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首页> 外文期刊>BMC Biotechnology >Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization
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Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization

机译：新型南极抗霉菌α-淀粉酶在烘焙行业中的功能表达及其磁固定化

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Backgroundα-Amylase plays a pivotal role in a broad range of industrial processes. To meet increasing demands of biocatalytic tasks, considerable efforts have been made to isolate enzymes produced by extremophiles. However, the relevant data of α-amylases from cold-adapted fungi are still insufficient. In addition, bread quality presents a particular interest due to its high consummation. Thus developing amylases to improve textural properties could combine health benefits with good sensory properties. Furthermore, iron oxide nanoparticles provide an economical and convenient method for separation of biomacromolecules. In order to maximize the catalytic efficiency of α-amylase and support further applications, a comprehensive characterization of magnetic immobilization of α-amylase is crucial and needed. ResultsA novel α-amylase ( AmyA1 ) containing an open reading frame of 1482?bp was cloned from Antarctic psychrotolerant fungus G. pannorum and then expressed in the newly constructed Aspergillus oryzae system. The purified recombinant AmyA1 was approximate 52?kDa. AmyA1 was optimally active at pH?5.0 and 40?°C, and retained over 20% of maximal activity at 0–20?°C. The K m and V max values toward soluble starch were 2.51?mg/mL and 8.24?×?10?2 mg/(mL?min) respectively, with specific activity of 12.8?×?103 U/mg. AmyA1 presented broad substrate specificity, and the main hydrolysis products were glucose, maltose, and maltotetraose. The influence of AmyA1 on the quality of bread was further investigated. The application study shows a 26% increase in specific volume, 14.5% increase in cohesiveness and 14.1% decrease in gumminess in comparison with the control. AmyA1 was immobilized on magnetic nanoparticles and characterized. The immobilized enzyme showed improved thermostability and enhanced pH tolerance under neutral conditions. Also, magnetically immobilized AmyA1 can be easily recovered and reused for maximum utilization. ConclusionsA novel α-amylase ( AmyA1 ) from Antarctic psychrotolerant fungus was cloned, heterologous expression in Aspergillus oryzae , and characterized. The detailed report of the enzymatic properties of AmyA1 gives new insights into fungal cold-adapted amylase. Application study showed potential value of AmyA1 in the food and starch fields. In addition, AmyA1 was immobilized on magnetic nanoparticles and characterized. The improved stability and longer service life of AmyA1 could potentially benefit industrial applications.
机译：背景α-淀粉酶在广泛的工业过程中起着关键作用。为了满足生物催化任务的日益增长的需求，已经做出了巨大的努力来分离由极端微生物产生的酶。然而，来自冷适应真菌的α-淀粉酶的相关数据仍然不足。另外，由于面包的高消费水平，面包的质量引起了人们的特别关注。因此，开发淀粉酶以改善质构特性可以将健康益处与良好的感官特性相结合。此外，氧化铁纳米颗粒提供了分离生物大分子的经济且方便的方法。为了使α-淀粉酶的催化效率最大化并支持进一步的应用，对α-淀粉酶的磁固定化进行全面表征是至关重要的并且是必需的。结果从南极精神抗性真菌G. pannorum中克隆了一个新的α-淀粉酶（AmyA1），其开放阅读框为1482bp，并在新构建的米曲霉系统中表达。纯化的重组AmyA1约为52？kDa。 AmyA1在pH？5.0和40？C时具有最佳活性，在0–20？C时保留最大活性的20％以上。可溶性淀粉的K m 和V max 值为2.51？mg / mL和8.24？×？10 ？2 mg /（mL？ min），比活为12.8？×？10 3 U / mg。 AmyA1具有广泛的底物特异性，主要水解产物为葡萄糖，麦芽糖和麦芽四糖。进一步研究了AmyA1对面包质量的影响。应用研究表明，与对照组相比，比容提高了26％，内聚力提高了14.5％，胶粘性降低了14.1％。将AmyA1固定在磁性纳米颗粒上并进行表征。固定的酶在中性条件下显示出改善的热稳定性和增强的pH耐受性。同样，磁性固定的AmyA1可以轻松回收并重新利用以实现最大利用率。结论克隆了一种新型的南极抗精神病真菌α-淀粉酶（AmyA1），并在米曲霉中异源表达并进行了鉴定。 AmyA1的酶学特性的详细报告提供了真菌冷适应淀粉酶的新见解。应用研究表明AmyA1在食品和淀粉领域具有潜在价值。另外，将AmyA1固定在磁性纳米颗粒上并进行了表征。 AmyA1的更高的稳定性和更长的使用寿命可能会有益于工业应用。

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