5 results about "Amidase" patented technology

In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide...

A method for producing and extracting N-acetylmuramoyl-L-alanine amidase by microbial fermentation

PendingCN122168580ABacteriaHydrolasesExtracellular proteinsAcetylmuramic acid
This invention relates to the field of microbial technology, specifically to a method for the production and extraction of N-acetylmuroic acid-L-alanine amidase via microbial fermentation. The method for preparing N-acetylmuroic acid-L-alanine amidase provided by this invention utilizes *Clostridium beijerinckii* XH0906 for fermentation to produce N-acetylmuroic acid-L-alanine amidase. As the main extracellular protein of this bacterium, N-acetylmuroic acid-L-alanine amidase has a high yield and is beneficial for subsequent separation and purification. This method has advantages such as simplicity, efficiency, and low cost, providing an effective method for the preparation of N-acetylmuroic acid-L-alanine amidase, and has good application prospects in the fields of microbial food, biomedicine, and antibacterial applications.
Owner:CHINA PETROLEUM & CHEMICAL CORP +2

An amidase mutant and its application in the preparation of (S)-fluopyram aniline

This invention provides an amidase mutant and its application in the preparation of ( S The application of )-fluopyrazopyr in aniline belongs to the fields of genetic engineering and enzyme catalysis technology. Compared with the amidase shown in SEQ ID No. 1, the amidase mutant of this invention has a mutation at position 109 (alanine) to valine and / or position 232 (leucine) to arginine. Compared with the wild-type amidase, the amidase mutant of this invention has a higher optimum temperature and thermal stability, and can catalyze the enzymatic reaction of racemic substrate M-1 (Formula I) in an aqueous phase to generate the key chiral intermediate (…). S )-M-2 (Formula II), further reacted with compound M-3 (Formula III), to efficiently prepare ( S The method for preparing 1-fluopyrazoline is characterized by mild reaction conditions, simple operation, and promising prospects for industrial application.
Owner:ZHEJIANG ACADEMY OF AGRICULTURE SCIENCES

Process for preparing substituted imidazo[1,5-α]pyrazines

Disclosed herein are processes for the preparation of fused heteroaryl dihydro pyrimidine compounds, or salts or stereoisomers thereof, which are useful for the treatment and prophylaxis of hepatitis B virus infections using compounds of formula IX or stereoisomers thereof,wherein a disclosed process comprisesa. reacting a compound formula IIwith hydrogen in the presence of a solvent and a palladium catalyst or a platinum catalyst, to form a compound of formula III:b. reacting the compound of formula III, or a salt or stereoisomer thereof, with a hydrolase selected from the group consisting of an amidase and a peptidase, or a mixture thereof, to form a compound of formula I:or a salt or stereoisomer thereof,c. protecting the compound of formula I, or a salt or stereoisomer thereof, with an amino protecting group (PG) selected from the group consisting of di-tert-butyl dicarbonate (Boc2O) and 2-(tert-butoxycarbonyloxyimino)-2-phenylacetonitrile, to form a compound of formula IV:d. reacting the compound of formula IV, or a salt or stereoisomer thereof, with a compound of the following formula: —R7—NH2 in the presence of a base and the coupling agent, carbonyldiimidazole (CDI), to form a compound of formula V:or a salt or stereoisomer thereof,e. reacting the compound of formula V above, or a salt or stereoisomer thereof, with oxalyl chloride to form a compound of formula VIf. reacting the compound of formula VI above, or a stereoisomer thereof, with a reducing agent selected from the group consisting of BH3·THF and NaBH4, to form a compound of formula VII:g. deprotecting the compound of formula VII above, or a stereoisomer thereof, with concentrated HCl in methyl isobutyl ketone (MIBK), to form a compound of formula IX:
Owner:F HOFFMANN LA ROCHE INC +1

Processes and enzymes for use therein

PCT designated stageWO2026132812A1HydrolasesFermentationPolymer scienceOligomer
The present invention relates to novel amidase enzymes, their use in the hydrolysis of polyamide oligomers and their use in processes for recycling polyamide polymers. The invention finds particular use in the hydrolysis of oligomers of polyamide 6,6 and therefore in processes for the recycling of this polymer.
Owner:EPOCH BIODESIGN LTD

Nutrient-degrading enzyme, engineering bacterial agent and application thereof in nutrient regulation of polymeric slow-release fertilizer

ActiveCN121592626BRetain degradation activityNo antagonistic effectBacteriaMicroorganism based processesBiotechnologyHeterologous
This invention discloses a nutrient-degrading enzyme, engineered microbial agents, and their application in the nutrient regulation of polymeric slow-release fertilizers, belonging to the field of enzyme engineering technology. This invention utilizes a specific polymeric slow-release fertilizer-degrading enzyme modified by artificial intelligence, which not only retains the degradation activity of the source strain enzyme but also achieves efficient heterologous expression while promoting a dual improvement in stability and catalytic efficiency. The constructed composite engineered strain exhibits no antagonistic effect, enabling low-cost, large-scale production of the degrading enzyme. The composite engineered strain can achieve precise regulation of nutrient release from polymeric slow-release fertilizers. By adjusting the ratio of engineered strains producing peptidases and amidases, precise supply of nutrients to different stages throughout the growth cycle of different crops can be achieved, resulting in complete degradation of polymeric slow-release fertilizers, significantly improving crop yield and nutrient utilization, and showing significant application prospects in the development of precision agriculture.
Owner:SHANDONG AGRICULTURAL UNIVERSITY