Calcium and sodium ions synergistically enhance the thermostability of a maltooligosaccharide-forming amylase from Bacillus stearothermophilus STB04

Abstract

Maltooligosaccharide-forming amylases (MFAses) are promising tools for a variety of food industry applications because of their ability to hydrolyze starch into maltooligosaccharides. However, high thermostability is a key requirement for enzymes used in these applications. In this work, we investigated the effect of Ca²⁺ and Na⁺ on the thermostability of an MFAse from Bacillus stearothermophilus (Bst-MFAse). The results showed that Ca²⁺ and Na⁺ synergistically prolong the half-life of Bst-MFAse. The most significant improvement, which preserved 71.1% of initial activity after incubation at 80 °C for 180 min, was achieved by adding 10 mM Ca²⁺ and 40 mM Na⁺ simultaneously. The increase in Bst-MFAse thermostability imparted by the addition of Ca²⁺ and Na⁺ may be associated with an important Ca²⁺-Na⁺-Ca²⁺ triad structure. This study provides an effective way to enhance the thermostability of Bst-MFAse and related enzymes.

Keywords: Ca(2+)–Na(+)–Ca(2+) binding site; Maltooligosaccharide-forming amylase; Synergistic effect; Thermostability.