2013•Fain kemikaruRequires access

Research on the Immobilization of S-Adenosylmethionine Synthetase with Sodium Alginate-Gelatin

Weining Niu

Open publisher page 0 citations

Abstract

S-Adenosylmethionine(SAM) synthetase was immobilized on sodium alginate-gelatin and then cross-linked with glutaraldehyde for improving the stability of the immobilized enzyme.The properties of the immobilized enzyme were identified.The results show that the optimal conditions for the immobilization of the enzyme were as follows:the mass fraction of sodium alginate,gelatin and calcium chloride was 2.0%,1.0% and 4.0% respectively;the amount of enzyme was 2.5 g/L gel;the volume fraction of glutaraldehyde was 0.6%.The cross-linked immobilized enzyme showed good stability compared with the free enzyme.After incubation at 50 ℃ for 5 h,the immobilized enzyme maintained 72% of the original activity while the free enzyme lost all activity.The cross-linked immobilized enzyme showed good stability in alkaline solution.It still kept more than 87% of the original activity when incubated in the buffer of pH=8.0~9.0 at 4 ℃ for 10 h.The cross-linked immobilized enzyme was employed to synthesize the SAM and it retained 65% activity after eight times repeated operations.

About this research paper

What this paper is about

S-Adenosylmethionine(SAM) synthetase was immobilized on sodium alginate-gelatin and then cross-linked with glutaraldehyde for improving the stability of the immobilized enzyme.The properties of the immobilized enzyme were identified.The results show that the optimal conditions for the immobilization of the enzyme were as follows:the mass fraction of sodium alginate,gelatin and calcium chloride was 2.0%,1.0% and 4.0% respectively;the amount of enzyme was 2.5 g/L gel;the volume fraction of glutaraldehyde was 0.6%.The cross-linked immobilized enzyme showed good stability compared with the free enzyme.After incubation at 50 ℃ for 5 h,the immobilized enzyme maintained 72% of the original activity while the free enzyme lost all activity.The cross-linked immobilized enzyme showed good stability in alkaline solution.It still kept more than 87% of the original activity when incubated in the buffer of pH=8.0~9.0 at 4 ℃ for 10 h.The cross-linked immobilized enzyme was employed to synthesize the SAM and it retained 65% activity after eight times repeated operations.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

S-Adenosylmethionine(SAM) synthetase was immobilized on sodium alginate-gelatin and then cross-linked with glutaraldehyde for improving the stability of the immobilized enzyme.The properties of the immobilized enzyme were identified.The results show that the optimal conditions for the immobilization of the enzyme were as follows:the mass fraction of sodium alginate,gelatin and calcium chloride was 2.0%,1.0% and 4.0% respectively;the amount of enzyme was 2.5 g/L gel;the volume fraction of glutaraldehyde was 0.6%.The cross-linked immobilized enzyme showed good stability compared with the free enzyme.After incubation at 50 ℃ for 5 h,the immobilized enzyme maintained 72% of the original activity while the free enzyme lost all activity.The cross-linked immobilized enzyme showed good stability in alkaline solution.It still kept more than 87% of the original activity when incubated in the buffer of pH=8.0~9.0 at 4 ℃ for 10 h.The cross-linked immobilized enzyme was employed to synthesize the SAM and it retained 65% activity after eight times repeated operations.

Key concepts: Glutaraldehyde, Gelatin, Chemistry, Immobilized enzyme, Enzyme, Chromatography, Enzyme assay, Sodium

Related papers

Back to paper searchBrowse research topicsOriginal source
Research on the Immobilization of S-Adenosylmethionine Synthetase with Sodium Alginate-Gelatin — Research Paper | ScholarLens