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Virgibacillus halodenitrificans ST‐1 for fermentation of shrimp paste and hydrolysates of its protease

机译:VIRGIBACILLUS HALODENITIFICANS ST-1用于发酵虾糊和水解产物的蛋白酶

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The nutrition and flavor of shrimp paste came from hydrolyzation by enzymes that were produced by microorganisms. The salt‐tolerant strain Virgibacillus halodenitrificans ST‐1 isolated from shrimp paste was studied and used in the fermentation of shrimp paste. The strain and the protease produced by ST‐1 were investigated. The optimum pH of the protease was 8.0, and the reaction temperature was 30°C. The protease showed high activity in the range of pH (5.0–11.0) and NaCl concentration (1%–15%). Divalent cations such as Ba2+, Ca2+, Mg2+, Mn2+, and Si2+ could enhance the protease activity. Residual activity of protease was more than 90% when it was incubated with PMSF and H2O2. Also, the enzyme retained more than 90% of initial activity after it was incubated with organic solvents. Variety of natural proteins could be substrates of the protease. By analyzing the release rate of free amino acids, it was predicted that the cleavage sites of the protease were mainly Glu, Asp, Gly, Leu, and Lys. Moreover, the hydrolysates of the protease had antioxidant activity, especially for DPPH and superoxide anion radical scavenging. The strain ST‐1 and the protease both were excellent candidates for food industries.
机译:虾糊的营养和风味来自微生物产生的酶的水解。研究并用于虾糊中分离的耐盐菌株Virgibacillus嗜睡症ST-1并用于虾糊的发酵。研究了ST-1产生的菌株和蛋白酶。蛋白酶的最佳pH值为8.0,反应温度为30℃。蛋白酶在pH(5.0-11.0)和NaCl浓度(1%-15%)的范围内显示出高活性。二价阳离子如Ba2 +,Ca2 +,Mg2 +,Mn2 +和Si2 +可以增强蛋白酶活性。当与PMSF和H 2 O 2一起温育时,蛋白酶的残余活性大于90%。此外,在将其与有机溶剂孵育后,酶在其孵育后保留超过90%的初始活性。各种天然蛋白质可以是蛋白酶的基材。通过分析游离氨基酸的释放速率,预测蛋白酶的切割位点主要是Glu,Asp,Gly,Leu和Lys。此外,蛋白酶的水解产物具有抗氧化活性,特别是对于DPPH和超氧化物阴离子自由基清除。菌株ST-1和蛋白酶都是食品工业的优秀候选者。

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