10.15480/882.2433
Burkhardt, Christin
Christin
Burkhardt
1163614564
Schäfers, Christian
Christian
Schäfers
0000-0001-5042-1899
1023584190
Claren, Jörg
Jörg
Claren
140102108
Schirrmacher, Georg
Georg
Schirrmacher
131446649
Antranikian, Garabed
Garabed
Antranikian
0000-0001-6934-5603
109822382
Comparative analysis and biochemical characterization of two endo-β-1,3-glucanases from the thermophilic bacterium fervidobacterium sp.
Multidisciplinary Digital Publishing Institute
2019
Fervidobacterium
endo-β-1,3-glucanase
laminarinase
glycoside hydrolase
thermostable
gene duplication
Biowissenschaften, Biologie
TUHH Universitätsbibliothek
TUHH Universitätsbibliothek
2019-10-14
2019-10-14
2019-10-01
2019-10-11
en
Journal Article
Catalysts 9 (10): 830 (2019)
http://hdl.handle.net/11420/3546
urn:nbn:de:gbv:830-882.051646
10.15480/882.2433
10.3390/catal9100830
https://creativecommons.org/licenses/by/4.0/
Laminarinases 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.
2073-4344
Catalysts
2019
Multidisciplinary Digital Publishing Institute