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|a SCI
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|a 572/.7
|2 23
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|a UAMI
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|a Ichishima, Eiji,
|d 1934-
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| 245 |
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|a Unique enzymes of Aspergillus fungi used in Japanese bioindustries /
|c Eiji Ichishima.
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|a New York :
|b Nova Science Publishers,
|c ©2012.
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| 300 |
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|a 1 online resource
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| 336 |
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|a text
|b txt
|2 rdacontent
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|a computer
|b c
|2 rdamedia
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| 338 |
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|a online resource
|b cr
|2 rdacarrier
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| 490 |
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|a Biotechnology in agriculture, industry and medicine
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|a Includes bibliographical references (pages 111-126) and index.
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|a Print version record.
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|a 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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|a 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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|a 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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|a 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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|a 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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| 546 |
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|a English.
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| 590 |
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|a eBooks on EBSCOhost
|b EBSCO eBook Subscription Academic Collection - Worldwide
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| 650 |
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|a Enzymes
|x Synthesis.
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| 650 |
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|a Aspergillus
|x Industrial applications.
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| 650 |
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|a Biotechnology industries
|z Japan.
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| 650 |
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|a Enzymes
|x Synthèse.
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| 650 |
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|a Aspergillus
|x Applications industrielles.
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| 650 |
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|a Bio-industries
|z Japon.
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| 650 |
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|a SCIENCE
|x Life Sciences
|x Biochemistry.
|2 bisacsh
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| 650 |
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|a Aspergillus
|x Industrial applications
|2 fast
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| 650 |
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|a Biotechnology industries
|2 fast
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| 650 |
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|a Enzymes
|x Synthesis
|2 fast
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| 651 |
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|a Japan
|2 fast
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| 776 |
0 |
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|i Print version:
|t Unique enzymes of Aspergillus fungi used in Japanese bioindustries.
|d Hauppauge, N.Y. : Nova Science Publishers, ©2012
|z 9781612097190
|w (DLC) 2011031513
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| 830 |
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0 |
|a Biotechnology in agriculture, industry and medicine series.
|
| 856 |
4 |
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|u https://ebsco.uam.elogim.com/login.aspx?direct=true&scope=site&db=nlebk&AN=760812
|z Texto completo
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|a ProQuest Ebook Central
|b EBLB
|n EBL3024223
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