Table 3.
Preliminary characterization of halophilic enzymes
Sample Site | Microorganism | Potent enzyme produced | Production level (UmL-1) | pH optima | Salt optima (%, NaCl) | Temp. optima (°C) | Solvent-stability† (25%, v/v) | Thermal stability (°C) # |
---|---|---|---|---|---|---|---|---|
Sambhar Lake | Haloalkaliphilic bacterium EMB1 | Protease | 28 | 9.5 | 5 | 50 | Stable | 50 |
Haloalkaliphilic bacterium EMB2 | Protease | 37 | 10.0 | 3 | 50 | Stable | 50 | |
Haloalkaliphilic bacterium EMB3 | Protease | 21 | 9.0 | 6 | 45 | Stable | 50 | |
Haloalkaliphilic bacterium EMB4 | Amylase | 1.2 | 9.0 | 3 | 40 | Stable | 50 | |
Kozhikode | Marinobactersp. EMB5 | Lipase | 129 | 9.0 | 2 | 50 | Stable | 60 |
Marinobactersp. EMB6 | Lipase | 88 | 9.5 | 2 | 65 | Stable | 60 | |
Virgibacillussp. EMB7 | Protease | 156 | 7.5 | 1 | 60 | Stable | 50 | |
Marinobactersp. EMB8 | Amylase | 4 | 7.0 | 1 | 45 | Stable | 50 | |
Goa | Bacillussp. EMB9 | Protease | 191 | 9.0 | 1 | 60 | * | * |
Oceanobacillussp. EMB10 | Protease | 26 | 9.0 | 1 | 55 | * | * | |
Triveni Sangam | Chromohalobactersp. EMB12 | Lipase | 65 | 9.5 | 2 | 65 | Stable | 50 |
Virgibacillussp. EMB13 | Protease | 62 | 7.5 | 1 | 60 | Stable | 50 | |
Halobacillussp. EMB14 | Amylase | 0.3 | 7.5 | 1 | 55 | * | * | |
Nagoa | Halobacillussp. EMB15 | Amylase | 0.2 | 8.0 | 1 | 55 | * | * |
Virgibacillussp. EMB16 | Protease | 60 | 7.5 | 1 | 60 | * | * | |
Halobacillussp. EMB17 | Amylase | 0.2 | 7.5 | 1 | 55 | * | * | |
Haloalkaliphilic bacterium D-10-102 | Lipase | 7 | 9.5 | 1.5 | 65 | * | * | |
Somnath | Halomonassp. EMB11 | Lipase | 42 | 9.0 | 2 | 65 | * | * |
Haloalkaliphilic bacterium EMB18 | Protease | 38 | 10.0 | 2 | 55 | Stable | 55 | |
Haloalkaliphilic bacterium S-15-9 | Lipase | 57 | 9.5 | 1.5 | 65 | Stable | 60 | |
Veraval | Haloalkaliphilic bacterium Ve2-20-92 | Lipase | 15 | 9.5 | 1.5 | 65 | * | * |
Not defined
Solvent stability checked in hexane, cyclohexane, decane, dodecane and toluene
Stability for 1h