The role of N1 domain on the activity, stability, substrate specificity and raw starch binding of amylopullulanase of the extreme thermophile Geobacillus thermoleovorans
Author:
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Biotechnology
Link
http://link.springer.com/content/pdf/10.1007/s00253-014-6345-8.pdf
Reference58 articles.
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2. Aoki H, Yopi, Sakano Y (1997) Molecular cloning and heterologous expression of the isopullulanase gene from Aspergillus niger A.T.C.C. 9642. Biochem J 323:757–764
3. Ara K, Igarashi K, Saeki K, Ito S (1995) An alkaline amylopullulanase from alkaliphilic Bacillus sp. KSM-1378; kinetic evidence for two independent active sites for the α-1,4 and α-1,6 hydrolytic reactions. Biosci Biotechnol Biochem 59:662–665
4. Ashikari T, Nakamura N, Tanaka Y, Kiuchi N, ShiBano Y, Tanaka T, Amachi T, Yoshizumi H (1986) Rhizopus raw-starch-degrading glucoamylase: its cloning and expression in yeast. Agric Biol Chem 50:957–964
5. Bertoldo C, Armbrecht M, Becker F, Schafer T, Antranikian G, Liebl W (2004) Cloning, sequencing, and characterization of a heat- and alkali-stable type I pullulanase from Anaerobranca gottschalkii. Appl Environ Microbial 70(6):3407–3416
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