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| Bai,Xi; Yuan,Xianjun; Wen,Aiyou; Li,Junfeng; Bai,Yunfeng; Shao,Tao. |
| Background: Cold-active endo-1, 4-β-glucanase (EglC) can decrease energy costs and prevent product denaturation in biotechnological processes. However, the nature EglC from C. farmeri A1 showed very low activity (800 U/L). In an attempt to increase its expression level, C. farmeri EglC was expressed in Escherichia coli as an N-terminal fusion to protein S (ProS) from Myxococcus xanthus. Results: A novel expression vector, pET(ProS-EglC), was successfully constructed for the expression of C. farmeri EglC in E. coli. SDS-PAGE showed that the recombinant protein (ProS-EglC) was approximately 60 kDa. The activity of ProS-EglC was 12,400 U/L, which was considerably higher than that of the nature EglC (800 U/L). ProS-EglC was active at pH 6.5-pH 8.0,... |
| Tipo: Journal article |
Palavras-chave: Cellulose degradation; Cellulose; Cold-active enzyme; Endoglucanases; Enzymatic properties; Escherichia coli; Expression; Novel expression vector; N-terminal fusion; Protein S-tag; Recombinant protein. |
| Ano: 2016 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600012 |
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| Oliveira,Arlem Nascimento de; Oliveira,Luiz Antonio de; Andrade,Jerusa Souza. |
| Amylase production and partial characterization of crude enzyme preparations from two rhizobia strains (R-926 and R-991) were evaluated. For both the strains, maximal amylase activities were achieved during the early-to-mid- exponential growth phase; both were active over a pH range from 4.5 to 8.5 and temperature from 30 to 50 ºC. None of the ions studied (K+, Na+, Ca2+, Hg2+, Mg2+, Mn2+, Cu2+ and Zn2+) was required for the catalytic activity of strain R-926; amylase activity of strain R-991 was stimulated in the presence of K+, Hg2+ and Zn2+. The surfactants SDS, Triton X-100 and Tween-80 did not have a pronounced inhibitory effect on enzyme activities; SDS and Tween-80 caused the highest stimulatory effects. Amylase activities from the rhizobia strains... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Rhizobium; Bradyrhizobium; Amylase production; Enzymatic properties. |
| Ano: 2010 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132010000100005 |
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