Burkhardt, ChristinChristinBurkhardtSchäfers, ChristianChristianSchäfersClaren, JörgJörgClarenSchirrmacher, GeorgGeorgSchirrmacherAntranikian, GarabedGarabedAntranikian2019-10-142019-10-142019-10-01Catalysts 9 (10): 830 (2019)http://hdl.handle.net/11420/3546Laminarinases exhibit potential in a wide range of industrial applications including the production of biofuels and pharmaceuticals. In this study, we present the genetic and biochemical characteristics of FLamA and FLamB, two laminarinases derived from a metagenomic sample from a hot spring in the Azores. Sequence comparison revealed that both genes had high similarities to genes from Fervidobacterium nodosum Rt17-B1. The two proteins showed sequence similarities of 62% to each other and belong to the glycoside hydrolase (GH) family 16. For biochemical characterization, both laminarinases were heterologously produced in Escherichia coli and purified to homogeneity. FLamA and FLamB exhibited similar properties and both showed highest activity towards laminarin at 90 °C and pH 6.5. The two enzymes were thermostable but differed in their half-life at 80 °C with 5 h and 1 h for FLamA and FLamB, respectively. In contrast to other laminarinases, both enzymes prefer β-1,3-glucans and mixed-linked glucans as substrates. However, FLamA and FLamB differ in their catalytic efficiency towards laminarin. Structure predictions were made and showed minor differences particularly in a kink adjacent to the active site cleft. The high specific activities and resistance to elevated temperatures and various additives make both enzymes suitable candidates for application in biomass conversion.en2073-4344201910Multidisciplinary Digital Publishing Institutehttps://creativecommons.org/licenses/by/4.0/Fervidobacteriumendo-β-1,3-glucanaselaminarinaseglycoside hydrolasethermostablegene duplicationBiowissenschaften, BiologieJournal Article2019-10-11urn:nbn:de:gbv:830-882.05164610.15480/882.243310.3390/catal910083010.15480/882.2433Journal Article