NDLI: Purification, characterization, and structural investigation of a new moderately thermophilic and partially calcium-independent extracellular α-amylase from Bacillus sp. TM1

Content Provider	Springer Nature Link
Author	Sajedi, Reza Hassan Naderi Manesh, Hossein Khajeh, Khosro Ranjbar, Bijan Ghaemi, Nasser Naderi Manesh, Mehdi
Copyright Year	2004
Abstract	A new α-amylase was extracted from a recently found strain of Bacillus sp. and purified by ion-exchange chromatography. Sodium dodecyl sulfate polyacrylamide gel electrophoresis showed a single band for the purified enzyme with an apparent molecular weight of 59 kDa. The optimum temperature and pH range of the enzyme were 40–60°C and 4.5–7.5, respectively, and its activation energy was 1.974 kcal/mol. The K $_{ m }$ value for the enzyme activity on solubie starch was 4 mg/mL, and the T $_{ m }$ values obtained from the circular dichroism (CD) results of thermal unfolding were 78.7 and 80.2°C in the absence and presence of the calcium, respectively. The enzyme was almost completely inhibited by the addition of Fe$^{3+}$, Mn$^{2+}$, and Zn$^{2+}$ and was activated by EDTA, Cr$^{3+}$, and Al$^{3+}$. Moreover, it was partially inhibited by Ca$^{2+}$, Ba$^{2+}$, Ni$^{2+}$, and Co$^{2+}$. Proteolytic digestion of the enzyme using trypsin combined with results from T $_{ m }$ using CD and irreversible thermoinactivation suggests that this enzyme can be considered a moderate thermophile with both mild flexibility and rigidity.
Starting Page	41
Ending Page	50
Page Count	10
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	119
Issue Number	1
e-ISSN	15590291
Language	English
Publisher	Humana Press
Publisher Date	2004-01-01
Publisher Place	Totowa
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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