An Insight Into Ameliorating Production, Catalytic Efficiency, Thermostability and Starch Saccharification of Acid-Stable α-Amylases From Acidophiles
Most of the extracellular enzymes of acidophilic bacteria and archaea are stable at acidic pH with a relatively high thermostability. There is, however, a dearth of information on their acid stability. Although several theories have been postulated, the adaptation of acidophilic proteins to low pH h...
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| Published in | Frontiers in bioengineering and biotechnology Vol. 6; p. 125 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
Frontiers Media S.A
28.09.2018
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| Subjects | |
| Online Access | Get full text |
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| Summary: | Most of the extracellular enzymes of acidophilic bacteria and archaea are stable at acidic pH with a relatively high thermostability. There is, however, a dearth of information on their acid stability. Although several theories have been postulated, the adaptation of acidophilic proteins to low pH has not been explained convincingly. This review highlights recent developments in understanding the structure and biochemical characteristics, and production of acid-stable and calcium-independent α-amylases by acidophilic bacteria with special reference to that of
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| Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 Reviewed by: Fu-Li Li, Qingdao Institute of Bioenergy and Bioprocess Technology (CAS), China; Roland Wohlgemuth, Lodz University of Technology, Poland Edited by: Caixia Wan, University of Missouri, United States This article was submitted to Process and Industrial Biotechnology, a section of the journal Frontiers in Bioengineering and Biotechnology |
| ISSN: | 2296-4185 2296-4185 |
| DOI: | 10.3389/fbioe.2018.00125 |