Characterization of a thermostable glycoside hydrolase (CMbg0408) from the hyperthermophilic archaeon Caldivirga maquilingensis IC-167.

Background: Hyperthermophilic archaea capable of functioning optimally at very high temperatures are a good source of unique and industrially important thermostable enzymes.

Results: A glycoside hydrolase family 1 β-galactosidase gene (BglB) from a hyperthermophilic archaeon Caldivirga maquilingensis IC-167 was cloned and expressed in Escherichia coli. The recombinant enzyme (CMbg0408) displayed optimum activity at 110 °C and pH 5.0. It also retained 92% and 70% of its maximal activity at 115 and 120 °C, respectively. The enzyme was completely thermostable and active after 120 min of incubation at 80 and 90 °C. It also showed broad substrate specificity with activities of 8876 ± 185 U mg for p-nitrophenyl-β-d-galactopyranoside, 4464 ± 172 U mg for p-nitrophenyl-β-d-glucopyranoside, 1486 ± 68 U mg for o-nitrophenyl-β-d-galactopyranoside, 2250 ± 86 U mg for o-nitrophenyl-β-d-xylopyranoside and 175 ± 4 U mg for lactose. A catalytic efficiency (k /K ) of 3059 ± 122 mmol L  s and K value of 8.1 ± 0.08 mmol L were displayed towards p-nitrophenyl-β-d-galactopyranoside.

Conclusion: As a result of its remarkable thermostability and high activity at high temperatures, this novel β-galactosidase may be useful for food and pharmaceutical applications. © 2016 Society of Chemical Industry.