Sago starch as a biomass source: Raw sago starch hydrolysis by commercial enzymes

Abstract

Raw sage starch and sage starch pretreated by heating at 60°C for 2 hours in sodium acetate buffer (pH 3.5) were hydrolysed using commercial glucoamylase-AMG (EC 3.2.1.3), α-amylases-BAN, Fungamyl and Termamyl (EC 3.2.1.1), debranching amylase-Promozyme (EC 3.2.1.41), and their mixtures in sodium acetate buffer, pH 5.0 at 35°C. Raw sage starch was a poor substrate for enzyme action compared to corn and tapioca starches tested under the same conditions, although pretreating the starch increased the extent and rate of hydrolysis. A strong synergism between glucoamylase and α-amylase on the hydrolysis of both untreated and pretreated sage starch was observed. The hydrolysis products were characterized by high-performance size-exclusion chromatography (HPSEC). The total carbohydrate concentration of hydrolysed sage starch decreased but the amylose and amylopectin ratios in the residues remained the same.

Raw sago starch and sago starch pretreated by heating at 60°C for 2 hours in sodium acetate buffer (pH 3.5) were hydrolysed using commercial glucoamylase-AMG (EC 3.2.1.3), α-amylases-BAN, Fungamyl and Termamyl (EC 3.2.1.1), debranching amylase-Promozyme (EC 3.2.1.41), and their mixtures in sodium acetate buffer, pH 5.0 at 35°C. Raw sago starch was a poor substrate for enzyme action compared to corn and tapioca starches tested under the same conditions, although pretreating the starch increased the extent and rate of hydrolysis. A strong synergism between glucoamylase and α-amylase on the hydrolysis of both untreated and pretreated sago starch was observed. The hydrolysis products were characterized by high-performance size-exclusion chromatography (HPSEC). The total carbohydrate concentration of hydrolysed sago starch decreased but the amylose and amylopectin ratios in the residues remained the same.