LEADER 01667oam 2200505zu 450 001 9910464717903321 005 20210721055107.0 035 $a(CKB)3710000000114920 035 $a(SSID)ssj0001415912 035 $a(PQKBManifestationID)12005005 035 $a(PQKBTitleCode)TC0001415912 035 $a(PQKBWorkID)11353378 035 $a(PQKB)11397592 035 $a(MiAaPQ)EBC1757911 035 $a(EXLCZ)993710000000114920 100 $a20160829d2014 uy 101 0 $aeng 181 $ctxt 182 $cc 183 $acr 200 10$aSustainable luxury and social entrepreneurship : stories from the pioneers 210 31$a[Place of publication not identified]$cGreenleaf Publishing$d2014 300 $aBibliographic Level Mode of Issuance: Monograph 311 $a1-78353-063-4 311 $a1-78353-064-2 606 $aSocial entrepreneurship$xEnvironmental aspects 606 $aLuxury goods industry 606 $aManagement$2HILCC 606 $aBusiness & Economics$2HILCC 606 $aManagement Styles & Communication$2HILCC 615 0$aSocial entrepreneurship$xEnvironmental aspects 615 0$aLuxury goods industry 615 7$aManagement 615 7$aBusiness & Economics 615 7$aManagement Styles & Communication 676 $a658.4/08 700 $aGardetti$b Miguel Ángel$0916036 702 $aGirâon$b Marâia Eugenia 702 $aGardetti$b Miguel âAngel 702 $aGirón$b María Eugenia 801 0$bPQKB 906 $aBOOK 912 $a9910464717903321 996 $aSustainable luxury and social entrepreneurship : stories from the pioneers$92260543 997 $aUNINA LEADER 04485nam 2200409 450 001 9910647242603321 005 20230327122712.0 010 $a3-0365-6266-4 035 $a(CKB)5680000000300001 035 $a(NjHacI)995680000000300001 035 $a(EXLCZ)995680000000300001 100 $a20230327d2023 uy 0 101 0 $aeng 135 $aur||||||||||| 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$aBiocatalytic applications in biotechnology /$fedited by Emmanuel M Papamichael, Panagiota-Yiolanda Stergiou 210 1$a[Place of publication not identified] :$cMDPI - Multidisciplinary Digital Publishing Institute,$d[2023] 210 4$d©2023 215 $a1 online resource (244 pages) 311 $a3-0365-6265-6 327 $aAbout the Editors -- Regioselective Hydroxylation of Rhododendrol by CYP102A1 and Tyrosinase -- Exploring Metagenomic Enzymes: A Novel Esterase Useful for Short-Chain Ester Synthesis -- Counterbalance of Stability and Activity Observed for Thermostable Transaminase from Thermobaculum terrenum in the Presence of Organic Solvents -- Kinetic Analysis of the Lipase-Catalyzed Hydrolysis of Erythritol and Pentaerythritol Fatty Acid Esters: A Biotechnological Application for Making Low-Calorie Healthy Food Alternatives -- Influence of Carrier Structure and Physicochemical Factors on Immobilisation of Fungal Laccase in Terms of Bisphenol A Removal -- Estimating the Product Inhibition Constant from Enzyme Kinetic Equations Using the Direct Linear Plot Method in One-Stage Treatment -- Polymer-Assisted Biocatalysis: Polyamide 4 Microparticles as Promising Carriers of Enzymatic Function -- Engineering of Bifunctional Enzymes with Uricase and Peroxidase Activities for Simple and Rapid Quantification of Uric Acid in Biological Samples -- Rigorous Model-Based Design and Experimental Verification of Enzyme-Catalyzed Carboligation under Enzyme Inactivation -- Conversion of Shrimp Head Waste for Production of a Thermotolerant, Detergent-Stable, Alkaline Protease by Paenibacillus sp. -- Catalytic Activities of Multimeric G-Quadruplex DNAzymes -- Biotransformation with a New Acinetobacter sp. Isolate for Highly Enantioselective Synthesis of a Chiral Intermediate of Miconazole -- Enhancing Enzymatic Properties of Endoglucanase I Enzyme from Trichoderma Reesei via Swapping from Cellobiohydrolase I Enzyme -- Bioproduction of Isoprenoids and Other Secondary Metabolites Using Methanotrophic Bacteria as an Alternative Microbial Cell Factory Option: Current Stage and Future Aspects -- Microbial Phosphotriesterase: Structure, Function, and Biotechnological Applications. 