Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL ® from A. niger

• Published in: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Analytical technologies in the biomedical and life sciences, 2007-02, Vol.846 (1), p.51-56
• Main Authors: Toledo, A.L., Severo, J.B., Souza, R.R., Campos, E.S., Santana, J.C.C., Tambourgi, E.B.
• Format: Article
• Language: English
• Subjects: Adsorption; alpha-Amylases - chemistry; alpha-Amylases - metabolism; Analysis; Analytical, structural and metabolic biochemistry; Aspergillus niger; Aspergillus niger - enzymology; Biochemistry characterization; Biological and medical sciences; Electrophoresis, Polyacrylamide Gel; Expanded bed adsorption; Expansion degree; Fundamental and applied biological sciences. Psychology; General pharmacology; Hydrolysis; Medical sciences; Molecular Weight; Pharmacology. Drug treatments; Purification; α-Amylase
• ISSN: 1570-0232; 1873-376X
• DOI: 10.1016/j.jchromb.2006.08.011

In this work the purification and biochemistry characterization of α-amylases from Aspergillus niger (FORILASE NTL ®) were studied. The effects of expansion degree of resin bed on enzyme purification by expanded bed adsorption (EBA) have also been studied. Residence time distributions (RTD) studies were done to achieve the optimal conditions of the amylases recovery on ion-exchange resin, and glucose solution was used as a new tracer. Results showed that height equivalent of the theoretical plates (HETP), axial dispersion and the Prandt number increased with bed height, bed voidage and linear velocity. The adsorption capacity of α-amylases, on the resin, increased with bed height and the best condition was at four-expansion degree. α-Amylase characterization showed that this enzyme has high affinity with soluble starch, good hydrolysis potential and molecular weight of 116 kDa.