{"text_format":"2","workbook":"xls","n_sheets":1,"sheets":["report2"],"not_rendered":{"charts":0,"images":0,"macros":0,"external_links":1,"defined_names":1,"comments":0,"pivot_tables":0},"unopened":[],"bounds":{"document_bytes":16777216,"sheet_cells":100000,"run_cost":"one","rows_first":2000,"rows_last":500,"rows_between":2000,"halvings":0,"cell_chars":16384,"cell_head_chars":4096},"cells_cut":0,"cells_raw":0,"read":"whole","date_system":"1900","formulas":"cached_only"}

{"sheet":"report2","index":0,"n_rows":25,"n_cols":5,"rows_kept":25,"cut":false,"hidden":false,"merged":[[0,2,0,3],[0,4,0,5],[1,2,1,3],[1,4,1,5],[2,2,2,3],[3,2,3,3],[4,2,4,3],[5,2,5,3],[6,2,6,3],[8,2,8,3],[9,2,9,3],[11,2,11,3],[12,2,12,3],[16,2,16,3]],"flags":["formulas_cached_only"]}
[null,"1.","Record Nr.",null,"UNINA9910959968403321"]
[null,null,"Titolo",null,"Lipase : functions, synthesis and role in disease / / Hamdi Sassi, Sofien Cannamela, editors"]
[null,null,"Pubbl/distr/stampa",null,"New York, : Nova Biomedical, Nova Science Publishers, c2012"]
[null,null,"ISBN",null,"1-62081-394-7"]
[null,null,"Edizione",null,"[1st ed.]"]
[null,null,"Descrizione fisica",null,"1 online resource (237 p.)"]
[null,null,"Collana",null,"Biochemistry research trends"]
[{"$nulls":4},"Biotechnology in agriculture, industry and medicine"]
[null,null,"Disciplina",null,"572.757"]
[null,null,"Soggetti",null,"Lipase - Industrial applications"]
[{"$nulls":4},"Lipase - Therapeutic use"]
[null,null,"Lingua di pubblicazione",null,"Inglese"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,null,"Note generali","Description based upon print version of record."]
[null,null,null,"Nota di bibliografia","Includes bibliographical references (p. 207-210) and index."]
[null,null,"Nota di contenuto",null,"Intro -- LIPASE -- LIPASE -- CONTENTS -- PREFACE -- ACQUISITION OF NEW PROPERTIES UNDER THE ACTION OF LIPASES AS A BIOTECHNOLOGICAL TOOL -- ABSTRACT -- 1. INTRODUCTION -- 2. LIPASE-CATALYZED MODIFICATION OF NATURAL PRODUCTS -- 2.1. Lipase-Catalyzed Production of Lysophospholipids -- A. Natural Sources of Phospholipids -- B. Lipase-Mediated Production of LPLs -- C. Characterization of Produced LPLs -- 2.2. Lipase-Catalyzed Synthesis of Waxes -- A. What Is Wax? -- B. Ester Composition of Waxes -- C. Wax Ester Production -- 3. LIPASE-CATALYZED SYNTHESIS OF NEW DERIVATIVES -- 3.1. Lipase-Catalyzed Synthesis of Triglycerides in Solvent Free Media -- A. Triolein Synthesis -- B. Synthesis of Medium Chain Triglycerides (MCT) -- C. Synthesis of N-3 Rich Triglycerides -- D. Trierucin Synthesis -- E. TG Synthesis: Effect of Chain Length and Unsaturation -- 3.2. Lipase-Catalyzed Synthesis of Fatty Acid Sugar Esters (FASEs) -- A. Effect of the Initial Fatty Acid Concentration -- B. Effect of the Initial Fructose Concentration -- C. Effect of the Fatty Acid Chain Length -- D. Effect of the Water Content -- E. Effect of the Initial Hydrophobicity -- 3.3. Lipase-Catalyzed Synthesis of Polyphenol Derivatives -- A. Effect of the Polyphenol Structure -- B. Effect of the Solvent -- C. Effect of the Acyl Donor -- E. Effect of Temperature and Reduced Pressure -- CONCLUSION -- REFERENCES -- SYNTHESIS OF ACYL SACCHARIDES AND ASCORBATES USING IMMOBILIZED LIPASE IN AN ORGANIC SOLVENT AND THEIR FUNCTIONALITIES -- ABSTRACT -- 1. INTRODUCTION -- 2. FACTORS AFFECTING THE REACTION EQUILIBRIUM OF LIPASE-CATALYZED "]
[{"$nulls":4},"CONDENSATION -- 2.1. Equilibrium Constants for the Lipase-Catalyzed Synthesis  of Acyl Hexoses -- 2.2. Effect of the Solvent on the Reaction Equilibrium in Tertiary Alcohol and Nitrile -- 2.3. Addition of Desiccant."]
