<strong><span style="font-size:9pt;line-height:115%;">The human feet and mouth are known as sources of methylated sulfides, which are produced by other microflora. Methylated sulfides could be oxidized by methylotrophic bacteria, which may result in odor reduction in human feet and mouth. In this study, we collected a total of 21 isolates from human feet, and 37 isolates from human mouth. These isolates were identified with biochemical test such as oxidase and catalase test and Gram staining assay. The presence of <em>mxaF</em> gene of methanol dehydrogenase was detected by PCR using specific primers. However, the result showed that most of the isolates did not possess <em>mxaF</em> gene. Hence, the methanol dehydrogenase (MDH) activity was also determined. From the total 21 isolates obtained from the feet, only 15 of them showed MDH activity whereas 23 isolates from the total 37 isolates obtained from teeth and tongue region also showed MDH activity. Isolate K25-3 (74.444 U/ml), K33-6 (79.815 U/ml), and K43-5 (69.259 U/ml) from human feet and M41L3 (135.926 U/ml), M27G2 (85.556 U/ml), and M51G1 (103.333 U/ml) from human mouth showed the highest total enzyme activity. Isolates with the highest total activity could be used for further studies such as purification of the enzyme and isolates characterization.</span></strong>

  • DIANA ELIZABETH WATURANGI Atma Jaya Catholic University of Indonesia
  • CATHERINE DELANY NICHOLAS Atma Jaya Catholic University of Indonesia
  • CINDY OKTAVIA SUSANTO Atma Jaya Catholic University of Indonesia
  • MAGGY THENAWIJAYA SUHARTONO Atma Jaya Catholic University of Indonesia
Keywords: <strong><span style="font-size, 9pt, line-height, 115%, ">The human feet and mouth are known as sources of methylated sulfides, which are produced by other microflora. Methylated sulfides could be oxidized by methylotrophic bacteria, which may result in odor reduction in human feet and mouth. In this study, we collected a total of 21 isolates from human feet, and 37 isolates from human mouth. These isolates were identified with biochemical test such as oxidase and catalase test and Gram staining assay. The presence of <em>mxaF</em> gene of methanol dehydrogenase was detected by PCR using specific primers. However, the result showed that most of the isolates did not possess <em>mxaF</em> gene. Hence, the methanol dehydrogenase (MDH) activity was also determined. From the total 21 isolates obtained from the feet, only 15 of them showed MDH activity whereas 23 isolates from the total 37 isolates obtained from teeth and tongue region also showed MDH activity. Isolate K25-3 (74.444 U/ml), K33-6 (79.815 U/ml), and K43-5 (69.259 U/ml) from human feet and M41L3 (135.926 U/ml), M27G2 (85.556 U/ml), and M51G1 (103.333 U/ml) from human mouth showed the highest total enzyme activity. Isolates with the highest total activity could be used for further studies such as purification of the enzyme and isolates characterization.</span></strong>

Abstract

The human feet and mouth are known as sources of methylated sulfides, which are produced by other microflora. Methylated sulfides could be oxidized by methylotrophic bacteria, which may result in odor reduction in human feet and mouth. In this study, we collected a total of 21 isolates from human feet, and 37 isolates from human mouth. These isolates were identified with biochemical test such as oxidase and catalase test and Gram staining assay. The presence of mxaF gene of methanol dehydrogenase was detected by PCR using specific primers. However, the result showed that most of the isolates did not possess mxaF gene. Hence, the methanol dehydrogenase (MDH) activity was also determined. From the total 21 isolates obtained from the feet, only 15 of them showed MDH activity whereas 23 isolates from the total 37 isolates obtained from teeth and tongue region also showed MDH activity. Isolate K25-3 (74.444 U/ml), K33-6 (79.815 U/ml), and K43-5 (69.259 U/ml) from human feet and M41L3 (135.926 U/ml), M27G2 (85.556 U/ml), and M51G1 (103.333 U/ml) from human mouth showed the highest total enzyme activity. Isolates with the highest total activity could be used for further studies such as purification of the enzyme and isolates characterization.

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Author Biographies

DIANA ELIZABETH WATURANGI, Atma Jaya Catholic University of Indonesia
Faculty of Biotechnology, Atma Jaya Catholic University of Indonesia
CATHERINE DELANY NICHOLAS, Atma Jaya Catholic University of Indonesia
Faculty of Biotechnology, Atma Jaya Catholic University of Indonesia
CINDY OKTAVIA SUSANTO, Atma Jaya Catholic University of Indonesia
Faculty of Biotechnology, Atma Jaya Catholic University of Indonesia
MAGGY THENAWIJAYA SUHARTONO, Atma Jaya Catholic University of Indonesia
Faculty of Biotechnology, Atma Jaya Catholic University of Indonesia
How to Cite
WATURANGID. E., NICHOLASC. D., SUSANTOC. O., & SUHARTONOM. T. (1). <strong><span style="font-size:9pt;line-height:115%;">The human feet and mouth are known as sources of methylated sulfides, which are produced by other microflora. Methylated sulfides could be oxidized by methylotrophic bacteria, which may result in odor reduction in human feet and mouth. In this study, we collected a total of 21 isolates from human feet, and 37 isolates from human mouth. These isolates were identified with biochemical test such as oxidase and catalase test and Gram staining assay. The presence of <em>mxaF</em> gene of methanol dehydrogenase was detected by PCR using specific primers. However, the result showed that most of the isolates did not possess <em>mxaF</em> gene. Hence, the methanol dehydrogenase (MDH) activity was also determined. From the total 21 isolates obtained from the feet, only 15 of them showed MDH activity whereas 23 isolates from the total 37 isolates obtained from teeth and tongue region also showed MDH activity. Isolate K25-3 (74.444 U/ml), K33-6 (79.815 U/ml), and K43-5 (69.259 U/ml) from human feet and M41L3 (135.926 U/ml), M27G2 (85.556 U/ml), and M51G1 (103.333 U/ml) from human mouth showed the highest total enzyme activity. Isolates with the highest total activity could be used for further studies such as purification of the enzyme and isolates characterization.</span></strong&gt;. HAYATI Journal of Biosciences, 18(1), 11. https://doi.org/10.4308/hjb.18.1.11
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