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Investigation of debranching pattern of a thermostable isoamylase and its application for the production of resistant starch

Li, Youran, Xu, Jingjing, Zhang, Liang, Ding, Zhongyang, Gu, Zhenghua, Shi, Guiyang
Carbohydrate research 2017 v.446-447 pp. 93-100
amylases, amylose, glucose, glycosidic linkages, isoamylase, liquid chromatography, molecular weight, nuclear magnetic resonance spectroscopy, oligosaccharides, pH, resistant starch, thermal stability
Debranching enzymes contribute to the enzymatic production of resistant starch (RS) by reducing substrate molecular weight and increasing amylose yield. In the present study, the action pattern of a thermostable isoamylase-type debranching enzyme on different types of starch was investigated. The molecular weight distribution, glycosidic bond composition and contents of oligosaccharides released were monitored by various liquid chromatography techniques and nuclear magnetic resonance spectroscopy (NMR). These analyses showed that the isoamylase could specifically and efficiently attack α-1,6-glucosidic linkages at branch points, leaving the amylose favored by other amylolytic enzymes. Its ability to attack side chains composed of 1–3 glucose residues differentiates it from other isoamylases, a property which is also ideal for the RS preparation process. The enzyme was used as an auxiliary enzyme in the hydrolytic stage. The highest RS yield (53.8%) was achieved under the optimized conditions of 70 °C and pH 5.0, using 7 U isoamylase per g starch and 2 NU amylase per g starch. These data also help us better understand the application of isoamylase for preparation of other products from highly branched starch materials.