Table 1 Different Enzymes from the genus Bacillus *
Enzyme | Species | Comments |
|---|---|---|
Agarase | Bacillus sp. | Hydrolyzes the (β-1,4 linkage of agarose |
α-Amylase | B. amyloliquefaciens B. caldolyticus, B. coagulans B. licheniformis, B. macerans B. stearothermophilus B. subtilis, B. subtilis var. amylosacchariticus | Endohydrolysis of the α-1,4-glucosidic linkages in polysaccharides; different species produce enzymes with different properties |
β-Amylase | B. cereus, B. megaterium B. polymyxa Alkalophilic Bacillus spp. | Exohydrolysis of the α-1,4-glucosidic linkages in polysaccharides yielding β-maltose |
Cellulase | B. brevis, B. firmus,B. polymyxa B. pumilus, B. subtilis | Hydrolysis of carboxymethyl cellulose to cellobiose |
Chitinase | B. circulans | Four enzymes induced by growth on crab-shell chitin |
β-1,3-glucanase | B. circulans, B. polymyxa B. subtilis, Alkalophilic Bacillus sp. | Endohydrolysis of the β-1,3-glycosidic linkages in laminarin and related glucans |
Isoamylase | B. amyloliquefaciens B. polymyxa | Hydrolysis of the α-1,6-glycosidic branch linkages in glycogen, amylopectin, etc. |
Pectate lyase | B. circulans, B. polymyxa B. pumilus, B. sphaericus B. stearothermophilus B. subtilis, Alkalophilic Bacillus sp. | Endocleavage of polygalacturonic acid by an eliminative reaction |
Pullulanase | Alkalophilic Bacillus sp. | Endohydrolysis of the α-1,6 linkage of pullulan |
Xylanase | B. amyloliquefaciens B. firmus, B. polymyxa B. subtilis, B. subtilis var. amylosacchariticus | Hydrolysis of xylans; specificity of the enzymes has not been studied in detail |
Proteases | ||
Alkalophilic protease | Alkalophilic Bacillus sp. | Serine enzymes from alkalophilic species with very high pH optima |
Aminopeptidase | B. licheniformis, B. subtilis | |
Esterase | B. subtilis | Serine enzyme with high esterolytic and low proteolytic activity |
Halophilic protease | Bacillus sp. | Produced optimally in media containing 1.0 M NaCl |
Metal protease | B. amyloliquefaciens B. cereus, B. licheniformis B. megaterium, B. polymyxa B. subtili, B. subtilis var. amylosacchariticus B. thermoproteolyticus B. thuringiensis | Enzymes require Ca+ for stability and Zn2+ for activity; pH optimum at or near neutral |
Serine protease | B. amyloliquefaciens B. licheniformis, B. pumilus B. subtilis, B. subtilis var. amylosacchariticus | The subtilisins; alkaline pH optima, serine residue at or near the active site |
Penicillinases | ||
β-Lactamase | B. anthracis, B. cereus B. licheniformis, B. megaterium B. subtilis | Hydrolysis of the amide bond in the β-lactam ring of penicillins and cephalosporins |
Nucleases and phosphatases | ||
Alkaline phosphatase | B. amyloliquefaciens B. cereus, B. subtilis Alkalophilic Bacillus sp. | Often cell-bound, the enzyme is extracellular in these species |
Deoxyribonucleaseribonuclease | B. amyloliquefaciens, B. cereus B. pumilus, B. subtilis | A large number of DNases, RNases, and phosphodiesterases with individual properties have been purified |
3-Nucleotidase | B. subtilis | Active on both ribonucleotides and deoxyribonucleotides |
5-Nucleotidase | Cell-bound enzyme in these species | |
Bacteriolytic enzymes | ||
Endo-N-acetylglucosaminidase | B. licheniformis, B. subtilis | |
Exo-N-acetylglucosaminidase | B. subtilis | |
Endo-N-acetylmuramidase | B. subtilis | True lysozyme |
Exo-N-acetylmuramidase | B. subtilis | |
N-acetyl-muramylL-alanine amidase | B. licheniformis B. subtilis | A cell-bound enzyme; the major autolysin |
Lipase | B. licheniformis | Hydrolysis of triacylglycerol to diacylglycerol and a fatty acid anion |
Phospholipase C | B. anthracis B. cereus B. thuringiensis | Responsible for the “egg-yolk” reaction |
Thiaminase | B. thiaminolyticus | |