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Agricultural Biocatalysis: Enzymes in Agriculture and Industry [Kõva köide]

Edited by (Bayer AG, Germany), Edited by (Kobe University, Japan)
  • Formaat: Hardback, 536 pages, kõrgus x laius: 229x152 mm, kaal: 621 g, 30 Tables, black and white; 30 Line drawings, color; 42 Line drawings, black and white; 6 Halftones, color; 7 Halftones, black and white; 36 Illustrations, color; 49 Illustrations, black and white
  • Ilmumisaeg: 22-Dec-2022
  • Kirjastus: Jenny Stanford Publishing
  • ISBN-10: 9814968471
  • ISBN-13: 9789814968478
Teised raamatud teemal:
Agricultural Biocatalysis: Enzymes in Agriculture and IndustrySuurem pilt
  • Formaat: Hardback, 536 pages, kõrgus x laius: 229x152 mm, kaal: 621 g, 30 Tables, black and white; 30 Line drawings, color; 42 Line drawings, black and white; 6 Halftones, color; 7 Halftones, black and white; 36 Illustrations, color; 49 Illustrations, black and white
  • Ilmumisaeg: 22-Dec-2022
  • Kirjastus: Jenny Stanford Publishing
  • ISBN-10: 9814968471
  • ISBN-13: 9789814968478
Teised raamatud teemal:
Püsilink: https://www.kriso.ee/db/9789814968478.html
Märksõnad:
Agricultural biocatalysis is of immense scientific interest nowadays owing to its increasing importance in the efforts for more sustainable agriculture while optimizing environmental impacts. Plant compatibility is essential for developing eco-friendly and sustainable microbial products. Therefore, our search for novel technologies ought to be in the foreground, for which a thorough understanding of biochemical processes, application of agricultural enzymes, traits, and viruses get the highest priority.

Volumes 8 to 10 in this series compile the recent research on agricultural biocatalysis by interdisciplinary teams from international institutes for chemistry, biochemistry, biotechnology, and materials and chemical engineering, who have been investigating agricultural-biocatalytic topics related to biochemical conversions or bioremediation, and modern biological and chemical applications exemplified by the use of selected and highly innovative agricultural enzymes, traits, and viruses. The editors are prominent researchers in agrochemistry and theoretical biophysical chemistry, and these three volumes are useful references for the students and researchers in the fields of agrochemistry, biochemistry, biology, biophysical chemistry, natural product chemistry, materials, and drug design. Volume 9 covers the research on plant and soil enzymes, herbicide tolerant traits, biochemical conversions, including aspects from bioremediation, plant viruses, and evaluation of the agricultural enzymes market.
Preface xv
Part I Agricultural Enzymes Market
1 Metagenomics as a Tool to Isolate New Enzymes for Application in Hydrolysis and Synthesis Reactions: The Case of Lipolytic Enzymes
3(36)
Roa'o Cuaspa Ropai'n
Robson Carlos Alnoch
Patricia Gruening de Mattos
Janaina Marques de Almeida
David Alexander Mitchell
Nadia Krieger
1.1 Introduction
4(2)
1.2 Metagenomics as an Enzyme Prospecting Tool
6(13)
1.3 Functional Screening in a Metagenomic Library
19(2)
1.4 Sequence-Based Screening in a Metagenomic Library
21(2)
1.5 Lipolytic Enzymes Isolated from Metagenomic Libraries
23(1)
1.6 The Lipases LipC12, LipG9, and LipMF3: A Case Study
24(7)
1.7 Conclusions
31(8)
2 Plant Pectin Methylesterase: An Insight into Agricultural and Industrial Applications
39(20)
Zeba Khan
Rakesh Srivastava
Sumit K. Bag
Praveen C. Verma
2.1 Introduction
40(1)
2.2 Pectin Methylesterases Classification
41(4)
2.3 Pectin Methylesterases: An Insight into Their Functions
45(4)
2.3.1 Role of PMEs in Different Aspects of Plant Development
46(3)