330 $aAt present, the increasing demand for novel biotechnological products is supported through the continuous development of biocatalytic applications. As a consequence, the progress of research regarding enzymatic catalysis in aqueous, non-aqueous, organic (polar or non-polar), and/or non-solvent media is decisive. Experimental design methods, which also may comprise in silico studies, the design of specific reactors and conditions, the reactions of significant chemical and/or biochemical processes that are relevant to industrial production, enzyme kinetic methods, the investigation of enzymatic mechanisms and the use of immobilized enzymes and/or microbial cells on various inert matrices, are all useful. A plethora of enzymes of several classes, which may potentially be used as biocatalysts in biotechnological applications, are available. Among these enzymes, the more common are oxidoreductases (laccase, catalase, glucose oxidase, etc.), hydrolases (amylases, lipases, proteases, amidases, cellulases, esterases, etc.), isomerases (epimerases, topoisomerases, mutases, etc.), and others. By means of the aforementioned biocatalysts and the utilization of specific biotechnological methods, important, cost-effective, sustainable, and environmentally friendly processes have been applied for the synthesis and/or the conversion of a huge number of market-required products. 606 $aBiotechnology 606 $aBiocatalysis 615 0$aBiotechnology. 615 0$aBiocatalysis. 676 $a660.6 702 $aPapamichael$b Emmanuel M 702 $aStergiou$b Panagiota-Yiolanda 801 0$bNjHacI 801 1$bNjHacl 906 $aBOOK 912 $a9910647242603321 996 $aBiocatalytic Applications in Biotechnology$93016397 997 $aUNINA LEADER 03198nam 2200649 450 001 9910787751503321 005 20230803031914.0 010 $a1-61251-328-X 035 $a(CKB)2670000000492218 035 $a(EBL)1474205 035 $a(OCoLC)858159633 035 $a(SSID)ssj0001041296 035 $a(PQKBManifestationID)11572901 035 $a(PQKBTitleCode)TC0001041296 035 $a(PQKBWorkID)11027101 035 $a(PQKB)11081277 035 $a(MiAaPQ)EBC1474205 035 $a(DLC) 2013037129 035 $a(Au-PeEL)EBL1474205 035 $a(CaPaEBR)ebr10821100 035 $a(CaONFJC)MIL686053 035 $a(EXLCZ)992670000000492218 100 $a20130807h20132013 uy| 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 10$aProceed to Peshawar $ethe story of a U.S. Navy intelligence mission on the Afghan border, 1943 /$fGeorge J. Hill, Captain, Medical Corps, USNR (Ret.) 210 1$aAnnapolis, MD :$cNaval Institute Press,$d[2013] 210 4$d©2013 215 $a1 online resource (272 p.) 300 $aDescription based upon print version of record. 311 $a1-322-54771-8 311 $a1-61251-280-1 320 $aIncludes bibliographical references and index. 330 $a"Proceed to Peshawar is a story of adventure in the Hindu Kush Mountains and of a previously untold military and naval intelligence mission during World War II by two American officers along 800 miles of the Durand Line, the porous border between Afghanistan and Pakistan. They passed through the tribal areas and the princely states of the North-West Frontier Province, and into Baluchistan. This appears to be the first time that any American officials were permitted to travel for any distance along either side of the Durand Line. Many British political and military officers believed that India would soon be free, and that the Great Game between Russia and Britain in the nineteenth and early twentieth centuries would then come to an end. Some of them thought that the United States should, and would, assume Britain's role in Central Asia, and they wanted to introduce America to this ancient contest. "--$cProvided by publisher. 517 3 $aStory of a U.S. Navy intelligence mission on the Afghan border, 1943 606 $aWorld War, 1939-1945$xMilitary intelligence$zUnited States 606 $aMilitary intelligence$zUnited States$xHistory$y20th century 606 $aIntelligence officers$zUnited States$vBiography 607 $aKhyber Pakhtunkhwa (Pakistan)$xHistory, Military 607 $aKhyber Pakhtunkhwa (Pakistan)$xDescription and travel 607 $aKhyber Pakhtunkhwa (Pakistan)$xHistory$y20th century 615 0$aWorld War, 1939-1945$xMilitary intelligence 615 0$aMilitary intelligence$xHistory 615 0$aIntelligence officers 676 $a940.54/8673 686 $aHIS027100$aHIS027000$aHIS027150$2bisacsh 700 $aHill$b George J.$f1932-$01525932 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910787751503321 996 $aProceed to Peshawar$93769962 997 $aUNINA