Lipase : an industrial enzyme through metagenomics / B. K. Konwar (PhD), Kalpana Sagar (PhD).
Konwar, B. K.| Call Number | 572.757 K827 |
| Author | Konwar, B. K., author. |
| Title | Lipase : an industrial enzyme through metagenomics / B. K. Konwar (PhD), Kalpana Sagar (PhD). |
| Physical Description | 1 online resource (xiv, 214 pages) |
| Contents | Application of lipases -- Metagenomics and unculturable bacteria -- Accessing metagenomics -- Metagenomics for lipase -- Functional approach for metagenomic library construction -- Ove rexpression of recombinant protein -- Biochemical characterization of purified lipase -- Genomic study of culture dependent bacteria -- Genomic study of culturable bacteria -- Microbial assay of culture supernatant containing crude lipase. |
| Summary | "Microbial lipases are industrially important and have gained their attention due to their stability, selectivity, and broad substrate specificity. Lipases are used as a medicine and also aid in indigestion, heartburn, allergy to gluten in wheat products (celiac disease), Crohn's disease, and cystic fibrosis. This new volume, Lipase: An Industrial Enzyme Through Metagenomics, considers the industrial demand for new sources of lipases with different catalytic characteristics that stimulate the growth and development isolation of new strains. The volume narrates the challenging metagenomic approach with the isolation of the lipase gene, its cloning into Escherichia coli, culture of the recombinant bacteria, and extraction and assessment of the lipase enzyme.Lipase-producing bacteria have been found in different habitats, such as industrial wastes, vegetable oil processing factories, dairy plants, and soils contaminated with oil and oil seeds among others. This volume is the effort of the authors to document the scientific findings carried out over the last eight years in the area of un-culturable soil microorganisms. The book presents the physicochemical features of lipases and their specific applications in different commercial industries. The in-depth study looks at metagenomics for lipases from all angles and provides a truly informative resource. It describes the biochemical characterization of lipase enzymes with the high activity in the presence of 1% tributyrin. The book also highlights the maximum activity of the enzyme at temperature 37 C and pH 7.5 in the presence of the divalent cations Ca2+, Mn2+, Zn2+ and Fe2+. CTAB, gum arabic, NaCl and organic solvents like ethanol, 1-propanol, acetone, acetonitrile, glycerol and DMSO.A wide review has been presented in the book on lipase enzymes purified from a large collection of microbes present in soil, seawater, waste-dumping sites, animal systems (including human beings), and the atmosphere. Stability of enzymes over changing environments of the industry is indeed a big issue, and the book deals at length with the changing temperatures and pH and metal ion concentrations. The book also highlights the antifungal and antibacterial activity of the lipase enzyme."--Provided by publisher. |
| Added Author | Sagar, Kalpana, author. |
| Subject | BIOCHEMISTRY. LIPASE. Metagenomics. |
| Multimedia |
Total Ratings:
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$a "Microbial lipases are industrially important and have gained their attention due to their stability, selectivity, and broad substrate specificity. Lipases are used as a medicine and also aid in indigestion, heartburn, allergy to gluten in wheat products (celiac disease), Crohn's disease, and cystic fibrosis. This new volume, Lipase: An Industrial Enzyme Through Metagenomics, considers the industrial demand for new sources of lipases with different catalytic characteristics that stimulate the growth and development isolation of new strains. The volume narrates the challenging metagenomic approach with the isolation of the lipase gene, its cloning into Escherichia coli, culture of the recombinant bacteria, and extraction and assessment of the lipase enzyme.Lipase-producing bacteria have been found in different habitats, such as industrial wastes, vegetable oil processing factories, dairy plants, and soils contaminated with oil and oil seeds among others. This volume is the effort of the authors to document the scientific findings carried out over the last eight years in the area of un-culturable soil microorganisms. The book presents the physicochemical features of lipases and their specific applications in different commercial industries. The in-depth study looks at metagenomics for lipases from all angles and provides a truly informative resource. It describes the biochemical characterization of lipase enzymes with the high activity in the presence of 1% tributyrin. The book also highlights the maximum activity of the enzyme at temperature 37 C and pH 7.5 in the presence of the divalent cations Ca2+, Mn2+, Zn2+ and Fe2+. CTAB, gum arabic, NaCl and organic solvents like ethanol, 1-propanol, acetone, acetonitrile, glycerol and DMSO.A wide review has been presented in the book on lipase enzymes purified from a large collection of microbes present in soil, seawater, waste-dumping sites, animal systems (including human beings), and the atmosphere. Stability of enzymes over changing environments of the industry is indeed a big issue, and the book deals at length with the changing temperatures and pH and metal ion concentrations. The book also highlights the antifungal and antibacterial activity of the lipase enzyme."--Provided by publisher.
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| Summary | "Microbial lipases are industrially important and have gained their attention due to their stability, selectivity, and broad substrate specificity. Lipases are used as a medicine and also aid in indigestion, heartburn, allergy to gluten in wheat products (celiac disease), Crohn's disease, and cystic fibrosis. This new volume, Lipase: An Industrial Enzyme Through Metagenomics, considers the industrial demand for new sources of lipases with different catalytic characteristics that stimulate the growth and development isolation of new strains. The volume narrates the challenging metagenomic approach with the isolation of the lipase gene, its cloning into Escherichia coli, culture of the recombinant bacteria, and extraction and assessment of the lipase enzyme.Lipase-producing bacteria have been found in different habitats, such as industrial wastes, vegetable oil processing factories, dairy plants, and soils contaminated with oil and oil seeds among others. This volume is the effort of the authors to document the scientific findings carried out over the last eight years in the area of un-culturable soil microorganisms. The book presents the physicochemical features of lipases and their specific applications in different commercial industries. The in-depth study looks at metagenomics for lipases from all angles and provides a truly informative resource. It describes the biochemical characterization of lipase enzymes with the high activity in the presence of 1% tributyrin. The book also highlights the maximum activity of the enzyme at temperature 37 C and pH 7.5 in the presence of the divalent cations Ca2+, Mn2+, Zn2+ and Fe2+. CTAB, gum arabic, NaCl and organic solvents like ethanol, 1-propanol, acetone, acetonitrile, glycerol and DMSO.A wide review has been presented in the book on lipase enzymes purified from a large collection of microbes present in soil, seawater, waste-dumping sites, animal systems (including human beings), and the atmosphere. Stability of enzymes over changing environments of the industry is indeed a big issue, and the book deals at length with the changing temperatures and pH and metal ion concentrations. The book also highlights the antifungal and antibacterial activity of the lipase enzyme."--Provided by publisher. |
| Contents | Application of lipases -- Metagenomics and unculturable bacteria -- Accessing metagenomics -- Metagenomics for lipase -- Functional approach for metagenomic library construction -- Ove rexpression of recombinant protein -- Biochemical characterization of purified lipase -- Genomic study of culture dependent bacteria -- Genomic study of culturable bacteria -- Microbial assay of culture supernatant containing crude lipase. |
| Subject | BIOCHEMISTRY. LIPASE. Metagenomics. |
| Multimedia |