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문태화(Tae Wha Moon),이현종(Hyun Jong Lee) 한국응용생명화학회 1993 Applied Biological Chemistry (Appl Biol Chem) Vol.36 No.4
Response surface methodology was employed to investigate the conditions for separating water-soluble proteins from egg yolk using sodium alginate, propylene glycol alginate (PGA), sodium carboxymethylcellulose (CMC) and pectin which are approved as food additives. Effects of plysaccharide concentration and pH of the reaction system on protein and lipid contents in the supernatant were evaluated at respectively five and three levels of concentration and pH using rotatable hexagon design. Statistical analysis showed that pH of the system was a more important factor than polysaccharide concentration as it significantly affected all two responses. Separating conditions established by a graphical optimization technique were 0.23∼0.25% of sodium alginate at pH 5.9∼6.0, 0.15∼0.17% of PGA at pH 4.3∼4.5, 0.30∼0.31% of CMC at pH 3.0, and 0.09∼0.10% of pectin at pH 5.6∼5.8.
최갑성,김재욱,문태화,Choi, Kap-Seong,Kim, Ze-Uook,Moon, Tae-Wha 한국식품과학회 1991 한국식품과학회지 Vol.23 No.2
리놀레산 과산화물이 펩신의 활성도에 미치는 영향을 실험한 결과 여러 온도와 pH 조건하에서 리놀레산 과산화물에 의해 펩신 활성도는 감소되었다. 또한, 각종 라디칼 소거제와 금속 이온 존재하에서 펩신 활성을 측정한 결과와 전기영동 결과에 비추에 볼 때 효소의 활성감소는 시스템내에 존재했던 라디칼에 의한 효소자체의 손상에서 비롯된 것으로 생각되었다. The effect of linoleate hydroperoxides(LAHPO) on pepsin activity was investigated. The activity of pepsin was largely decreased by LAHPO at various temperatures and pH. The inactivation of pepsin seems to be the radicals in the system because ascorbate and metal ions enhanced the inactivation of enzyme by LAHPO. It was shown by SDS-PAGE that LAHPO caused scission of the enzyme in the model system.
카제인의 탈인산화가 카제인 미셀의 에탄올 안정성에 미치는 영향
신원선(Weon Sun Shin),문태화(Tae Wha Moon) 한국응용생명화학회 1995 Applied Biological Chemistry (Appl Biol Chem) Vol.38 No.3
Various artificial casein micelle systems were prepared from dephosphorylated whole casein, β- or κ-casein and their stabilities towards ethanol were assessed. Ethanol stability was lower in the micelle systems with dephosphorylated whole casein as compared to the artificial micelles prepared from native whole casein, and the stability decreased with the extent of dephosphorylation. The casein micelles with partially dephosphorylated κ-casein had a lower ethanol stability than those with native x-casein. Ethanol stability of the micelle system with dephosphorylated β-casein decreased as the degree of dephosphorylation increased. Progressive dephosphorylation of caseins in skim milk system resulted in a decrease of the stability towards ethanol. The decrease was less than that in the system with dephosphorylated individual caseins. Increase in pH of the artificial casein micelle systems in the range of 6.3∼7.2 led to an increased ethanol stability manifesting that the presence of serine phosphates contributes significantly to the stability towards ethanol.