[{"$nulls":4},"2.4. Improvement of the Product Concentration by the Use  of a Sugar Derivative -- 3. KINETICS FOR THE LIPASE-CATALYZED CONDENSATION -- 3.1. Reactivity of Substrates for the Lipase-Catalyzed Condensation -- 3.2. Kinetics of the Lipase-Catalyzed Condensation of Fatty Acid  and Alkyl Glucoside -- 3.3. Thermostability of Immobilized Lipase in 1-Alcohol -- 4. CONTINUOUS OR SEMI-CONTINUOUS REACTOR SYSTEMS  FOR LIPASE-CATALYZED CONDENSATION -- 4.1. Continuous Reactor Systems of Plug Flow Type -- 4.2. Continuous Production of Acyl Ascorbate by a Continuous  Stirred Tank Reactor -- 4.3. Semi-Continuous Production of Kojic Acid Ester -- 5. FUNCTIONALITIES OF THE PRODUCTS -- 5.1. Surfactant Properties of Acyl Saccharides, Ascorbates  and Sugar Alcohols -- 5.2. Bacteriostatic Activities of Acyl Saccharides and Sugar Alcohols -- 5.3. Antioxidative Properties of Acyl Ascorbates and Alkyl Ferulates -- 5.4. Oxidation of Linoleoyl Residue of its Trehalose Ester in a Micelle System -- 5.5. Stability of Acyl Ascorbates -- ACKNOWLEDGMENTS -- REFERENCES -- SOLVENT-FREE BIOCATALYTIC SYNTHESIS OF POLYGLYCEROL POLYRICINOLEATE (PGPR) USING IMMOBILISED CANDIDA RUGOSA  AND RHIZOPUS ARRHIZUS LIPASES -- ABSTRACT -- 1. INTRODUCTION -- 2. MATERIALS AND METHODS -- 2.1. Materials -- 2.1.1. Enzymes -- 2.1.2. Substrates -- 2.1.3. Immobilisation Reagents and Activators -- 2.1.4. Immobilisation Supports -- 2.2. Methods -- 2.2.1. Immobilisation by Covalent Binding -- 2.2.2. Immobilisation by Physical Adsorption -- 2.2.3. Synthesis of Polyricinoleic Acid, PR -- 2.2.3.1. With Free Candida rugosa Lipase -- Preliminary Studies -- Open Air Reactor Experiments -- 2.2.3.2. With Immobilised Candida rugosa Lipase vv -- Open Air Reactor Experiments -- Vacuum Reactor Experiments -- 2.2.4. Synthesis of Polyglycerol Polyricinoleate, PGPR -- 2.2.4.1. With Free Lipase -- Selection Studies."]
