Purification and characterization of a recombinant beta-glucosidase in Escherichia coli
Tác giả: Nguyen Thi Binh, Nguyen Thi Quy, Le Thi Thu Hong, Truong Nam Hai
Số trang:
P. 599-607
Tên tạp chí:
Công nghệ sinh học - Vietnam Journal of Biotechnology
Số phát hành:
Vol. 20(4)
Kiểu tài liệu:
Tạp chí trong nước
Nơi lưu trữ:
03 Quang Trung
Mã phân loại:
570
Ngôn ngữ:
Tiếng Anh
Từ khóa:
Affinity chromatography,enzyme characteristics, Eschericia coliRosetta 1, protein purification, recombinant beta-glucosidase
Chủ đề:
Biology
Tóm tắt:
Beta-glucosidase (BGL) is anenzyme involvedin the degradationof cellulose and playsan essential partin many biological processes. Currently, most BGLs applied in the industryare derived from fungi. Exploring novel BGLswith desired propertiesisattractive. The recombinant BGL derived from microorganismssurroundingwhite-rot fungus in Cuc Phuong National Park was successfully expressed in Escherichia coliRosetta 1(denoted asthe GH3S2 gene).The protein GH3S2was purified by an affinity chromatography column using buffer PBS 50 mM (NaCl-free) pH 7, and the enzymewas collected in buffer containing imidazole 300 mM.
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