Protease-, pectinase-and amylase-producing bacteria from a Kenyan soda lake
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Background: Alkaline enzymes are stable biocatalysts with potential applications in industrial technologies that offer high quality products. Objective: The growing demand for alkaline enzymes in industry has enhanced the search for microorganisms that produce these enzymes. Methods: Eighteen bacterial isolates from Lake Bogoria, Kenya, were screened for alkaline proteases, pectinases and amylases; characterized and subjected to quantitative analysis of the enzymes they produced. Results: The screening analysis ranked 14, 16 and 18 of the bacterial isolates as potent producers of alkaline proteases, pectinases and amylases, respectively. The isolates were classified into two groups: Group 1 (16 isolates) were facultatively alkaliphilic B. halodurans while group 2 (2 isolates) were obligately alkaliphilic B. pseudofirmus. Further analysis revealed that group 1 isolates were divided into two sub-groups, with sub-group I (4 isolates) being a phenotypic variant sub-population of sub-group II (12 isolates). Variation between the two populations was also observed in their enzymatic production profiles e.g. sub-group I isolates did not produce alkaline proteolytic enzymes while those in sub-group II did so (0.01-0.36 U/ml). Furthermore, they produced higher levels of the alkaline pectinolytic enzyme polygalacturonase (0.12-0.46 U/ml) compared to sub-group II isolates (0.05-0.10 U/ml), which also produced another pectinolytic enzyme-pectate lyase (0.01 U/ml). No clear distinction was however, observed in the production profiles of alkaline amylolytic enzymes by the isolates in the two sub-populations [0.20-0.40 U/ml (amylases), 0.24-0.68 U/ml (pullulanases) and 0.01-0.03 U/ml (cyclodextrin glycosyl transferases)]. On the other hand, group 2 isolates were phenotypically identical to one another and also produced similar amounts of proteolytic (0.38, 0.40 U/ml) and amylolytic [amylases (0.06, 0.1 U/ml), pullulanases (0.06, 0.09 U/ml) and cyclodextrin glycosyl transferases (0.01, 0.02 U/ml)] enzymes. Conclusion: The facultatively alkaliphilic B. halodurans and obligately alkaliphilic B. pseudofirmus isolates are attractive biotechnological sources of industrially important alkaline enzymes.
|Research areas and keywords||
Subject classification (UKÄ) – MANDATORY
|Number of pages||13|
|Journal||Open Biotechnology Journal|
|Publication status||Published - 2018 Jan 1|