Purification of laccase from newly isolated Bacillus Safensis and analysis of biochemical and structural properties of Laccase enzymes

Publish Year: 1396
نوع سند: مقاله کنفرانسی
زبان: English
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BSCONF05_014

تاریخ نمایه سازی: 22 دی 1396

Abstract:

laccase (EC 1.10.3.2) is an extracellular oxygenated oxidizer that uses molecular oxygen as the final receptor. In this study, the purity and location of the laccase enzyme from the new Bacillus safensisbacteria. The laccase active protein, expression was performed under aerobic conditions and at low temperature. The recombinant protein by the column tends to customize and determine the molecular gel of the enzyme by 60 SDS-PAGE clients. The enzyme has the best performance at 35 degree. The optimum pH of the enzyme activity is 5.5. This distinguishes its unusual property from other known bacterial laccases.

Authors

Atena Mashhadi

Department of Biology, Science and Research Branch, Islamic AzadUniversity,Tehran,Iran

Khosro Khajeh

Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran

Maryam Monsef Shokri

International Sturgeon Research Institute, Agricultural Research, Education & Extension Organization (AREEO), Rasht, Iran.

Bahare Dabirmanesh

Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran