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Unique enzymes of Aspergillus fungi used in Japanese bioindustries / Eiji Ichishima.

By: Material type: TextTextSeries: Biotechnology in agriculture, industry and medicine seriesPublisher: New York : Nova Science Publishers, ©2012Description: 1 online resourceContent type:
  • text
Media type:
  • computer
Carrier type:
  • online resource
ISBN:
  • 9781633210271
  • 1633210278
Subject(s): Genre/Form: Additional physical formats: Print version:: Unique enzymes of Aspergillus fungi used in Japanese bioindustries.DDC classification:
  • 572/.7 23
LOC classification:
  • TP248.E5
Online resources:
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.
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
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.
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.
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.
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Includes bibliographical references (pages 111-126) and index.

Print version record.

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.

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

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.

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.

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.

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