TY  - JOUR
AU  - Falkenberg, Fabian
AU  - Rahba, Jade
AU  - Fischer, David
AU  - Bott, Michael
AU  - Bongaerts, Johannes
AU  - Siegert, Petra
TI  - Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensis Kh10‐101 T
JO  - FEBS Open Bio
VL  - 12
IS  - 10
SN  - 2211-5463
CY  - Hoboken, NJ
PB  - Wiley
M1  - FZJ-2022-02898
SP  - 1729-1746
PY  - 2022
N1  - Biotechnologie 1
AB  - Halophilic and halotolerant microorganisms represent a promising source of salt-tolerant enzymes suitable for various biotechnological applications where high salt concentrations would otherwise limit enzymatic activity. Considering the current growing enzyme market and the need for more efficient and new biocatalysts, the present study aimed at the characterization of a high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T. The protease gene was cloned and expressed in Bacillus subtilis DB104. The recombinant protease SPAO with 269 amino acids belongs to the subfamily of high-alkaline subtilisins. The biochemical characteristics of purified SPAO were analyzed in comparison with subtilisin Carlsberg, Savinase, and BPN'. SPAO, a monomer with a molecular mass of 27.1 kDa, was active over a wide range of pH 6.0–12.0 and temperature 20–80 °C, optimally at pH 9.0–9.5 and 55 °C. The protease is highly oxidatively stable to hydrogen peroxide and retained 58% of residual activity when incubated at 10 °C with 5% (v/v) H2O2 for 1 h while stimulated at 1% (v/v) H2O2. Furthermore, SPAO was very stable and active at NaCl concentrations up to 5.0 m. This study demonstrates the potential of SPAO for biotechnological applications in the future.
LB  - PUB:(DE-HGF)16
C6  - 35727859
UR  - <Go to ISI:>//WOS:000820971100001
DO  - DOI:10.1002/2211-5463.13457
UR  - https://juser.fz-juelich.de/record/908891
ER  -