Earticle

초록

영어

Mussels inhabit seashore by attachment themselves using their foot proteins (fps) which has underwater adherent properties. L-3,4-dihydroxyphenyl alanine (Dopa) is regarded as key factor for strong and submerged adhesion. However, other essential adhesion processes including condensation of fps with as high as 30% (w/v) in vacuoles and secretion as a watery liquid with
no dispersion into water are poorly understood yet. In this circumstance, we suggest potential complex coacervation process of fps due to their notable properties, such as low interfacial tension, liquid/liquid phase separation (via concentration) and viscoelasticity. Previously, we successfully produced hybrid fp proteins, fp-151 which is composed of six fp-1 decapeptide repeats at both termini of fp-5 and fp-131, containing six fp-1 decapeptide repeats at both termini of fp-3 variant A in Escherichia coli to overcome low production and purification yields from single fps. We observed successful formation of complex coacervation between fp-151 or fp-131 and hyaluronic acid (HA), an anionic partner for cationic hybrid fps. Formation of coacervation was evidenced through analyses with electrophoretic mobility, turbidity, and morphology. Interestingly, it was revealed that coacervation process improves adhesion ability of hybrid fps in bulk adhesion test and the fps coacervates can encapsulates the oil droplet to form microencapsulated particle.

키워드

저자

• Seonghye LIM [ Department of Chemical Engineering, Pohang University of Science and Technology ]
• Yoo Seong CHOI [ Department of Chemical Engineering, Pohang University of Science and Technology ]
• Dong Gyun KANG [ Department of Chemical Engineering, Pohang University of Science and Technology ]
• Hyung Joon CHA [ Department of Chemical Engineering, Pohang University of Science and Technology ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576