Immobilized Enzyme

Lipase,Candida antarctica (Immobilized) is an immobilized lipase isolated from Candida antarctica fraction B. Lipase,Candida antarctica (Immobilized) features high stability and selectivity. Lipase,Candida antarctica (Immobilized) is widely used in fields such as chemical synthesis, food oil modification, and biodiesel production.

Lipase,Candida antarctica (Immobilized on hydrophilic carrier) (Candida antarctica lipase B) is a lipase derived from Candida antarctica and immobilized on a hydrophilic carrier. Lipase,Candida antarctica (Immobilized on hydrophilic carrier) is a green catalyst that can be used to catalyze polymer synthesis.

Lipase, Pseudomonas fluorescens (Immobilized) is an immobilized biocatalyst derived from Pseudomonas fluorescens. Lipase, Pseudomonas fluorescens (Immobilized) efficiently catalyzes the hydrolysis, esterification and transesterification of triacylglycerols in solvent-free systems, and is particularly suitable for biodiesel production from soybean oil and selective modification of oils rich in EPA and DHA. Lipase, Pseudomonas fluorescens (Immobilized) exhibits optimal activity at pH 8.5 and 45°C, and retains residual activity after repeated cycles of use. Lipase, Pseudomonas fluorescens (Immobilized) is activated by Ca²⁺, but inhibited by Co²⁺, Ni²⁺, Fe³⁺, Fe²⁺ and EDTA.

Glucose isomerase (immobilized) is glucose isomerase, which catalyzes the reversible isomerization of D-glucose and D-xylose into D-fructose and D-xylulose, respectively. Glucose isomerase (immobilized) can be used to produce fructose syrup under high-temperature conditions above 90 ℃. Glucose isomerase (immobilized) is widely distributed in prokaryotes.

Penicillin amidase, E. coli (Immobilized) (PGA) is an amidohydrolase commonly used in industrial biocatalysis. Penicillin amidase, E. coli (Immobilized) serves as a starting material in the synthesis of semi-synthetic penicillins. Penicillin amidase, E. coli (Immobilized) promotes the production of semi-synthetic β-lactam antibiotics, participates in peptide synthesis, and catalyzes the formation of chiral compounds. Penicillin amidase, E. coli (Immobilized) is regulated by temperature and phenylacetic acid in E. coli. In free E. coli, it participates in the assimilation of aromatic compounds as a carbon source. Penicillin amidase, E. coli (Immobilized) is hypothesized to act as a scavenging enzyme for phenylacetyl-containing compounds in microbial metabolism and is associated with bacterial quorum sensing.

Penicillin G acylase (Immobilized) is an immobilized penicillin acylase with improved temperature and pH stability. Penicillin G acylase (Immobilized) has reusable performance and high recovery rates, retaining much of its original activity after 12 cycles. Among them, Penicillin G acylase (Immobilized) can catalyze penicillin G (PG) to generate 6-aminopenicillanic acid (6-APA) and 7-aminodeacetoxycephalosporanic acid, which are key intermediates for β-lactam antibiotics.

Lipase, Candida cylindracea (Immobilized) is an immobilized hydrolase and biocatalyst with relaxed positional and substrate specificity. Lipase, Candida cylindracea (Immobilized) can target primary and secondary ester bonds to completely hydrolyze triglycerides into fatty acids and glycerol, producing only trace amounts of monoglycerides. Lipase, Candida cylindracea (Immobilized) exhibits chain specificity, with a relatively fast hydrolysis rate for oleic acid and lauric acid chains, and the slowest hydrolysis rate for stearic acid chains. Lipase, Candida cylindracea (Immobilized) shows high catalytic activity toward long-chain triglycerides under the conditions of pH 8.0 and 37°C.

High-efficiency lipase,Candida antarctica (Immobilized on hydrophilic carrier) is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.

D-Amino acid oxidase is an enzyme to metabolize exogenous D-amino acids in animals for detoxifying action. D-Amino acid oxidase also modulates the level of D-serine in brain.

AMG 118 Immobilized cephalosporin C acylase is an enzyme that catalyzes in immobilized form and is generally used in industrial catalytic production of the important pharmaceutical intermediate 7-aminocephalosporanic acid (7-ACA). It contains CPC acylase, a highly specialized beta-lactam acylase or peptidase that cleaves the amide bonds between beta-lactams.

Arginase, Microorganism immobilized (L-Arginine amidinase) is an enzyme of the urea cycle. Arginase catalyzes the hydrolysis of L-arginine to L-ornithine and urea.

PNGase F (Immobilized, Microspin) is a resin in which PNGase F (peptide N-glycosidase F) is covalently coupled to agarose beads, and it is used to remove N-glycans from antibodies, fusion proteins and other N-glycosylated proteins. The enzyme is recombinantly expressed in Escherichia coli, with its sequence derived from Flavobacterium meningsepticum.

IdeS (Immobilized, Microspin) is a resin that covalently couples IdeS protease to agarose beads and cleaves IgG at specific sites to generate F(ab')2 and Fc fragments. After IdeS (Immobilized, Microspin) digestion, F(ab')2 and Fc fragments are obtained in the solution without IdeS enzyme.

Lipase, Aspergillus niger (Immobilized) is an immobilized triacylglycerol acyl hydrolase and biocatalyst. Lipase, Aspergillus niger (Immobilized) broadly catalyzes the hydrolysis of glycerol-long-chain fatty acid esters, exhibits positional selectivity for the 1,3-positions of glycerol, but shows low hydrolysis efficiency for castor oil. Lipase, Aspergillus niger (Immobilized) displays optimal activity at 45°C and pH 7.0, and remains stable at temperatures up to 60°C and over a broad pH range of 2.0-9.0. Lipase, Aspergillus niger (Immobilized) is activated by Ca²⁺ and Mg²⁺, but inhibited by Mn²⁺, Fe²⁺ and Zn²⁺.

Lipase (Immobilized,Used for biodiesel production) is a methanol-resistant lipase with high catalytic activity and can be used for the production of biodiesel. The reaction conditions of Lipase (Immobilized,Used for biodiesel production) are mild, which can avoid the oxidation of hydroxyl groups and the opening of double bonds, and prevent the production of by-products other than glycerol.

Lipase,Burkholderiacepacia (Immobilized) comes from Burkholderiacepacia and can be used for catalytic reaction.

Amoxicillin acylase (Immobilized) is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.

Cephalexin acylase (Immobilized) is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.

Cefaclor acylase (Immobilized) is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.

Cefradine acylase (Immobilized) is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.