[{"$nulls":4},"Open Air Reactor Experiments -- 2.2.4.2. With Immobilised Lipase -- Open Air Reactor Experiments -- Vacuum Reactor Experiments -- 2.2.5. Measurement of the Reaction Extension -- 2.2.6. Measurement of the Water Content -- 2.2.7. Recovery of the Immobilised Derivative -- 3. RESULTS AND DISCUSSION -- 3.1. Condensation of Ricinoleic Acid to Obtain Polyricinoleic Acid  by Candida rugosa Lipase -- 3.1.1. Preliminary Studies with Free Candida rugosa Lipase -- 3.1.2. Immobilisation of Candida rugosa Lipase -- 3.1.2.1. Choice of the Immobilised Derivative -- 3.1.2.2. Choice of Support Activator -- 3.1.2.3. Influence of Enzyme Concentration and pH -- 3.1.2.4. Effect of Mixing in the Immobilisation Process -- 3.1.2.5. Comparison of Free and Immobilised Lipase -- 3.1.2.6. Reuse of the Immobilised Derivative -- 3.1.3. Production of Polyricinoleic Acid with Immobilised Candida rugosa Lipase -- 3.1.3.1. Influence of the Amount of Enzyme -- 3.1.3.2. Influence of the Temperature -- 3.1.3.3. Influence of the Initial Water Content -- 3.1.3.3. Influence of Pressure and Water Content -- 3.2. Esterification of Polyricinoleic Acid with Polyglycerol to Obtain PGPR -- 3.2.1. Screening and Selection of Lipases for the Enzymatic Production of PGPR -- 3.2.1.1. Selection of Lipases -- 3.2.1.2. Immobilisation of the Selected Lipases -- 3.2.2. Synthesis of Polyglycerol Polyricinoleate with Rhizopus arrhizus Lipase -- 3.2.2.1. Influence of Initial Water Content -- 3.2.2.2. Influence of Temperature -- 3.2.2.3. Influence of the Amount of Enzyme -- 3.2.2.4. Lipase Immobilisation and Comparison with Free Enzyme -- 3.2.2.5. Reuse of the Immobilised Derivative -- 3.2.2.6. Obtaining PGPR in the Vacuum Reactor -- CONCLUSION -- ACKNOWLEDGMENTS -- REFERENCES -- "]
[{"$nulls":4},"FUNGAL LIPASES: VERSATILE TOOLS  FOR BIOCATALYSIS -- ABSTRACT -- INTRODUCTION -- ESSENTIAL CHARACTERISTICS OF FUNGAL LIPASES."]
[{"$nulls":4},"BIOTECHNOLOGICAL APPLICATIONS OF FUNGAL LIPASES -- 1. Food Industry -- Fats and Oil Industry -- Dairy Industry -- Flavor Production -- Bakery Industry -- 2. Detergent Industry -- 3. Agrochemicals -- 4. Biopolymers -- 5. Biodiesel Production -- 6. Environmental Management -- 7. Biomedical Applications -- 8. Cosmetics -- 9. Biosensors -- 10. Pulp and Paper Industry -- 11. Textile Industry -- 12. Leather Industry -- REFERENCES -- SECRETED PHOSPHOLIPASE A2 INHIBITORS FROM CYNARA CARDUNCULUS L.AND ALOE VERA EXTRACTS AS POTENTIAL THERAPEUTIC DRUG FOR INFLAMMATORY DISEASES -- ABSTRACT -- INTRODUCTION -- MATERIAL AND METHODS -- Enzymes and Reagents -- Extractions -- Fractionation of Compounds -- Assay of sPLA2 Activity -- Total Phenols Determination -- Assays of Antioxidant Activity -- DPPH Radical Scavenging Assay -- Reducing Power Assay -- Statistical Analysis and Correlation Study -- RESULTS -- Extraction Yields of Cynara Cardunculus and Aloe Vera -- Total Phenolic Contents of Aloe Vera -- Antioxidant Activity of Aloe Vera -- DPPH Radical Scavenging Activity -- Reducing Power Assay -- Evaluation of the PLA2 Inhibitory Effect -- Leaves of Cynara Cardunculus -- Stems of Cynara Cardunculus L. -- Leaf Skin of Aloe Vera -- Correlation Significance Study -- DISCUSSION -- Anti-Inflammatory Activity of Cynara Cardunculus L -- Anti-Inflammatory Activity of Aloe Vera -- REFERENCES -- LIPOPROTEIN LIPASE ACTIVITY IN SICKLE CELL NEPHROPATHY: A REVIEW -- ABSTRACT -- INTRODUCTION -- RENAL CHANGES IN SICKLE CELL DISEASE -- RATE OF SYNTHESIS OF LIPOPROTEIN LIPASE -- Subclass -- EFFECT OF RACE, ENVIRONMENT AND SEX  ON LIPOPROTEIN LIPASE -- Effect of Race and Environment -- Effect of Sex -- LIPOPROTEIN LIPASE ACTIVITY IN PATIENTS  WITH SICKLE CELL DISEASE -- EFFECTS OF ALTERED LIPOPROTEIN LIPASE ON LIPOPROTEINS  IN SICKLE CELL NEPHROPATHY."]
