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| Yi,Xiuli; Shi,Yan; Xu,Hui; Li,Wei; Xie,Jie; Yu,Rongqing; Zhu,Jun; Cao,Yi; Qiao,Dairong. |
| The analysis of individual gene product should enable to clarify the role of a particular enzyme in a complex xylanase system of A. niger. The two genes encoding precursors of co-produced endo-1,4-β-D-xylanases, xynA1 and xynB, were isolated from Aspergillus niger SCTCC 400264 (SCTCC, China) by using RT-PCR technique and then successfully expressed in Escherichia coli BL21. The nucleotide sequences of the xynA1 and xynB genes revealed that they were only 52.5% homology to each other. Characterization of the recombinant enzymes revealed the different properties: the specific activity of recombinant XYNA1 was 16.58 U/mg compared to 1201.7 U/mg for recombinant XYNB; The optimum temperature and pH of the recombinant XYNA1 were 35 ºC and 3.0, respectively,... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Aspergillus niger; Xylanase; Prokaryotic expression; Enzymatic characterization. |
| Ano: 2010 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822010000300030 |
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| BOSSO,Alessandra; MORIOKA,Luiz Rodrigo Ito; SANTOS,Leandro Freire dos; SUGUIMOTO,Hélio Hiroshi. |
| Abstract The commercial enzyme (E.C. = 3.2.1.23) from Kluyveromyces lactis (liquid) and Aspergillus oryzae(lyophilized) was investigated for its hydrolysis potential in lactose substrate, UHT milk, and skimmed milk at different concentrations (0.7; 1.0 and 1.5%), pH values (5.0; 6.0; 6.5 and 7.0), and temperature (30; 35; 40 and 55 ºC). High hydrolysis rates were observed for the enzyme from K. lactis at pH 7.0 and 40 ºC, and from A. oryzae at pH 5.0 and 55 ºC. The enzyme from K. lactis showed significantly higher hydrolysis rates when compared to A. oryzae. The effect of temperature and β-galactosidase concentration on the lactose hydrolysis in UHT milk was higher than in skimmed milk, for all temperatures tested. With respect to the thermal stability, a... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: UHT and skimmed milk; Β-galactosidase; Enzymatic characterization; Lactose intolerance; Enzyme activity. |
| Ano: 2016 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612016000100159 |
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| Leis, Benedikt; Heinze, Simon; Angelov, Angel; Pham, Vu Thuy Trang; Thürmer, Andrea; Jebbar, Mohamed; Golyshin, Peter N.; Streit, Wolfgang R.; Daniel, Rolf; Liebl, Wolfgang. |
| Extreme habitats serve as a source of enzymes that are active under extreme conditions and are candidates for industrial applications. In this work, six large-insert mixed genomic libraries were screened for hydrolase activities in a broad temperature range (8–70°C). Among a variety of hydrolytic activities, one fosmid clone, derived from a library of pooled isolates of hyperthermophilic archaea from deep sea vents, displayed hydrolytic activity on carboxymethyl cellulose substrate plates at 70°C but not at lower temperatures. Sequence analysis of the fosmid insert revealed a gene encoding a novel glycoside hydrolase family 12 (GHF12) endo-1,4-β-glucanase, termed Cel12E. The enzyme shares 45% sequence identity with a protein from the archaeon Thermococcus... |
| Tipo: Text |
Palavras-chave: Functional screenings; Extreme thermostable protein; Archaeal endoglucanase; Enzymatic characterization. |
| Ano: 2015 |
URL: https://archimer.ifremer.fr/doc/00601/71319/69744.pdf |
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