摘要
以果胶为唯一碳源,通过透明圈法和DNS法从上海海洋大学橘园的土壤中筛选出1株高产、有良好热稳定性和酸碱耐受性的产果胶酶野生型菌株Z-5。通过16S rDNA分子技术并综合生理生化特征确定为枯草芽孢杆菌(Bacillus subtilis)。对该果胶酶进行酶学性质研究,结果表明最佳酶活性的反应温度为60℃,最佳酶活性的反应pH为6.0,在此作用温度和作用pH下,酶活力为(879±2.733)U/mL。此外,该酶在40~50℃、pH 6.0~9.0稳定性良好。Ba^(2+)、Fe^(2+)、Ca^(2+)、Cu^(2+)对该酶表现出促进作用,Zn^(2+)、Mn^(2+)对该酶表现出抑制作用。其中Cu^(2+)促进作用最强,Zn^(2+)抑制作用最强,而Mg^(2+)、Hg^(2+)对该酶无明显影响。Bacillus subtilis Z-5所产的果胶酶具有应用于食品商用果胶酶的潜力。
In this study,using pectin as the sole carbon source,a wild-type pectinase-producing strain Z-5 with high yield,good thermal stability,and acid-base tolerance was screened from the soil of citrus orchard of Shanghai Ocean University by transparent zone method and DNS method.And identified as Bacillus subtilis based on the 16S rDNA molecular technique,and comprehensive physiological and biochemical characteristics.Enzymatic properties indicated that the pH and temperature optima were 6.0 and 60℃,the enzyme activity was(879±2.733)U/mL in these conditions.In addition,the enzyme had good stability under the conditions of 40-50℃and pH 6.0-9.0.Ba^(2+),Fe^(2+),Ca^(2+)and Cu^(2+)had positive effects on the enzyme,Zn^(2+)and Mn^(2+)had negative effects on the enzyme.Cu^(2+)had the strongest positive effect on the enzyme,Zn^(2+)had the strongest negative effect on the enzyme,whereas the effect of Mg^(2+)and Hg^(2+)on the enzyme was not obvious.The pectinase produced by Bacillus subtilis Z-5 has the potential to be used as a commercial pectinase for food applications.
作者
张小丹
赵赛赛
林一
宁喜斌
ZHANG Xiaodan;ZHAO Saisai;LIN Yi;NING Xibin(College of Food Science and Technology,Shanghai Ocean University,Shanghai 201306,China;Laboratory of Quality and Safety Risk Assessment for Aquatic Products on Storage and Preservation(Shanghai),Ministry of Agriculture,Shanghai 201306,China;National R&D Branch Center for Freshwater Aquatic Products Processing Technology(Shanghai),Shanghai 201306,China)
出处
《食品与发酵工业》
CAS
CSCD
北大核心
2023年第11期34-40,共7页
Food and Fermentation Industries
关键词
果胶酶
筛选
鉴定
枯草芽孢杆菌
酶学性质
pectinase
screening
identification
Bacillus subtilis
enzymatic properties
