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新埃及分离株(嗜糖乳杆菌YNDH)产生的蛋白酶/角蛋白酶的高效多功能生物技术应用

Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH).

作者信息

Goda Doaa A, Bassiouny Ahmad R, Abdel Monem Nihad M, Soliman Nadia A, Abdel Fattah Yasser R

机构信息

Bioprocess Development Department, Genetic Engineering and Biotechnology Research Institute (GEBRI), City of Scientific Research and Technological Applications (SRTA-City), New Burg El-Arab City, Universities and Research Institutes Zone, Alexandria, Post 21934, Egypt.

Biochemistry Department, Faculty of Science, Alexandria, Egypt.

出版信息

J Genet Eng Biotechnol. 2020 Jul 2;18(1):23. doi: 10.1186/s43141-020-00037-7.

DOI:10.1186/s43141-020-00037-7
PMID:32617705
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7332587/
Abstract

BACKGROUND

Due to a multitude of industrial applications of keratinolytic proteases, their demands are increasing. The present investigation studied the production and monitoring of the most possible multi-functional applications of YNDH thermoalkaline keratin-degrading enzyme.

RESULTS

This work is considered the first that reported YNDH strain closely related to Laceyella sacchari strain; YNDH is a producer of protease/keratinase enzyme and able to degrade natural keratin such as feathers, wool, human hairs, and nails. Experimental design Plackett-Burman (PBD) was applied to evaluate culture conditions affecting the production of thermoalkaline protease/keratinase. Afterwards, Box-Behnken design (BBD) was applied to find out the optimum level of significant variables namely, NHCl, yeast extract, and NaNO3 with a predicted activity of 1324.7 U/ml. Accordingly, the following medium composition and parameters were calculated to be optimum (%w/v): NH4Cl, 0.08; feather, 1; yeast extract, 0.04; MgSO.7HO, 0.02; NaNO, 0.016; KHPO, 0.01; KHPO 0.01; pH, 8; inoculum size; 5%, cultivation temperature (Temp.) 45 °C and incubation time 48 h. The studied enzyme can degrade keratin-azure, remove proteinaceous materials, and is able to remove hairs from goat hides. These interesting characteristics make this enzyme a good candidate in many applications especially in detergent (Det.), in leather industries, and in pharmaceuticals particularly in nail treatment.

CONCLUSION

The promising properties of the newly keratin-degrading protease enzyme from Laceyella sacchari strain YNDH would underpin its efficient exploitation in several industries to cope with the demands of worldwide enzyme markets.

摘要

背景

由于角蛋白分解蛋白酶在众多工业应用中,其需求量不断增加。本研究对YNDH热碱性角蛋白降解酶最可能的多功能应用进行了生产和监测。

结果

本研究首次报道了与嗜糖拉氏菌菌株密切相关的YNDH菌株;YNDH是一种蛋白酶/角蛋白酶的生产者,能够降解天然角蛋白,如羽毛、羊毛、人发和指甲。采用Plackett-Burman(PBD)实验设计评估影响热碱性蛋白酶/角蛋白酶生产的培养条件。之后,应用Box-Behnken设计(BBD)找出显著变量(即氯化铵、酵母提取物和硝酸钠)的最佳水平,预测活性为1324.7 U/ml。据此,计算出以下培养基组成和参数为最佳(%w/v):氯化铵0.08;羽毛1;酵母提取物0.04;硫酸镁·7水合物0.02;硝酸钠0.016;磷酸二氢钾0.01;磷酸氢二钾0.01;pH值8;接种量5%;培养温度(Temp.)45°C;培养时间48小时。所研究的酶能够降解角蛋白天青、去除蛋白质物质,并且能够去除山羊皮上的毛发。这些有趣的特性使该酶在许多应用中成为良好的候选者,特别是在洗涤剂(Det.)、皮革工业和制药行业,尤其是在指甲治疗方面。

结论

来自嗜糖拉氏菌菌株YNDH的新型角蛋白降解蛋白酶的优良特性将支持其在多个行业中的有效开发,以满足全球酶市场的需求。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/21b95e869f6c/43141_2020_37_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/8fee7a2e57aa/43141_2020_37_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/3cab64279794/43141_2020_37_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/c562900c3dd1/43141_2020_37_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/940ed68e6702/43141_2020_37_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/21b95e869f6c/43141_2020_37_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/8fee7a2e57aa/43141_2020_37_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/3cab64279794/43141_2020_37_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/c562900c3dd1/43141_2020_37_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/940ed68e6702/43141_2020_37_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6b85/7332587/21b95e869f6c/43141_2020_37_Fig5_HTML.jpg

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