Park Joo D, Park Jae W
OSU Seafood Laboratory, 2001 Marine Dr. nr 253, Astoria, OR 97103, USA.
J Food Sci. 2007 May;72(4):C202-7. doi: 10.1111/j.1750-3841.2007.00322.x.
Myoglobin (Mb) was extracted from Pacific sardine and added to Pacific whiting surimi to measure its effects on protein gelation. The purity of Mb extract was determined by SDS-PAGE. Mb extract using ethanol showed higher purity than Mb extract using ammonium sulfate. The addition of 0.2% Mb significantly reduced breaking force. However, a synergistic effect of 1.0% Mb was observed with 1.0% beef plasma protein (BPP) to increase surimi gel strength. The highest storage modulus of gels was observed at 1.0% Mb addition, which corresponded with the nonfracture gel and also supported a synergistic interaction between 1.0% Mb and 1.0% BPP. Differential scanning calorimetry showed Mb addition might have affected myosin denaturation and aggregation.
从太平洋沙丁鱼中提取肌红蛋白(Mb),并添加到太平洋无须鳕鱼糜中,以测定其对蛋白质凝胶化的影响。通过SDS-PAGE测定Mb提取物的纯度。使用乙醇的Mb提取物比使用硫酸铵的Mb提取物具有更高的纯度。添加0.2%的Mb显著降低了断裂力。然而,观察到1.0%的Mb与1.0%的牛血浆蛋白(BPP)具有协同效应,可提高鱼糜凝胶强度。在添加1.0% Mb时观察到凝胶的储能模量最高,这与未断裂凝胶相对应,也支持了1.0% Mb与1.0% BPP之间的协同相互作用。差示扫描量热法表明,添加Mb可能影响了肌球蛋白的变性和聚集。