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...

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Main Authors: Rameshwar Tiwari, Kanika Kumar, Surender Singh, Lata Nain, Pratyoosh Shukla
Format: Article
Language:English
Published: Frontiers Media S.A. 2016-10-01
Series:Frontiers in Microbiology
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01597/full
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author Rameshwar Tiwari
Rameshwar Tiwari
Kanika Kumar
Surender Singh
Lata Nain
Pratyoosh Shukla
author_facet Rameshwar Tiwari
Rameshwar Tiwari
Kanika Kumar
Surender Singh
Lata Nain
Pratyoosh Shukla
author_sort Rameshwar Tiwari
collection DOAJ
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 sulphur 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.
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spelling doaj.art-b3f79ca548194b879eb1de3c818bfdb32022-12-21T23:35:48ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2016-10-01710.3389/fmicb.2016.01597222900Molecular detection and environment-specific diversity of glycosyl hydrolase family 1 β-glucosidase in different habitatsRameshwar Tiwari0Rameshwar Tiwari1Kanika Kumar2Surender Singh3Lata Nain4Pratyoosh Shukla5Department of Microbiology Maharshi Dayanand University, Rohtak-124001, Haryana, INDIADivision of Microbiology, IARI, New DelhiICAR-National Research Centre on Plant Biotechnology, LBS Centre, IARI, Pusa Campus, New DelhiDivision of Microbiology, IARI, New DelhiDivision of Microbiology, IARI, New DelhiDepartment of Microbiology Maharshi Dayanand University, Rohtak-124001, Haryana, INDIAβ-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 sulphur 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.http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01597/fullMetagenomicsmicrobial communitymetabolic profilingOperational taxonomic unitsGH1 β-glucosidase
spellingShingle Rameshwar Tiwari
Rameshwar Tiwari
Kanika Kumar
Surender Singh
Lata Nain
Pratyoosh Shukla
Molecular detection and environment-specific diversity of glycosyl hydrolase family 1 β-glucosidase in different habitats
Frontiers in Microbiology
Metagenomics
microbial community
metabolic profiling
Operational taxonomic units
GH1 β-glucosidase
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 Metagenomics
microbial community
metabolic profiling
Operational taxonomic units
GH1 β-glucosidase
url http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01597/full
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