TY  - JOUR
A1  - Falkenberg, Fabian
A1  - Voß, Leonie
A1  - Bott, Michael
A1  - Bongaerts, Johannes
A1  - Siegert, Petra
T1  - New robust subtilisins from halotolerant and halophilic Bacillaceae
JF  - Applied Microbiology and Biotechnology
N2  - The aim of the present study was the characterisation of three true subtilisins and one phylogenetically intermediate subtilisin from halotolerant and halophilic microorganisms. Considering the currently growing enzyme market for efficient and novel biocatalysts, data mining is a promising source for novel, as yet uncharacterised enzymes, especially from halophilic or halotolerant Bacillaceae, which offer great potential to meet industrial needs. Both halophilic bacteria Pontibacillus marinus DSM 16465ᵀ and Alkalibacillus haloalkaliphilus DSM 5271ᵀ and both halotolerant bacteria Metabacillus indicus DSM 16189 and Litchfieldia alkalitelluris DSM 16976ᵀ served as a source for the four new subtilisins SPPM, SPAH, SPMI and SPLA. The protease genes were cloned and expressed in Bacillus subtilis DB104. Purification to apparent homogeneity was achieved by ethanol precipitation, desalting and ion-exchange chromatography. Enzyme activity could be observed between pH 5.0–12.0 with an optimum for SPPM, SPMI and SPLA around pH 9.0 and for SPAH at pH 10.0. The optimal temperature for SPMI and SPLA was 70 °C and for SPPM and SPAH 55 °C and 50 °C, respectively. All proteases showed high stability towards 5% (w/v) SDS and were active even at NaCl concentrations of 5 M. The four proteases demonstrate potential for future biotechnological applications.
KW  - Biotechnological application
KW  - Bacillaceae
KW  - Subtilisin
KW  - Subtilases
KW  - Halotolerant protease
Y1  - 2023
U6  - http://dx.doi.org/10.1007/s00253-023-12553-w
SN  - 1432-0614
N1  - Corresponding author: Petra Siegert
VL  - 107
SP  - 3939
EP  - 3954
PB  - Springer Nature
CY  - Berlin
ER  -