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Karthik, M. V. K.; Shukla, Pratyoosh

doi:10.1007/978-1-4614-4723-8_2

Cited by 2 publications

(2 citation statements)

References 88 publications

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“…Serine-type endopeptidase activity was found in the translated sequence, the total length of conserve domain was 57 amino acids with total alignment score of 223 and Identities of 44/53 (83%), Positives of 48/53 (90%) with the target domain when submitted in the ProDom server. Such studies were also done in inulinases ( Singh and Shukla, 2011 ; Singh et al, 2011 , 2016 ), Xylanses ( Karthik and Shukla, 2012 ).…”

Section: Discussionmentioning

confidence: 99%

An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of Its Binding Model toward Its Applications As Detergent Additive

et al. 2016

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A proteolytic strain of Bacillus pumilus MP 27 was isolated from water samples of Southern ocean produced alkaline protease. Since protease production need expensive ingredients, an economically viable process was developed by using low cost carbon source, wheat straw, supplemented with peptone. This protease was active within temperature ranges 10–70°C at pH 9. This process was optimized by response surface methodology using a Box Bekhman design by Design Expert 7.0 software that increased the protease activity to 776.5 U/ml. Moreover, the enzyme was extremely stable at a broad range of temperature and pH retaining 69% of its activity at 50°C and 70% at pH 11. The enzyme exhibited excellent compatibility with surfactants and commercial detergents, showing 87% stability with triton X-100 and 100% stability with Tide commercial detergent. The results of the wash performance analysis demonstrated considerably good de-staining at 50 and 4°C with low supplementation (109 U/ml). Molecular modeling of the protease revealed the presence of serine proteases, subtilase family and serine active site and further docking supported the association of catalytic site with the various substrates. Certainly, such protease can be considered as a good detergent additive in detergent industry with a possibility to remove the stains effectively even in a cold wash.

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Section: Discussionmentioning

confidence: 99%

An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of Its Binding Model toward Its Applications As Detergent Additive

et al. 2016

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“…Also, few studies on ecological screening, process optimization and enzymatic applications in industries are broadening the scope and new niche for their utilization (Shukla et al, 2007 ; Zhang et al, 2010 ; Banerjee et al, 2016 ; Baweja et al, 2016 ). Additionally, the modern techniques of gene editing, systems biology, molecular modeling of enzyme are the notable areas, where the innovation can provide novel products and applications (Singh and Shukla, 2011 ; Karthik and Shukla, 2012 ; Baweja et al, 2015 ; Gupta and Shukla, 2016b ; Kumar et al, 2016 ; Singh et al, 2016 ).…”

Section: Introductionmentioning

confidence: 99%

Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats

et al. 2016

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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.

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Background

Cited by 2 publications

References 88 publications

An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of Its Binding Model toward Its Applications As Detergent Additive

An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of Its Binding Model toward Its Applications As Detergent Additive

Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats

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