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Cultivable Microbial Diversity in Domestic Bentonites and Their Hydrolytic Enzyme Production

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초록

We have isolated and identified 72 bacterial strains from four bentonite samples collected at the mining areas located in Gyeongsangbuk-do, Republic of Korea, and measured their hydrolytic enzyme (α-amylase, protease, and cellulase) activities to identify the isolates with industrial-use potential. Most of the isolates belonged to the Bacillaceae, with minor portions being from the Paenibacillaceae, Micrococcaceae, and Bacillales Family XII at the family level. Of the strains isolated, 33 had extracellular α-amylase activity, 30 strains produced cellulase, and 35 strains produced protease. Strain MBLB1268, having the highest α- amylase activity, was identified as Bacillus siamensis (0.38 ± 0.06 U/ml). Bacillus tequilensis MBLB1223, isolated from Byi33-b, showed the highest cellulase activity (0.26 ± 0.04 U/ml), whereas Bacillus wiedmannii MBLB1197, isolated from Zdb130-b, exhibited the highest protease activity (54.99 ± 0.78 U/ml). These findings show that diverse bacteria of the Bacillaceae family adhere to and exist in bentonite and are potential sources of industrially useful hydrolytic enzymes.

Abstract

We have isolated and identified 72 bacterial strains from four bentonite samples collected at the mining areas located in Gyeongsangbuk-do, Republic of Korea, and measured their hydrolytic enzyme (α-amylase, protease, and cellulase) activities to identify the isolates with industrial-use potential. Most of the isolates belonged to the Bacillaceae, with minor portions being from the Paenibacillaceae, Micrococcaceae, and Bacillales Family XII at the family level. Of the strains isolated, 33 had extracellular α-amylase activity, 30 strains produced cellulase, and 35 strains produced protease. Strain MBLB1268, having the highest α- amylase activity, was identified as Bacillus siamensis (0.38 ± 0.06 U/ml). Bacillus tequilensis MBLB1223, isolated from Byi33-b, showed the highest cellulase activity (0.26 ± 0.04 U/ml), whereas Bacillus wiedmannii MBLB1197, isolated from Zdb130-b, exhibited the highest protease activity (54.99 ± 0.78 U/ml). These findings show that diverse bacteria of the Bacillaceae family adhere to and exist in bentonite and are potential sources of industrially useful hydrolytic enzymes.

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