A novel method of immobilizing penicillin acylase on basic anion exchange resin with hexamethylene diisocyanate and p-hydroxybenzaldehyde

Kobayashi, Kobee; Kageyama, Bunji; Yagi, Shigeo; Sonoyama, Takayasu

doi:10.1016/0922-338x(92)90044-u

Cited by 4 publications

(2 citation statements)

References 6 publications

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“…The primary amino groups can be activated by use of hexamethylene diisocyanate [441] or 2,4-toluylenediisocynate [250]. The primary amino groups can be activated by use of hexamethylene diisocyanate [441] or 2,4-toluylenediisocynate [250].…”

Section: Polymers Containing Amino Groupsmentioning

confidence: 99%

“…Remarkably, penicillin G acylase immobilized on Diaion CR 20 activated by hexamethylene diisocyanate can be used 300 times with 70 % of the original activity [441]. Remarkably, penicillin G acylase immobilized on Diaion CR 20 activated by hexamethylene diisocyanate can be used 300 times with 70 % of the original activity [441].…”

Section: Polymers Containing Amino Groupsmentioning

confidence: 99%

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Covalent Enzyme Immobilization

Cao¹

2005

Carrier‐bound Immobilized Enzymes

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Section: Polymers Containing Amino Groupsmentioning

confidence: 99%

Section: Polymers Containing Amino Groupsmentioning

confidence: 99%

Covalent Enzyme Immobilization

Cao¹

2005

Carrier‐bound Immobilized Enzymes

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Immobilization of Glucose Oxidase on Ordered Macroporous Silicas Functionalized with Amino Group

Wu¹,

He²,

Zhang³

et al. 2012

Chin. J. Chem.

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A novel glucose oxidase immobilized on three‐dimensionally ordered macroporous (3DOM) material has been prepared by firstly preparation of hybrid 3DOM SiO2‐NH2 materials using colloidal crystal method, and following covalent immobilization of glucose oxidase on the pore walls of the 3DOM materials. The materials were characterized by SEM, FTIR, DSC and BET techniques. SEM observation shows that the macropores are highly ordered and are interconnected by small windows. FTIR measurement shows that there are amino and organic groups in the pore walls. The surface area of the 3DOM SiO2‐NH2 material is about 10.2 m2/g. The loaded amount of enzyme is increased with amino content in the materials. The immobilized enzyme has high activity, thermal stability and can be reused.

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Batch production of deacetyl 7-aminocephalosporanic acid by immobilized cephalosporin-C deacetylase

Takimoto

Takakura

Tani

et al. 2004

Appl Microbiol Biotechnol

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Bacillus subtilis SHS0133 cephalosporin-C deacetylase (CAH) overexpressed in Escherichia coli was immobilized on an anion-exchange resin, KA-890, using glutaraldehyde. The activity yield of immobilized enzyme was approximately 55% of the free enzyme. The pH range for stability of the immobilized enzyme (pH 5-10) was broader than that for free enzyme. The K(m)(app) value of immobilized enzyme for 7-aminocephalosporanic acid (7-ACA) was similar to that of the free enzyme. This immobilized enzyme obeyed Michaelis-Menten kinetics similar to those of the free enzyme. A batch-type reactor with a water jacket was employed for deacetylation of 7-ACA using CAH immobilized on KA-890. Ten kilograms of 7-ACA were completely converted to deacetyl 7-ACA at pH 8.0 within 90 min. The reaction kinetics agreed well with a computer simulation model. Moreover, the immobilized enzyme exhibited only a slight loss of the initial activity even after repeated use (52 times ) over a period of 70 days. This reaction will thus be useful for the production of cephalosporin-type antibiotics.

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A novel method of immobilizing penicillin acylase on basic anion exchange resin with hexamethylene diisocyanate and p-hydroxybenzaldehyde

Cited by 4 publications

References 6 publications

Covalent Enzyme Immobilization

Covalent Enzyme Immobilization

Immobilization of Glucose Oxidase on Ordered Macroporous Silicas Functionalized with Amino Group

Batch production of deacetyl 7-aminocephalosporanic acid by immobilized cephalosporin-C deacetylase

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