| Description |
1 online resource |
| Series |
Biotechnology in agriculture, industry and medicine |
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Biotechnology in agriculture, industry and medicine series.
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| Contents |
UNIQUE ENZYMES OF ASPERGILLUS FUNGI USED IN JAPANESE BIOINDUSTRIES; LIBRARY OF CONGRESS CATALOGING-IN-PUBLICATION DATA; Contents; Preface; Chapter 1: Introduction; Chapter 2: The Third Active Site Residue of Aspartic Proteinase from Aspergillus is Essential for Trypsinogen Activation at Ph 3-4.5; 2.1. Aspartic Proteinase; 2.2. Aspergillopepsin I; 2.3. D76S-Aspergillopepsin I Abolished Trypsinogen Activation ; 2.4. Characterization of the S1 Subsite Specificity; Chapter 3: Engineering of Porcine Pepsin; 3.1. Pepsin |
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3.2. Alteration of S1 Substrate Specificity of Pepsin to Those of Fungal Aspartic ProteinaseChapter 4: Aorsin from Aspergillus Oryzae, a Novel Serine Proteinase with Trypsinogen Activating Specificity at Acidic Ph; 4.1. Sedolisin; 4.2. Aorsin From A. Oryzae; Chapter 5: Deuterolysin from Aspergillus, A Member of Aspzincin Family with a New Zinc-Binding Motif (HEXXH +); 5.1. DEUTEROLYSIN -- EXTREAMLY HEAT STABLE19 KDA ZN2+-PROTEASE -; 5.2. SPECIFICITY OF DEUTEROLYSIN; 5.3. CO-DEUTEROLYSIN; 5.4. PENICILLOLYSIN -- THERMOLABILE 19KDA ZN2+-PROTEASE |
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Chapter 6: Acid Carboxypeptidase from Aspergillus Saitoi6.1. Acid Carboxypeptidase; 6.2. Specificity of Acid Carboxypeptidase; 6.3. Cloning and Expression of Acid Carboxypeptidase Gene (CpdS) ; 6.4. Debittering of the Bitter Peptides; 6.5. A New High-Mannose Type N-Linked Oligosaccharide; 6.6. Carbohydrate Moiety of Acid Carboxypeptidase; Chapter 7: 1,2-Ü-D-Mannosidase from Aspergillus Saitoi; 7.1. 1,2-Ü-D-Mannosidase; 7.2. Expression of A. Saitoi 1,2-Ü-D-Mannosidase Gene (Msds) In A. Oryzae Cells; 7.3. Catalytic Residues of Ca2+-Independent 1,2-Ü-D-Mannosidas from A. SaiToi |
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7.4. A Single Cysteine Residue and Disulfide Bond of 1,2-Ü-D-Mannosidase 7.5 Production of Human Compatible High Mannose-Type (Man5GlcNAc2) Sugar Chain in Yeast Cells; Chapter 8: Acid Activation of Protyrosinase from Aspergillus Oryzae; 8.1. Acid Activation of Protyrosinase from A. Oryzae; 8.2. Homo-Tetrameric Protyrosinase is Converted to Active Dimers with an Essential Intersubunit Disulfide Bond at Acidic Ph; Chapter 9: Hyper Production System of Aspergillus Oryzae Glucoamylase in Submerged Culture under Tyrosinase-Encoding Gene (MelO) Promoter Control |
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9.1. Glucoamylase from A. Oryzae9.2. Hyper Production System of Glucoamylase Under MelO Gene Promoter Control ; Appendix: Enzymes Referred to in Chapters 1-9; Acknowledgments; Profile; References; Index |
| Bibliography |
Includes bibliographical references (pages 111-126) and index |
| Notes |
English |
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Print version record |
| Subject |
Enzymes -- Synthesis.
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Aspergillus -- Industrial applications
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Biotechnology industries -- Japan
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SCIENCE -- Life Sciences -- Biochemistry.
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Aspergillus -- Industrial applications.
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Biotechnology industries.
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Enzymes -- Synthesis.
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Japan.
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| Form |
Electronic book
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| LC no. |
2020677932 |
| ISBN |
9781633210271 |
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1633210278 |
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