淡紫色拟青霉对“头发废物”进行生物处理,作为一种具有漂白、碱性和热稳定性的角蛋白酶,并有可能应用于洗衣添加剂:表征和洗涤性能分析。

Ivana A Cavello, Roque A Hours, Sebastián F Cavalitto
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引用次数: 25

摘要

淡紫拟青霉(Thom) Samson LPS 876是一种局部分离的真菌菌株,在含有“头发废物”的最小矿物培养基上生长,“头发废物”是毛发保存脱毛过程中的残留物,并产生具有角朊酶活性的蛋白酶。对该酶进行了生物化学表征。采用响应面法确定最佳反应条件为60℃、pH 6.0。它在很宽的ph和温度范围内都非常稳定。添加Ca(2+)、Mg(2+)或山梨糖醇可以有效地提高蛋白酶的热稳定性。PMSF和Hg(2+)抑制了蛋白水解活性,表明存在巯基依赖性丝氨酸蛋白酶。对表面活性剂、漂白剂和溶剂均表现出较高的稳定性。它也与商业洗涤剂(7 mg/mL)兼容,如Ariel、Skip、Drive和Ace,在40°C孵育1小时后,在所有洗涤剂中保持70%以上的蛋白水解活性。洗涤性能分析表明,该蛋白酶能有效去除血渍。从这些性质来看,这种酶可能被认为是未来在生物技术过程中使用的潜在候选者,以及在洗衣粉的配方中。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Bioprocessing of "Hair Waste" by Paecilomyces lilacinus as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis.

Bioprocessing of "Hair Waste" by Paecilomyces lilacinus as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis.

Bioprocessing of "Hair Waste" by Paecilomyces lilacinus as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis.

Bioprocessing of "Hair Waste" by Paecilomyces lilacinus as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis.

Paecilomyces lilacinus (Thom) Samson LPS 876, a locally isolated fungal strain, was grown on minimal mineral medium containing "hair waste," a residue from the hair-saving unhairing process, and produced a protease with keratinolytic activity. This enzyme was biochemically characterized. The optimum reaction conditions, determined with a response surface methodology, were 60°C and pH 6.0. It was remarkably stable in a wide range of pHs and temperatures. Addition of Ca(2+), Mg(2+), or sorbitol was found to be effective in increasing thermal stability of the protease. PMSF and Hg(2+) inhibited the proteolytic activity indicating the presence of a thiol-dependent serine protease. It showed high stability toward surfactants, bleaching agents, and solvents. It was also compatible with commercial detergents (7 mg/mL) such as Ariel, Skip, Drive, and Ace, retaining more than 70% of its proteolytic activity in all detergents after 1 h of incubation at 40°C. Wash performance analysis revealed that this protease could effectively remove blood stains. From these properties, this enzyme may be considered as a potential candidate for future use in biotechnological processes, as well as in the formulation of laundry detergents.

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