2.4 Role of PMEs in Plant Defense-Related Mechanism
49(2)
2.5 Agriculture and Industrial Applications of PMEs
51(2)
2.6 Conclusion
53(6)
3 Induced Polyphenol Oxidases Are Associated with Laccase Activity in Different Genotypes of Resistant Chickpea Cultivars Infected by Fusarium oxysporm f.sp. ciceris and Salicylic Acid
59(16)
Shivashankar Gayatridevi
Kuruba Sreeramulu
Senigala K. Jayalakshmi
3.1 Introduction
60(2)
3.2 PPO and Laccase Activity
62(2)
3.3 Detection of PPO and Laccase Isozymes in Native Page
64(5)
3.4 Conclusion
69(6)
Part II Plant Enzymes
4 Classification and Evolutionary Landscape of Acid Phosphatase-Encoding Gene Families in Plants
75(42)
Amir Feizi
Mohammad Ali Malboobijavad Zamani
Tahmineh Lohrasebi
Shahrokh Kazempour-Osaloo
4.1 Introduction
76(3)
4.2 Plant APase Sequences Retrieval and Comparison
79(10)
4.3 Sequence Alignments, Clustering, and Phylogenetic Analysis
89(1)
4.4 PAP Family
90(7)
4.4.1 PAP I Subfamily
93(2)
4.4.2 PAP II Subfamily
95(1)
4.4.3 PAP III Subfamily
96(1)
4.4.4 PAP IV Subfamily
96(1)
4.4.5 PAP V Subfamily
96(1)
4.5 Halo Acid Dehalogenases (HADJ-Related APase Family
97(3)
4.5.1 HRPI Subfamily
97(3)
4.5.2 HRP II Subfamily
100(1)
4.6 Phospholipid Phosphatase (PLP) Family
100(2)
4.7 Histidine Acid Phosphatase Family
102(2)
4.8 Protein E (SurE)-Related Acid Phosphatase Family
104(2)
4.9 Structural Comparisons of APase Families
106(2)
4.10 Concluding Remarks
108(9)
5 Acid Phosphatases Roles in Plant Performance
117(42)
Mohammad Ali Malboobi
Mohammad Sadegh Sabet
Katayoun Zamani
Tahmineh Lohrasebi
Zahra Fathi
Javad Zamani
5.1 Introduction
118(1)
5.2 Phosphate Ion and Its Significance
119(2)
5.3 Stepwise Plant Response to Available Pi
121(1)
5.4 APases Types and Functions
122(5)
5.4.1 Purple Acid Phosphatase (PAP] Family
123(1)
5.4.2 Haloacid Dehalogenase (HAD)-Related Acid Phosphatase (HRP) Family
124(1)
5.4.3 Phospholipid Phosphatases (PLP) Family
125(1)
5.4.4 Histidine Acid Phosphatase (HAP) Family
126(1)
5.4.5 SurE-Related Acid Phosphatase (SAP) Family
127(1)
5.5 Multiple Isoforms and Broad Substrates Range of APases
127(5)
5.6 Tissue-Specific Expression of APases
132(3)
5.7 Responsiveness of APases to Pi Status
135(2)
5.8 Roles of APases in Pi Homeostasis
137(3)
5.9 APases Responsive to Other Stresses
140(1)
5.10 Interplay between APases to Keep Pi Homeostasis
141(4)
5.11 Concluding Remarks
145(14)
6 Superoxide Dismutases in Plants: New Insights into Regulation and Functioning
159(66)
Ravi Prakash Sanyal
Abiraami T. V.
Sabiha Perween
Satish B. Verulkar
Hari S. Misra
Ajay Saini
6.1 Introduction
160(1)
6.2 Impact of Great Oxygenation Event (GOE) on Cellular Metabolism
161(1)
6.3 Reactive Species: Generation, Molecular Targets, and Scavenging
162(6)
6.3.1 Superoxide Radical (O2-)
166(1)
6.3.2 Hydrogen Peroxide (H2O2)
166(1)
6.3.3 Hydroxyl Radical (OH)
166(1)
6.3.4 Singlet Oxygen (1O2)
167(1)
6.3.5 Other Reactive Species (RNS, RCS, RSS)
167(1)
6.4 Reactive Species and Important Sites of Generation in Plants
168(2)
6.5 Reactive Species: Detrimental and Beneficial Effects
170(2)
6.6 Cellular Antioxidant Defense Systems
172(4)
6.6.1 Nonenzymatic Antioxidants
173(1)
6.6.2 Enzymatic Antioxidant Defense System
174(2)
6.7 Multiple SOD Isoforms and Their Need in Biological Systems
176(1)
6.8 Nickel Superoxide Dismutase (Ni SOD)
177(1)
6.9 Cambialistic Superoxide Dismutase (Fe/Mn SOD)
178(1)
6.10 Iron Superoxide Dismutase (Fe SOD)
179(4)
6.11 Manganese Superoxide Dismutase (Mn SOD)
183(2)
6.12 Copper Zinc Superoxide Dismutases (CuZn SODs)
185(3)
6.13 Dynamics of Regulation and Functioning of SODs
188(15)
6.13.1 Cis Elements-Mediated Regulation ofSODs
188(3)
6.13.2 MicroRNA miR398-Mediated Regulation of CuZn SODs
191(1)
