2001•Biotechnology(Faisalabad)Requires access

Purification,partial N-terminal sequencing and properties of an endoglucanase from Aspergillus niger

Shen Zhiyang, Guo Chunteng, Deng Wenhan, Pingfan Rao

Open publisher page 1 citations

Abstract

A novel cellulase was identified and isolated from a commercial Aspergillus niger cellulase preparation.The crude enzyme preparation,which was prepared by precipitation of the water extract of the culture of Aspergillus niger with ammonium sulfate,was further fractionated by three steps of chromatography of weak anion exchange to obtain an electrophoretically homogeneous cellulase. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be 36kD under non-reduced conditions and 38kD under reduced conditions, with the optimun pH at 3.5, and the optimum temperature at 55℃. The partial N-terminal amino acid sequences of the purified enzyme was identified as XXXFKCVGSMEDGAES.

About this research paper

What this paper is about

A novel cellulase was identified and isolated from a commercial Aspergillus niger cellulase preparation.The crude enzyme preparation,which was prepared by precipitation of the water extract of the culture of Aspergillus niger with ammonium sulfate,was further fractionated by three steps of chromatography of weak anion exchange to obtain an electrophoretically homogeneous cellulase. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be 36kD under non-reduced conditions and 38kD under reduced conditions, with the optimun pH at 3.5, and the optimum temperature at 55℃. The partial N-terminal amino acid sequences of the purified enzyme was identified as XXXFKCVGSMEDGAES.

Why it matters

OpenAlex reports 1 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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

A novel cellulase was identified and isolated from a commercial Aspergillus niger cellulase preparation.The crude enzyme preparation,which was prepared by precipitation of the water extract of the culture of Aspergillus niger with ammonium sulfate,was further fractionated by three steps of chromatography of weak anion exchange to obtain an electrophoretically homogeneous cellulase. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be 36kD under non-reduced conditions and 38kD under reduced conditions, with the optimun pH at 3.5, and the optimum temperature at 55℃. The partial N-terminal amino acid sequences of the purified enzyme was identified as XXXFKCVGSMEDGAES.

Key concepts: Aspergillus niger, Cellulase, Ammonium sulfate precipitation, Ammonium sulfate, Chemistry, Chromatography, Enzyme, Ammonium

Related papers

Back to paper searchBrowse research topicsOriginal source
Purification,partial N-terminal sequencing and properties of an endoglucanase from Aspergillus niger — Research Paper | ScholarLens