1984Journal of Chemical Technology and Biotechnology BiotechnologyRequires access

Production and properties of Aspergillus niger inulinase

Dirk G. Derycke, Erick Vandamme

Open publisher page 70 citations

Abstract

Abstract An inulinase producing Aspergillus niger strain was isolated from Compositae rhizosphere soil samples. High inulinase levels were produced on a corn steep liquor (CSL)‐maltose medium in the absence of inulin at 28°C within 110 h of fermentation. Media based on CSL‐sucrose yielded high cell‐bound inulinase activity; on inulin‐based media the enzyme was mainly extracellularly produced. Both crude extra‐and intracellular inulinase preparations displayed identical pH and temperature optima with maximal activity at pH 4.3–4.4 and at 55–56°C. These properties are favourable in view of large scale inulinase application for pure fructose production. High operation temperatures would avoid microbial contamination of reactors and would allow the use of high inulin‐substrate concentrations, a limiting factor in obtaining high conversion ratios. The remarkably low pH optimum prevents colour formation and undesirable chemical side reactions. An advantageous low ratio of invertase to inulinase activity (S/I value) of 0.85 was found for the crude extracellular enzyme preparation. Crude inulin (chicory) extracts are hydrolysed faster than pure inulin. Apart from inulin (100% hydrolysis), sucrose (45%) and raffinose (20%) are also hydrolysed, and no liberation of oligomers or of sucrose from inulin was observed. These facts indicate that the A. niger enzyme is an exo‐acting inulinase. The above characteristics make this A. niger inulinase an industrially attractive enzyme for the preparation of pure fructose from inulin‐containing agricultural crops.

About this research paper

What this paper is about

Abstract An inulinase producing Aspergillus niger strain was isolated from Compositae rhizosphere soil samples. High inulinase levels were produced on a corn steep liquor (CSL)‐maltose medium in the absence of inulin at 28°C within 110 h of fermentation. Media based on CSL‐sucrose yielded high cell‐bound inulinase activity; on inulin‐based media the enzyme was mainly extracellularly produced. Both crude extra‐and intracellular inulinase preparations displayed identical pH and temperature optima with maximal activity at pH 4.3–4.4 and at 55–56°C. These properties are favourable in view of large scale inulinase application for pure fructose production. High operation temperatures would avoid microbial contamination of reactors and would allow the use of high inulin‐substrate concentrations, a limiting factor in obtaining high conversion ratios. The remarkably low pH optimum prevents colour formation and undesirable chemical side reactions. An advantageous low ratio of invertase to inulinase activity (S/I value) of 0.85 was found for the crude extracellular enzyme preparation. Crude inulin (chicory) extracts are hydrolysed faster than pure inulin. Apart from inulin (100% hydrolysis), sucrose (45%) and raffinose (20%) are also hydrolysed, and no liberation of oligomers or of sucrose from inulin was observed. These facts indicate that the A. niger enzyme is an exo‐acting inulinase. The above characteristics make this A. niger inulinase an industrially attractive enzyme for the preparation of pure fructose from inulin‐containing agricultural crops.

Why it matters

OpenAlex reports 70 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

Abstract An inulinase producing Aspergillus niger strain was isolated from Compositae rhizosphere soil samples. High inulinase levels were produced on a corn steep liquor (CSL)‐maltose medium in the absence of inulin at 28°C within 110 h of fermentation. Media based on CSL‐sucrose yielded high cell‐bound inulinase activity; on inulin‐based media the enzyme was mainly extracellularly produced. Both crude extra‐and intracellular inulinase preparations displayed identical pH and temperature optima with maximal activity at pH 4.3–4.4 and at 55–56°C. These properties are favourable in view of large scale inulinase application for pure fructose production. High operation temperatures would avoid microbial contamination of reactors and would allow the use of high inulin‐substrate concentrations, a limiting factor in obtaining high conversion ratios. The remarkably low pH optimum prevents colour formation and undesirable chemical side reactions. An advantageous low ratio of invertase to inulinase activity (S/I value) of 0.85 was found for the crude extracellular enzyme preparation. Crude inulin (chicory) extracts are hydrolysed faster than pure inulin. Apart from inulin (100% hydrolysis), sucrose (45%) and raffinose (20%) are also hydrolysed, and no liberation of oligomers or of sucrose from inulin was observed. These facts indicate that the A. niger enzyme is an exo‐acting inulinase. The above characteristics make this A. niger inulinase an industrially attractive enzyme for the preparation of pure fructose from inulin‐containing agricultural crops.

Key concepts: Inulinase, Inulin, Aspergillus niger, Fructose, Chemistry, Food science, Sucrose, Hydrolysis

Related papers

Back to paper searchBrowse research topicsOriginal source
Production and properties of Aspergillus niger inulinase — Research Paper | ScholarLens