从一株新分离的地衣芽孢杆菌 ZJ0702 中纯化和表征一种新型中性耐热植酸酶。
Purification and characterization of a novel neutral and heat-tolerant phytase from a newly isolated strain Bacillus nealsonii ZJ0702.
机构信息
College of Food Science and Biotechnology, Zhejiang Gongshang University, 149 Jiaogong Road, Hangzhou 310035, Zhejiang Province, PR China.
出版信息
BMC Biotechnol. 2013 Sep 28;13:78. doi: 10.1186/1472-6750-13-78.
BACKGROUND
Phytic acid and phytates can interact with biomolecules, such as proteins and carbohydrates, and are anti-nutritional factors found in food and feed. Therefore, it is necessary to remove these compounds in food and feed processing. Phytase can hydrolyze phytic acid and phytates to release a series of lower phosphate esters of myoinositol and orthophosphate. Thus, the purification and characterization of novel phytases that can be used in food and feed processing is of particular interest to the food and feed industries.
RESULTS
A novel neutral and heat-tolerant phytase from a newly isolated strain Bacillus nealsonii ZJ0702 was purified to homogeneity with a yield of 5.7% and a purification fold of 44. The molecular weight of the purified phytase obtained by SDS-PAGE was 43 kDa. The homology analysis based on N-terminal amino acid and DNA sequencing indicated that the purified phytase was different from other known phytases. The optimal thermal and pH activity of the phytase was observed at 55°C and 7.5, respectively. Seventy-three percent of the original activity of the phytase was maintained following incubation at 90°C for 10 min. The phytase was stable within a pH range of 6.0-8.0 and showed high substrate specificity for sodium phytate. Cu²⁺, Co²⁺, Zn²⁺, Mn²⁺, Ba²⁺ and Ni²⁺ ions were found to inhibit the activity of the phytase.
CONCLUSIONS
A novel phytase purified from B. nealsonii ZJ0702 was identified. The phytase was found to be thermally stable over a wide temperature range at neutral pH. These properties suggest that this phytase is a suitable alternative to fungal phytases for the hydrolysis of phytic acid and phytates in food and feed processing industries.
背景
植酸和植酸盐可以与生物分子（如蛋白质和碳水化合物）相互作用，是食物和饲料中的抗营养因子。因此，在食品和饲料加工过程中需要去除这些化合物。植酸酶可以水解植酸和植酸盐，释放一系列肌醇低磷酸盐和正磷酸盐。因此，新型植酸酶的纯化和特性研究对于食品和饲料工业具有特别的意义，因为新型植酸酶可以用于食品和饲料加工。
结果
从一株新分离的地衣芽孢杆菌 ZJ0702 中纯化得到一种新型中性耐热植酸酶，产率为 5.7%，纯化倍数为 44。SDS-PAGE 获得的纯化植酸酶的分子量为 43 kDa。基于 N 端氨基酸和 DNA 测序的同源性分析表明，纯化的植酸酶与其他已知植酸酶不同。该植酸酶的最佳热和 pH 活性分别为 55°C 和 7.5。在 90°C 孵育 10 分钟后，植酸酶仍保持 73%的原始活性。该植酸酶在 pH 6.0-8.0 范围内稳定，对植酸钠具有较高的底物特异性。Cu²⁺、Co²⁺、Zn²⁺、Mn²⁺、Ba²⁺和 Ni²⁺离子均对植酸酶的活性有抑制作用。
结论
从地衣芽孢杆菌 ZJ0702 中纯化得到一种新型植酸酶。该植酸酶在中性 pH 下具有较宽温度范围内的热稳定性。这些特性表明，该植酸酶是替代真菌植酸酶用于水解食品和饲料加工行业中植酸和植酸盐的合适选择。
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