A hyper-thermostable α-amylase from Pyrococcus furiosus accumulates in Nicotiana tabacum as functional aggregates

A hyper-thermostable α-amylase from Pyrococcus furiosus accumulates in Nicotiana tabacum as functional aggregates

Abstract Background Alpha amylase hydrolyzes α-bonds of polysaccharides such as starch and produces malto-oligosaccharides. Its starch saccharification applications make it an essential enzyme in the textile, food and brewing industries. Commercially available α-amylase is mostly produced from Bacil...

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Bibliographic Details
Main Authors: Hong Zhu, L. Bruce Reynolds, Rima Menassa
Format: Article
Language:English
Published: BMC 2017-06-01
Series:BMC Biotechnology
Subjects:
Amylase
Thermostable
Tobacco
Hyperthermostable enzyme
PFA
Starch hydrolase
Online Access:http://link.springer.com/article/10.1186/s12896-017-0372-3

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http://link.springer.com/article/10.1186/s12896-017-0372-3

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