2009
DOI: 10.1007/bf03175604
|View full text |Cite
|
Sign up to set email alerts
|

Molecular cloning and characterization of an α-amylase with raw starch digestibility fromBacillus sp. YX-1

Abstract: The complete gene (amy) that encoding a raw starch digesting -amylase (BYXA) from Bacillus sp. YX-1 was cloned, sequenced and expressed in Escherichia coli. The amy gene consisted of 1545 base pairs and encoded a protein of 514 amino acid residues with a calculated molecular mass of 58 kDa. The recombinant protein was purified by Ni 2+ affinity chromatography and subsequently characterized. The optimal pH and temperature for the purified recombinant enzyme were 5.5 and 45 °C, respectively. The enzyme showed st… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2011
2011
2023
2023

Publication Types

Select...
3
1

Relationship

0
4

Authors

Journals

citations
Cited by 4 publications
(1 citation statement)
references
References 17 publications
0
1
0
Order By: Relevance
“…The same result was observed for Bacillus velezensis KB 2216 (pH 5.5), Aspergillus oryzae IFO-30103 (pH 5.5), Bacillus sp. YX-1 (pH 5.5), Penicillium olsonii (pH 5.5) [28][29][30][31].…”
Section: Properties Of Purified Amy T Temperature and Ph Optima For A...mentioning
confidence: 99%
“…The same result was observed for Bacillus velezensis KB 2216 (pH 5.5), Aspergillus oryzae IFO-30103 (pH 5.5), Bacillus sp. YX-1 (pH 5.5), Penicillium olsonii (pH 5.5) [28][29][30][31].…”
Section: Properties Of Purified Amy T Temperature and Ph Optima For A...mentioning
confidence: 99%