Immobilization of Streptomyces phospholipase D on a Dowex macroporous resin

• Published in: Biotechnology and bioprocess engineering Vol. 13; no. 1; pp. 102 - 107
• Main Authors: Yon, J.O. (Yeungnam University, Gyeongsan, Republic of Korea), Lee, J.S. (Yeungnam University, Gyeongsan, Republic of Korea), Kim, B.G. (Yeungnam University, Gyeongsan, Republic of Korea), Kim, S.D. (Yeungnam University, Gyeongsan, Republic of Korea), Nam, D.H. (Yeungnam University, Gyeongsan, Republic of Korea), E-mail: dhnam@ynu.ac.kr
• Format: Journal Article
• Language: English
• Published: Heidelberg The Korean Society for Biotechnology and Bioengineering 01.02.2008; Springer Nature B.V; 한국생물공학회
• Subjects: Biotechnology; CEFALINAS; CEPHALINE; CEPHALINS; Chemistry; Chemistry and Materials Science; Chromatography; Enzymatic activity; Enzymes; IMMOBILISATION; IMMOBILIZATION; Industrial and Production Engineering; INMOVILIZACION; macroporous resin; phospholipase D; Porous resins; Proteins; STREPTOMYCES; transphosphatidylation; 생물공학; phospholipase D; phosphatidylserine; immobilization; macroporous resin; transphosphatidylation
• ISSN: 1226-8372; 1976-3816
• DOI: 10.1007/s12257-007-0188-4

The immobilization of phospholipase D produced by Streptomyces sp. YU100 was evaluated to see it would be practical for industrial applications. To accomplish this, the purified enzyme, which contained 53 unit/mg of protein, was subjected to immobilization on various matrices. When immobilization supports including calcium alginate gel, polyacrylamide gel, and macroporous resin were evaluated, the highest enzyme retention ratio (greater than 42%) was observed on a Dowex MSA-2 macroporous resin. This may have occurred as a result of the ability of the hydrophobic domain of phospholipase D to interact with the polystyrene backbone of the resin, as well as the ability of the dimethylethanolamine group of the MSA-2 resin to retain the enzyme by forming hydrogen bonds with the acidic residues of the enzyme. Upon the operation of a reactor packed with enzyme that had been immobilized on a Dowex MSA-2 resin, greater than 80% of the initial enzyme activity was retained for 16 days. During the reaction, phosphatidylcholine became bound to the immobilized resin and interfered with the enzyme reaction, therefore, the resin was washed with ethyl ether every 2 h. A process for recovering excessive L-serine from phospholipids using the Dowex MR-3 resin was designed, and the separated L-serine was employed again after replacing the amount that was used.