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首页> 美国卫生研究院文献>Scientific Reports >A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry
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A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry

机译：一种新型的碱性蛋白酶来自嗜碱的Idiomarina sp。 C9-1在皮革行业中可用于环保型酶促脱毛

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Alkaline proteases have a myriad of potential applications in many industrial processes such as detergent, food and feed production, waste management and the leather industry. In this study, we isolated several alkaline protease producing bacteria from soda lake soil samples. A novel serine alkaline protease (AprA) gene from alkaliphilic Idiomarina sp. C9-1 was cloned and expressed in Escherichia coli. The purified AprA and its pre-peptidase C-terminal (PPC) domain-truncated enzyme (AprA-PPC) showed maximum activity at pH 10.5 and 60 °C, and were active and stable in a wide range of pH and temperature. Ca2+ significantly improved the thermostability and increased the optimal temperature to 70 °C. Furthermore, both AprA and AprA-PPC showed good tolerance to surfactants and oxidizing and reducing agents. We found that the PPC domain contributed to AprA activity, thermostability and surfactant tolerance. With casein as substrate, AprA and AprA-PPC showed the highest specific activity of 42567.1 U mg−1 and 99511.9 U mg−1, the Km values of 3.76 mg ml−1 and 3.98 mg ml−1, and the Vmax values of 57538.5 U mg−1 and 108722.1 U mg−1, respectively. Secreted expression of AprA-PPC in Bacillus subtilis after 48 h cultivation resulted in yield of 4935.5 U ml−1 with productivity of 102.8 U ml−1 h−1, which is the highest reported in literature to date. Without adding any lime or sodium sulfide, both of which are harmful pollutants, AprA-PPC was effective in dehairing cattle hide and skins of goat, pig and rabbit in 8–12 h without causing significant damage to hairs and grain surface. Our results suggest that AprA-PPC may have great potentials for ecofriendly dehairing of animal skins in the leather industry.
机译：碱性蛋白酶在许多工业过程中具有许多潜在应用，例如洗涤剂，食品和饲料生产，废物管理和皮革工业。在这项研究中，我们从苏打湖土壤样品中分离了几种产生碱性蛋白酶的细菌。一个新的丝氨酸碱性蛋白酶（AprA）基因从嗜碱的Idiomarina sp。 C9-1被克隆并在大肠杆菌中表达。纯化的AprA及其前肽酶C末端（PPC）域截短的酶（AprA-PPC）在pH 10.5和60°C下显示最大活性，并且在宽的pH和温度范围内均具有活性和稳定性。 Ca 2 + 显着提高了热稳定性，并将最佳温度提高到70C。此外，AprA和AprA-PPC均显示出对表面活性剂以及氧化剂和还原剂的良好耐受性。我们发现PPC域有助于AprA活性，热稳定性和表面活性剂耐受性。以酪蛋白为底物，AprA和AprA-PPC的最高比活性为42567.1 U mg -1 和99511.9 U mg -1 ，Km值为3.76 ofmg ml < sup> -1 和3.98 mg ml -1 ，Vmax值分别为57538.5 U mg -1 和108722.1 U mg −1 。培植枯草芽孢杆菌48 h后AprA-PPC的秘密表达导致产量4935.5 U ml -1 ，生产力为102.8 U ml -1 h -1 ，这是迄今为止文献中报道的最高数量。不添加任何石灰或硫化钠（这两种都是有害污染物），AprA-PPC可以在8–12 h的时间内对山羊，猪和兔子的牛皮革和山羊皮进行脱毛，而不会对毛发和谷物表面造成重大损害。我们的结果表明，AprA-PPC在皮革行业中具有对动物皮肤进行生态脱毛的巨大潜力。

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