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| Wu,Gaobing; Zhan,Tao; Guo,Yiming; Kumar,Ashok; Liu,Ziduo. |
| Background: Glycine oxidase (GO), a type of D-amino acid oxidase, is of biotechnological interest for its potential in several fields. In our previous study, we have characterized a new glycine oxidase (BceGO) from Bacillus cereus HYC-7. Here, a variant of N336K with increased the affinity against all the tested substrate was obtained by screening a random mutant library of BceGO. It is observed that the residue N336 is invariable between its homogeneous enzymes. This work was aimed to explore the role of the residue N336 in glycine oxidase by site-directed mutagenesis, kinetic assay, structure modeling and substrate docking. Results: The results showed that the affinity of N336H, N336K and N336R increased gradually toward all the substrates, with increase... |
| Tipo: Journal article |
Palavras-chave: Bacillus cereus; Error-prone PCR; Glycine oxidase; Site-directed mutagenesis; Substrate affinity. |
| Ano: 2016 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000400004 |
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| Cançado,F.C.; Chimoy Effio,P; Terra,W.R.; Marana,S.R.. |
| cDNA coding for two digestive lysozymes (MdL1 and MdL2) of the Musca domestica housefly was cloned and sequenced. MdL2 is a novel minor lysozyme, whereas MdL1 is the major lysozyme thus far purified from M. domestica midgut. MdL1 and MdL2 were expressed as recombinant proteins in Pichia pastoris, purified and characterized. The lytic activities of MdL1 and MdL2 upon Micrococcus lysodeikticus have an acidic pH optimum (4.8) at low ionic strength (μ = 0.02), which shifts towards an even more acidic value, pH 3.8, at a high ionic strength (μ = 0.2). However, the pH optimum of their activities upon 4-methylumbelliferyl N-acetylchitotrioside (4.9) is not affected by ionic strength. These results suggest that the acidic pH optimum is an intrinsic property of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Lysozyme; Digestive lysozyme; Substrate affinity; PH optimum. |
| Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008001100005 |
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