刺槐豆胶
米曲霉
化学
椰子
食品科学
色谱法
核化学
水溶液中的金属离子
酶
生物化学
金属
黄原胶
有机化学
材料科学
复合材料
流变学
作者
Uttam Kumar Jana,Rahul Kumar Suryawanshi,Bhanu Pratap Prajapati,Hemant Soni,Naveen Kango
标识
DOI:10.1016/j.biortech.2018.07.143
摘要
A multi-tolerant β-mannanase (ManAo) was produced by Aspergillus oryzae on copra meal, a low-cost agro waste. Under statistically optimized conditions, 4.3-fold increase in β-mannanase production (434 U/gds) was obtained. Purified ManAo had MW ∼34 kDa and specific activity of 335.85 U/mg with optimum activity at 60 °C and at pH 5.0. Activity of ManAo was enhanced by most metal ions and modulators while maximum enhancement was noticed with Ag+ and Triton X-100. Km and Vmax were 2.7 mg/mL and 1388.8 µmol/min/mg for locust bean gum while the enzyme showed lower affinity towards konjac gum (8.8 mg/mL, 555.5 µmol/min/mg). Evaluation of various thermodynamic parameters indicated high-efficiency of the ManAo with activation energy 12.42 KJ/mol and 23.31 KJ/mol towards LBG and konjac gum, respectively. End product analysis of β-mannanase action by fluorescence assisted carbohydrate electrophoresis (FACE) revealed the generation of sugars from DP 1-4 with some higher DP MOS from different mannans.
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