Cargando…
Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats
β-glucosidase is a crucial element of the microbial cellulose multienzyme complex since it is responsible for the regulation of the entire cellulose hydrolysis process. Therefore, the aim of the present work was to explore the diversity and distribution of glycosyl hydrolase family 1 β-glucosidase g...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5062022/ https://www.ncbi.nlm.nih.gov/pubmed/27790196 http://dx.doi.org/10.3389/fmicb.2016.01597 |
_version_ | 1782459692895698944 |
---|---|
author | Tiwari, Rameshwar Kumar, Kanika Singh, Surender Nain, Lata Shukla, Pratyoosh |
author_facet | Tiwari, Rameshwar Kumar, Kanika Singh, Surender Nain, Lata Shukla, Pratyoosh |
author_sort | Tiwari, Rameshwar |
collection | PubMed |
description | β-glucosidase is a crucial element of the microbial cellulose multienzyme complex since it is responsible for the regulation of the entire cellulose hydrolysis process. Therefore, the aim of the present work was to explore the diversity and distribution of glycosyl hydrolase family 1 β-glucosidase genes in three different environmental niches including, Himalayan soil, cow dung and compost by metagenomic approach. Preliminary evaluation through metabolic profiling using BIOLOG based utilization patterns of carbon, nitrogen, phosphorus and sulfur revealed the environment and substrate specific nature of the indigenous microbial population. Furthermore, clonal library selection, screening and sequence analysis revealed that most of the GH1 β-glucosidase proteins had low identities with the available database. Analysis of the distribution of GH1 β-glucosidase gene fragments and β-glucosidase producing microbial community revealed the environment specific nature. The OTUs obtained from Himalayan soil and compost metagenomic libraries were grouped into 19 different genera comprising 6 groups. The cow dung sample displayed the least diversity of GH1 β-glucosidase sequences, with only 14 genera, distributed among three groups- Bacteroidetes, Firmicutes, and Actinobacteria. The metagenomic study coupled with metabolic profiling of GH1 β-glucosidase illustrated the existence of intricate relationship between the geochemical environmental factors and inherent microbial community. |
format | Online Article Text |
id | pubmed-5062022 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-50620222016-10-27 Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats Tiwari, Rameshwar Kumar, Kanika Singh, Surender Nain, Lata Shukla, Pratyoosh Front Microbiol Microbiology β-glucosidase is a crucial element of the microbial cellulose multienzyme complex since it is responsible for the regulation of the entire cellulose hydrolysis process. Therefore, the aim of the present work was to explore the diversity and distribution of glycosyl hydrolase family 1 β-glucosidase genes in three different environmental niches including, Himalayan soil, cow dung and compost by metagenomic approach. Preliminary evaluation through metabolic profiling using BIOLOG based utilization patterns of carbon, nitrogen, phosphorus and sulfur revealed the environment and substrate specific nature of the indigenous microbial population. Furthermore, clonal library selection, screening and sequence analysis revealed that most of the GH1 β-glucosidase proteins had low identities with the available database. Analysis of the distribution of GH1 β-glucosidase gene fragments and β-glucosidase producing microbial community revealed the environment specific nature. The OTUs obtained from Himalayan soil and compost metagenomic libraries were grouped into 19 different genera comprising 6 groups. The cow dung sample displayed the least diversity of GH1 β-glucosidase sequences, with only 14 genera, distributed among three groups- Bacteroidetes, Firmicutes, and Actinobacteria. The metagenomic study coupled with metabolic profiling of GH1 β-glucosidase illustrated the existence of intricate relationship between the geochemical environmental factors and inherent microbial community. Frontiers Media S.A. 2016-10-13 /pmc/articles/PMC5062022/ /pubmed/27790196 http://dx.doi.org/10.3389/fmicb.2016.01597 Text en Copyright © 2016 Tiwari, Kumar, Singh, Nain and Shukla. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Tiwari, Rameshwar Kumar, Kanika Singh, Surender Nain, Lata Shukla, Pratyoosh Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats |
title | Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats |
title_full | Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats |
title_fullStr | Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats |
title_full_unstemmed | Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats |
title_short | Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats |
title_sort | molecular detection and environment-specific diversity of glycosyl hydrolase family 1 β-glucosidase in different habitats |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5062022/ https://www.ncbi.nlm.nih.gov/pubmed/27790196 http://dx.doi.org/10.3389/fmicb.2016.01597 |
work_keys_str_mv | AT tiwarirameshwar moleculardetectionandenvironmentspecificdiversityofglycosylhydrolasefamily1bglucosidaseindifferenthabitats AT kumarkanika moleculardetectionandenvironmentspecificdiversityofglycosylhydrolasefamily1bglucosidaseindifferenthabitats AT singhsurender moleculardetectionandenvironmentspecificdiversityofglycosylhydrolasefamily1bglucosidaseindifferenthabitats AT nainlata moleculardetectionandenvironmentspecificdiversityofglycosylhydrolasefamily1bglucosidaseindifferenthabitats AT shuklapratyoosh moleculardetectionandenvironmentspecificdiversityofglycosylhydrolasefamily1bglucosidaseindifferenthabitats |