6.13.3 Alternative Splicing in Regulation and Functioning of SODs
192(3)
6.13.4 Copper Chaperone for Superoxide Dismutase (CCS)-Mediated Regulation and Functioning of CuZn SODs
195(3)
6.13.5 Role of Posttranslational Modifications (PTMs) in SOD Functioning
198(3)
6.13.6 Genome Duplication-Mediated Copy Number Increase of Plant SOD Genes
201(2)
6.14 Stress Responsiveness of SODs
203(1)
6.15 Biotechnological Applications of SODs for Stress Tolerance Enhancement
204(4)
6.16 Industrial Applications of Plant SODs
208(1)
6.17 Conclusions
208(17)
7 Peroxisomes from Higher Plants and Their Metabolic Diversity
225(20)
Francisco J. Corpas
Jose M. Palma
7.1 Introduction
226(2)
7.2 Photorespiration
228(1)
7.3 Fatty Acids β-Oxidation, Glyoxylate Cycle, and Auxin Metabolism
229(2)
7.4 Biosynthesis of Jasmonic Acid and Polyamine Metabolism
231(1)
7.5 Metabolism of ROS and RNS
232(3)
7.6 Pexophagy
235(1)
7.7 Conclusions and Further Perspectives
235(10)
Part III Herbicide-Tolerant Traits
8 Oxygenase Enzymes for Agricultural Biotechnology Applications
245(24)
Clayton T. Larue
8.1 Introduction
246(3)
8.2 Discovery and Early Development of Herbicide Tolerance Traits
249(4)
8.3 Dioxygenases for FOP and 2,4-D Tolerance Traits
253(4)
8.4 Monooxygenase Enzyme for Dicamba Tolerance
257(3)
8.5 Dioxygenase Enzyme for HPPD Inhibitor Tolerance
260(2)
8.6 Conclusion
262(7)
Part IV Plant Viruses
9 PI Leader Proteinases from the Potyviridae Family
269(34)
Fabio Pasin
Hongying Shan
9.1 Introduction
270(5)
9.2 PI Diversity of the Potyviridae Genomes
275(1)
9.3 Structural Properties and Proteolytic Activity of P1
276(2)
9.4 PI Proteins as Viral Suppressors of RNA Silencing
278(2)
9.5 PI Proteins as Host-Range and Symptom Determinants
280(7)
9.6 Additional PI Functions
287(1)
9.7 Biotechnologies of PI Proteinases
288(2)
9.8 Conclusions
290(13)
Part V Soil Enzymes
10 Soil Enzymes: Distribution, Interactions, and Influencing Factors
303(32)
Sesan Abiodun Aransioia
Femi Afolabi
Femi Joseph
Naga Raju Maddela
10.1 Introduction
304(1)
10.2 Source, Distribution, and Abundance of Soil Enzymes
305(5)
10.3 Ecological Stoichiometry of Plant-Soil-Enzyme Interactions
310(4)
10.3.1 Role of Plant in Soil Health
311(1)
10.3.2 Plant-Soil-Enzyme Relationship and Soil Health
312(1)
10.3.2.1 Soil urease
313(1)
10.3.2.2 Soil invertase
314(1)
10.3.2.3 Soil phosphatase
314(1)
10.4 Soil Chemical Properties Versus Soil Enzyme Activities
314(3)
10.5 Impact of Anthropogenic Factors on Soil Enzyme Activities
317(8)
10.6 Conclusions
325(10)
11 Carbon-, Nitrogen-, Phosphorus-, and Sulfur-Cycling Enzymes and Functional Diversity in Agricultural Systems
335(32)
Avijit Ghosh
Ranjan Paul
Abhijit Sarkar
M. C. Manna
Sudeshna Bhattacharjya
Khurshid Alam
Sourav Choudhury
Phthusayak Mondal
11.1 Introduction
336(1)
11.2 Carbon-Cycling Enzymes and Their Mechanisms
337(7)
11.2.1 Amylase
337(1)
11.2.2 jS-Glucosidase
338(1)
11.2.3 Cellulase and Hemicellulase
339(2)
11.2.4 Ligninase
341(1)
11.2.5 Invertase
342(1)
11.2.6 Laccase
342(1)
11.2.7 Pectinase
342(2)
11.3 Nitrogen-Cycling Enzymes and Their Mechanisms
344(1)
11.3.1 Soil Protease
344(1)
11.3.2 Urease
344(1)
11.3.3 Chitinase
345(1)
11.4 Phosphorus-Cycling Enzymes and Their Mechanisms
345(8)
11.4.1 Phosphatase Enzymes
345(3)
11.4.2 Phosphomonoesterases
348(1)
11.4.3 Phosphodiesterases
349(1)
11.4.4 Phosphotriesterases
350(1)
11.4.5 Polyphosphates
351(2)
11.4.6 Phosphoamidase
353(1)
11.5 Sulfur-Cycling Enzymes and Their Mechanisms
353(2)
11.5.1 Aryl Sulfatases
353(2)
11.6 Microbial Functional Diversity in Agrosystems
355(1)
11.7 Conclusions and Future Prospects
355(12)
Part VI Bioremediation
12 Bioremediation: Removal of Polycyclic Aromatic Hydrocarbons from Soil
367(46)
