Earticle

초록

영어

β-agarase hydrolyzes β-1,4 linkages of agarose, yielding neoagarooligosaccharides. The neoagaro-oligosaccharides inhibit the growth of bacteria and slow down the degradation of starch and they can reduce the caloric value as additives. Therefore, economically feasible
production process of β-agarase enzyme is required. The β-agarase gene (agaB, 1 kb ORF) from Zobellia galactanivorans was subcloned into Pichia expression vector, pPIC9. The constructed plasmid pPICAgaB (9 kb) was integrated into HIS4 and AOX1 locus of P. pastoris
genome, respectively, resulting in Mut+(AOX1) and Muts (aox1Δ, methanol utilization slow) strain. The transformed cells showed red halos around its colonies in methanol agar plate by adding iodine solution, indicating the secretory expression of agaB in P. pastoris.
Also, the protein and activity of secreted β-agarase were confirmed by using SDS-PAGE and zymographic analysis. When transformed cells (Mut+ and Muts) were cultured on medium containing each 0.1%, 0.5% and 1% methanol, the extracellular activity of β-agarase were
increased from about 1.3 unit/ml to 1.6 unit/ml according to elevate methanol concentration. However, the expression level of β-agarase in Mut+ strain was indistinguishable from that of Muts strain.

키워드

저자

• Ji-Hwan SEOK [ Dept. of Biotechnology and Bioengineering, Dong-Eui University ]
• Hee-Gyun PARK [ Dept. of Biotechnology and Bioengineering, Dong-Eui University ]
• Sang-Hyeon LEE [ Dept. of Pharmaceutical Engineering, College of Medical Life Sciences, Silla University ]
• Soo-Wan NAM [ Dept. of Biotechnology and Bioengineering, Dong-Eui University ]
• Yeon-Hee KIM [ Dept. of Biotechnology and Bioengineering, Dong-Eui University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576