tailieunhanh - SO SÁNH MỘT SỐ TÍNH CHẤT CỦA CHẾ PHẨM ENZYME LIPASE TỪ CANDIDA RUGOSA VÀ PORCINE PANCREAS

Trong nghiên cứu này, một vài tính chất của Enzyme lipase Candida rugosa và Porcine pancreas dạng tự do được nghiên cứu thông qua sự xúc tác sinh học trong môi trường nước (sự thủy phân). Trước tiên, hai chế phẩm enzyme được xác định và so sánh về trọng lượng phân tử (MW) và các điều kiện như pH, nhiệt độ, bậc phản ứng, độ bền pH, độ bền nhiệt độ theo thời gian, ảnh hưởng của ion kim loại và năng lượng hoạt hóa (Ea) của phản ứng thủy phân dầu olive. Từ đó, điều kiện tối ưu mới cho hai chế phẩm. | Tạp chí Khoa học 2012 22b 210-220 Trường Đại học Cần Thơ SO SÁNH MỘT SỐ TÍNH CHẤT CỦA CHẾ PHẨM ENZYME LIPASE TỪ CANDIDA RUGOSA VÀ PORCINE PANCREAS Trần Thị Bé Lan1 Nguyễn Minh Nam2 Tạ Thị Thanh Thúy3 và Phan Ngọc Hòa3 ABSTRACT In this study some characteristics of free Candida rugosa and Porcine pancreas lipase were studied by the biocatalyst performance in aqueous hydrolysis media. Firstly two enzyme lipases were compared in term of molecular weight MW and boundary conditions such as pH temperature level reaction pH and thermal stability the influence of metal ion and active energy Ea following the olive oil hydrolysis. The new optimum values of the two enzymes were then established. The results showed that the activity of the biocatalysis of lipasefrom Candida rugosa was better than that from Porcine pancreas. New optimum values of Candida rugosa enzyme found were MW of lipase from Candida rugosa was about 60 kilodalton the phosphate buffer pH was of the temperature was of 40 C. Under these conditions the batch was repeated in order to determine the pH stability after 60 minutes. The results showed that enzyme activity was still of U mg half-life time t1 2 was found to be 210 min deactivation constant kd was min-1 after 60 minutes thermal stability of enzyme activity was still of 84 U mg and Ea was found to be kJ mol . Similarly the results from Porcine pancreas enzyme were MW of lipase from Porcine pancreas was about 50 kilodalton the borate buffer pH was of the temperature was of 40 C. The batch under these conditions was repeated in order to determine the pH stability after 30 minutes. The results showed that enzyme activity was still of 100 5 88 U mg t1 2 was found to be 148 min kd is min 1 after 60 minutes thermal stability of enzyme activity was still of 4 2 U mg and Ea was found to be kJ mol . From the results of this study it was concluded that the