Screening, purification, and characterization of a novel organic solvent-tolerant esterase, Lip2, from Monascus purpureus strain M7
Screening, purification, and characterization of a novel organic solvent-tolerant esterase, Lip2, from Monascus purpureus strain M7
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紫红曲霉菌株 M7 中新型耐有机溶剂酯酶 Lip2 的筛选、纯化和表征
DOI:
10.1007/s00792-016-0907-x
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发表时间:
2017-01
期刊:
影响因子:
2.9
通讯作者:
Mu Li
中科院分区:
文献类型:
--
作者:
Li-Jing Kang;Zi-Tong Meng;Chen Hu;Yan Zhang;Hai-Lun Guo;Qing Li;Mu Li
Organic solvent-tolerant esterases are proven to be excellent biocatalysts in chemical and pharmaceutical industries. A novel organic solvent-tolerant esterase gene, lip2, was isolated from filamentous fungi Monascus purpureus M7. The sequence analysis suggested that lip2 has a conserved "GDSL" motif near the active center. The multiple-sequence alignment and phylogenetic analysis revealed that Lip2 displayed two unique amino-acid sequence motifs that clearly separate it from any other previously described lipase family. After incubation in 20% methanol and ethanol for 3 h, the Lip2 displayed 190 and 180% residual activities, respectively. It retained 99-110% relative activity in 20% (v/v) hydrophilic organic solvents after incubation for 1 day. This esterase showed optimal activity at 40 °C and retained about 70% maximal activity at 60 °C. The enzyme also displayed more than 50% residual activity over a range of pH 5-11. In the presence of most of metal ions or additives, Lip2 retained most of the activity. These unique properties of Lip2 make it a promising as biocatalyst for industrial processes.
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DOI:
--
发表时间:
2007
期刊:
--
影响因子:
--
作者:
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通讯作者:
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影响因子:
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