Zdenek Kosndf
Johanka Wernerovd
Petr Fruhbauer
Pavel Tlustos
12.1 Introduction
368(13)
12.1.1 General Description of Polycyclic Aromatic Hydrocarbons (PAHs]
368(3)
12.1.2 Basic Description of 16 Individual US EPA PAHs
371(4)
12.1.3 Sources of PAHs in the Environment
375(2)
12.1.4 Emissions of PAHs in the Environment
377(1)
12.1.5 Soil Contamination by PAHs
378(1)
12.1.6 Impact of PAHs on Animal and Human Health
379(2)
12.2 Conventional Remediation of Soils Contaminated by PAHs
381(1)
12.3 Bioremediation of Soil Contaminated by PAHs
382(21)
12.3.1 Phytoremediation of Soil Contaminated by PAHs
384(7)
12.3.2 Bacterial Remediation of Soil Contaminated by PAHs
391(4)
12.3.3 Mycoremediation of Soil Contaminated by PAHs
395(8)
12.4 Conclusions
403(10)
Part VII Biochemical Conversion
13 Enzymatic Saccharification of Lignocellulosic Biomass
413(58)
Madhavi Latha Gandla
Chaojun Tang
Carlos Martin
Leif J. Jonsson
13.1 Introduction
414(1)
13.2 Lignocellulosic Biomass
415(5)
13.3 Biodegradation of Lignocellulose in Nature
420(2)
13.4 Fungal Enzymes
422(19)
13.4.1 Glycoside Hydrolases
422(9)
13.4.2 Polysaccharide Lyases
431(3)
13.4.3 Carbohydrate Esterases
434(2)
13.4.4 Auxiliary Activities
436(3)
13.4.5 Associated Modules
439(2)
13.5 Bacterial Enzymes
441(2)
13.6 Determination of Cellulolytic Activity
443(2)
13.7 Biorefining of Lignocellulosic Feedstocks
445(3)
13.8 Pretreatment to Facilitate Enzymatic Saccharification
448(6)
13.9 Inhibition of Enzymatic Saccharification
454(1)
13.10 Process Configurations
455(4)
13.11 Future Outlook
459(12)
14 Biological Biorefineries Based on Orange Peel Wastes
471(44)
Alberto Garci'a-Martin
Itziar A. Escanciano
V. Martin-Dominguez
Alvaro Lorente-Arevalo
Jorge Garcia-Montalvo
Jesus Esteban
Juan M. Bolivar
Victoria E. Santos
Miguel Ladero
14.1 Introduction
472(4)
14.2 Upstream Processes in Biological Biorefineries from OPW
476(8)
14.2.1 Pretreatment of OPWs
476(5)
14.2.2 Enzymatic Saccharification of OPWs
481(3)
14.3 Biological Processes to Platform Chemicals and Materials
484(20)
14.3.1 Bioethanol and Superior Alcohols
484(3)
14.3.2 Gas Energy and Material Vectors from OPW
487(9)
14.3.3 Monomers and Other Organic Compounds
496(3)
14.3.4 Production of Enzymes from OPWs
499(3)
14.3.5 Biopolymers, Exopolysaccharides, and High Molecular Weight Active Ingredients
502(2)
14.4 Techno-Economic and Environmental Impact Studies
504(2)
14.5 Conclusions
506(9)
Index 515
Peter Jeschke gained his PhD in organic chemistry at the University of Halle-Wittenberg, Germany, after which he moved to Fahlberg-List Company, Germany, to pursue agrochemical research before moving to the Institute of Neurobiology and Brain Research, German Academy of Sciences. In 1989, he joined Bayer AG in animal health research and eight years later took a position in insecticide research, where he was a senior fellow in Research and Development, Pest Control Chemistry, Crop Science Division. Since 2011, he has been honorary professor at the Universität Düsseldorf, Germany. Prof. Jeschke is an associate editor for Pest Management Science (Society of Chemical Industry, UK) and also a member of the editorial advisory board for Ullmanns Encyclopedia of Industrial Chemistry (Wiley-VCH). Retired since 2022, he has authored more than 250 patent applications and publications.

Evgeni B. Starikov is a specialist in theoretical biophysical chemistry with nearly 40 years of professional experience. Currently, he is a freelance researcher at Chalmers University of Technology, Sweden, and Kobe University, Japan. Prof. Starikov has authored more than 100 articles and a monograph and co-edited two books. His current research interests include applications of thermodynamics.