Molecular Cloning and Characterization of an Enzyme Hydrolyzingp-Nitrophenyl α-D-Glucoside fromBacillus stearothermophilusSA0301

Molecular cloning and biochemical characterization of two novel oligo‐1,6‐glucosidases from Bacillus mycoides and Thermomyces lanuginosus

“…By comparing the biochemical properties of oligo‐1,6‐glucosidases from different microorganisms, we can conclude that most OGls are usually stable under neutral or alkaline pH, ranging from pH 6.0 to pH 11.0 . In contrast, BmOGL was highly active at acidic and neutral conditions, with a loss of only 20% of the initial activity after incubation at pH 4.0–8.0 for 1 h (Fig.…”

“…All of the oligo‐1,6‐glucosidases are not particularly thermostable, as it has been demonstrated that α‐glucosidase is fairly stable below 60°C, while isomaltase nearly completely loses its activity after only 15 min incubation at 52.5°C . Although the optimum temperature of TlOGL from the thermophilic fungus T. lanuginosus was lower than those of OGLs from thermophilic bacteria (ranging from 60 to 100°C), such as B. stearothermophilus , B. coagulans , B. thermoglucosidius , B. flavocaldarius , and Sulfolobus acidocaldarius , it was more thermostable than most OGLs ever reported (Fig. B), with an exception of OGL from S. acidocaldarius (its half life was 33.8 h at 90°C) .…”

Analysis ofα-glucosidase enzyme activity used in a rapid test for steam sterilization assurance

“…; Kobayashi et al . ). However, there is minimal knowledge of enzymes acting on α ‐MUG to give the fluorescent MU readout used to assess G. stearothermophilus spore inactivation.…”