[{"$nulls":4},"PATHOPHYSIOLOGY OF DYSLIPIDAEMIA  IN CHRONIC KIDNEY DISEASE -- EFFECT OF INFLAMMATION AND ANTIOXIDANTS ON LIPOPROTEIN LIPASE IN SICKLE CELL DISEASE -- POLYMORPHISM IN GENES THAT CODE FOR LIPOPROTEIN LIPASE AND ASSOCIATION WITH LIPID METABOLISM -- REFERENCES -- LIPASES IN THE PHARMACEUTICAL INDUSTRY:  AN APPROACH FOR RACEMIC DRUGS -- ABSTRACT -- INTRODUCTION -- MICROBIAL LIPASES -- Production of Microbial Lipases -- Purification, Characterization and Immobilization of Microbial Lipases -- RACEMIC DRUGS -- General Aspects -- LIPASES ON RACEMIC DRUGS -- Hydrolysys Reactions -- Esterification Reactions -- Transesterification Reactions -- Amidation Reactions -- CONCLUSION -- REFERENCES -- YEAST CELL SURFACE DISPLAY OF LIPASES -- ABSTRACT -- INTRODUCTION -- DEVELOPED SYSTEMS FOR YEAST SURFACE DISPLAY OF PROTEINS -- C-Terminal System of Cell Surface Display -- N-Terminal System of Cell Surface Display -- LIPASE CELL SURFACE DISPLAY -- Display of Lip2 on the Cell Surface of Y. Lipolytica -- CONCLUSION -- ACKNOWLEDGMENTS -- REFERENCES -- MICROBIAL LIPASES AND THEIR APPLICATIONS IN STRUCTURED LIPIDS -- ABSTRACT -- INTRODUCTION -- MICROBIAL LIPASES -- STRUCTURED LIPIDS -- Generic Aspects -- BIOCHEMICAL AND NUTRITIONAL ASPECTS OF STRUCTURED LIPIDS -- OBTAINING STRUCTURED LIPIDS USING MICROBIAL LIPASES -- CONCLUSION -- REFERENCES -- INDEX."]
[null,null,null,"Sommario/riassunto","Lipases are ubiquitous enzymes which catalyze the hydrolysis of triacylglycerols to glycerols and free fatty acids. Due to their characteristics of enantioselectivity and regioselectivity and stability in "]
[{"$nulls":4},"organic solvents, they have gained importance in industrial applications. In this book, the authors examine the functions, synthesis and role in disease of lipases. Topics discussed include the action of lipases as a biotechnological tool; fungal lipases in biocatalysis; secreted phospholipase A2 inhibitors from cynara cardunculus L. and aloe vera extract as a potential therapeutic drug for inflammatory diseases; lipoprotein lipase activity in sickle cell nephropathy; lipases in the pharmaceutical industry; and yeast cell surface display of lipases."]