Characterization of maltotriose production by hydrolyzing of soluble starch with α-amylase from Microbulbifer thermotolerans DAU221
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| 024 | 7 | 0 | |a 10.1007/s00253-014-6186-5 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00253-014-6186-5 | ||
| 245 | 0 | 0 | |a Characterization of maltotriose production by hydrolyzing of soluble starch with α-amylase from Microbulbifer thermotolerans DAU221 |h [Elektronische Daten] |c [Yong-Suk Lee, Dong-Ju Park, Yong-Lark Choi] |
| 520 | 3 | |a A maltotriose-producing α-amylase, AmyA, from a newly isolated bacterial strain Microbulbifer thermotolerans DAU221 was purified and characterized in the heterologous host, Escherichia coli, using the pCold I vector. The amyA gene encoded a 761-residue protein composed of a 33 amino acid secretion signal peptide. The purified α-amylase with a molecular mass of 80kDa, approximately, shared a sequence motif characteristic of the glycoside hydrolase family 13. The enzyme was optimally active, at 50°C in sodium phosphate buffer (pH 6.0), by the traditional one factor-at-a-time method. But the optimal conditions of time, temperature, and pH for production of maltotriose from soluble starch were 1.76h, 44.95°C, and pH 6.35 by response surface methodology, respectively. Maltotriose, as the major enzyme reaction product, was analyzed by thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC). The enzyme was found to be inhibited by the addition of 10mM Cu2+, Fe3+, Hg2+, Zn2+, and EDTA, but exhibited extreme stability toward hexane. The K m and V max values for the hydrolysis of soluble starch were 1.08mg/mL and 1.736mmol maltotriose/mg protein/min, respectively. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2014 | ||
| 690 | 7 | |a Microbulbifer thermotolerans |2 nationallicence | |
| 690 | 7 | |a Maltotriose |2 nationallicence | |
| 690 | 7 | |a Maltotriose-producing α-amylase |2 nationallicence | |
| 690 | 7 | |a Response surface methodology |2 nationallicence | |
| 700 | 1 | |a Lee |D Yong-Suk |u Department of Biotechnology, Dong-A University, 604-714, Busan, Republic of Korea |4 aut | |
| 700 | 1 | |a Park |D Dong-Ju |u Department of Biotechnology, Dong-A University, 604-714, Busan, Republic of Korea |4 aut | |
| 700 | 1 | |a Choi |D Yong-Lark |u Department of Biotechnology, Dong-A University, 604-714, Busan, Republic of Korea |4 aut | |
| 773 | 0 | |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/9(2015-05-01), 3901-3911 |x 0175-7598 |q 99:9<3901 |1 2015 |2 99 |o 253 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00253-014-6186-5 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00253-014-6186-5 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Lee |D Yong-Suk |u Department of Biotechnology, Dong-A University, 604-714, Busan, Republic of Korea |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Park |D Dong-Ju |u Department of Biotechnology, Dong-A University, 604-714, Busan, Republic of Korea |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Choi |D Yong-Lark |u Department of Biotechnology, Dong-A University, 604-714, Busan, Republic of Korea |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/9(2015-05-01), 3901-3911 |x 0175-7598 |q 99:9<3901 |1 2015 |2 99 |o 253 | ||