Purification and characterisation of thermostable α-amylases from microbial sources

• Main Authors: Hazwani-Oslan, S.N (Author), Lim, S.J (Author), Oslan, S.N (Author)
• Format: Article
• Language: English
• Published: North Carolina State University, 2020
• Subjects: Amylases; Bacteriology; Characterisation; Column chromatography; Column Chromatography; Edta; Enzymes; Escherichia coli; Genetic manipulations; Glucose; High specificity; Inhibitory effect; Large scale productions; Microbial sources; Microorganism; Optimum temperature; Precipitation (chemical); Purification; Salt precipitation; Sources; Starch; Starch degradation; Thermostable; Α-Amylase
• Online Access: View Fulltext in Publisher; View in Scopus
• ISBN: 19302126 (ISSN)
• ISSN: 19302126 (ISSN)
• DOI: 10.15376/biores.15.1.2005-2029

α-Amylases (E. C 3.2.1.1) hydrolyse starch into smaller moieties such as maltose and glucose by breaking α-1,4-glycosidic linkages. The application of α-amylases in various industries has made the large-scale productions of these enzymes crucial. Thermostable α-amylase that catalyses starch degradation at the temperatures higher than 50 °C is favourable in harsh industrial applications. Due to ease in genetic manipulation and bulk production, this enzyme is most preferably produced by microorganisms. Bacillus sp. and Escherichia coli are commonly used microbial expression hosts for α-amylases (30 to 205 kDa in molecular weight). These amylases can be purified using ultrafiltration, salt precipitation, dialysis, and column chromatography. Recently, affinity column chromatography has shown the most promising result where the recovery rate was 38 to 60% and purification up to 13.2-fold. Microbial thermostable α-amylases have the optimum temperature and pH ranging from 50 °C to 100 °C and 5.0 to 10.5, respectively. These enzymes have high specificity towards potato starch, wheat starch, amylose, and amylopectin. EDTA (1 mM) gave the highest inhibitory effect (79%), but Ca2+ (5 mM) was the most effective co-factor with 155%. This review provides insight regarding thermostable α-amylases obtained from microbial sources for industrial applications. © 2020, North Carolina State University.