血红素
肌红蛋白
血红素
信号肽
异源的
发酵
化学
色谱法
工业发酵
生物反应器
肽
生物化学
生物
食品科学
酶
重组DNA
基因
有机化学
作者
Bohan Zhang,Xinrui Zhao,Ziwei Wang,Haoze Wang,Jingwen Zhou,Guocheng Du,Jian Chen,Jianghua Li
标识
DOI:10.1021/acs.jafc.1c04124
摘要
Myoglobin (MG) is one of the eukaryotic heme-binding proteins that is closely associated with the real color and metallic taste of meat and can be used as a color additive in artificial meat alternatives. However, the traditional extraction methods are expensive and time-consuming and the heterologous biosynthesis of MG has never been reported. Herein, we achieved the secretory expression of porcine MG by engineered Komagataella phaffii using the suitable host (X33), signal peptide (α-factor signal peptide), and modified constitutive promoter (G1 promoter). In addition, the fermentation conditions for MG production were optimized at shaking-flask level (BMGY medium with 40 mg/L of hemin, 30 °C) and at fermenter level (30% DO, feeding 150 mg/L of hemin), resulting in the highest titer of 285.42 mg/L MG in fed-batch fermentations. Furthermore, a purification method for food-grade MG was developed, which can obtain 0.22 mol of heme/mol of MG with 88.0% purity and 66.1% recovery rate.
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