米曲霉 VKPM F-1593 的角质溶解潜力及其酶与商业角质酶制剂的比较

S. Timorshina, E. Popova, K. Kuleshova, A. Akyol, A. Osmolovskiy
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引用次数: 0

摘要

畜牧业是一个快速发展的农业分支,产量每年都在增加,而含角蛋白的废物(羽毛、刚毛)占该行业所有废物的绝大部分。开发以环保方式处理这些废弃物以获取宝贵资源(氨基酸和寡肽)的方法是现代科学(包括生物技术)的一项重要任务。符合现代绿色经济发展潮流的处理畜牧业废物的方法之一是利用微生物及其酶。研究了在各种氮源和碳源的深层条件下,包括生产者在动物粪便上生长的条件下,获得黑曲霉 VKPM F-1593 角质溶解酶的可能性。在使用混合碳源和氮源时,达到了最高的目标活性(96.1 E):无机碳源--硝酸钠,易消化有机碳源--鱼粉水解物,难消化有机碳源--磨碎的鸡毛。改变发酵培养基成分中各种底物的含量不仅能调节蛋白水解活性的水平,还能在不同的培养日达到生产者活性的峰值。克拉维氏菌 VKPM F-1593(pI 9.3)对各种蛋白质底物的特异性角蛋白酶活性与商业蛋白酶 K 的活性相同。然而,A. clavatus VKPM F-1593 蛋白酶的总体蛋白水解活性更高,这说明这种培养物在动物废弃物生物降解方面前景广阔。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
KERATINOLYTIC POTENTIAL OF MICROMYCETE ASPERGILLUS CLAVATUS VKPM F-1593 AND COMPARISON OF ITS ENZYMES WITH THE COMMERCIAL KERATINASE PREPARATION
Animal husbandry is a rapidly developing branch of agriculture, increasing the volume of production annually, and keratin-containing waste (feathers, bristles) make up the majority of all waste from this industry. The development of methods of environmentally friendly processing of such waste to obtain valuable resources (amino acids and oligopeptides) is an important mission of modern science, including biotechnology. One of the ways to dispose of animal husbandry waste that meets modern trends in the development of a green economy is the use of microorganisms and their enzymes. The possibility of obtaining keratinolytic enzymes of Aspergillus clavatus VKPM F-1593 under deep conditions with various sources of nitrogen and carbon, including with the growth of the producer on animal waste, was studied. The highest target activity (96.1 E) was achieved using mixed carbon and nitrogen sources: inorganic - sodium nitrate, easily digestible organic - fi sh meal hydrolysate and hard-toreach organic - ground chicken feather. Varying the content of various substrates in the composition of fermentation media allowed not only to regulate the level of proteolytic activity, but also to reach the peak of producer activity on diff erent days of cultivation. The specifi c keratinase activity of A. clavatus VKPM F-1593 (pI 9.3) to various protein substrates with the activity of a commercial proteinase K. Both enzymes showed a similar level of activity regarding most of the substrates used. However, protease A. clavatus VKPM F-1593 has a greater overall proteolytic activity, which confi rms the prospects of this culture for biodegradation of animal waste
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