Cargando…

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

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 i...

Descripción completa

Detalles Bibliográficos
Autores principales: Goda, Doaa A., Bassiouny, Ahmad R., Abdel Monem, Nihad M., Soliman, Nadia A., Abdel Fattah, Yasser R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7332587/
https://www.ncbi.nlm.nih.gov/pubmed/32617705
http://dx.doi.org/10.1186/s43141-020-00037-7
_version_ 1783553557002190848
author Goda, Doaa A.
Bassiouny, Ahmad R.
Abdel Monem, Nihad M.
Soliman, Nadia A.
Abdel Fattah, Yasser R.
author_facet Goda, Doaa A.
Bassiouny, Ahmad R.
Abdel Monem, Nihad M.
Soliman, Nadia A.
Abdel Fattah, Yasser R.
author_sort Goda, Doaa A.
collection PubMed
description 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, NH(4)Cl, 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(4).7H(2)O, 0.02; NaNO(3), 0.016; KH(2)PO(4), 0.01; K(2)HPO(4,) 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.
format Online
Article
Text
id pubmed-7332587
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher Springer Berlin Heidelberg
record_format MEDLINE/PubMed
spelling pubmed-73325872020-07-10 Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH) Goda, Doaa A. Bassiouny, Ahmad R. Abdel Monem, Nihad M. Soliman, Nadia A. Abdel Fattah, Yasser R. J Genet Eng Biotechnol Research 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, NH(4)Cl, 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(4).7H(2)O, 0.02; NaNO(3), 0.016; KH(2)PO(4), 0.01; K(2)HPO(4,) 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. Springer Berlin Heidelberg 2020-07-02 /pmc/articles/PMC7332587/ /pubmed/32617705 http://dx.doi.org/10.1186/s43141-020-00037-7 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Research
Goda, Doaa A.
Bassiouny, Ahmad R.
Abdel Monem, Nihad M.
Soliman, Nadia A.
Abdel Fattah, Yasser R.
Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH)
title Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH)
title_full Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH)
title_fullStr Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH)
title_full_unstemmed Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH)
title_short Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate (Laceyella sacchari YNDH)
title_sort effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new egyptian isolate (laceyella sacchari yndh)
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7332587/
https://www.ncbi.nlm.nih.gov/pubmed/32617705
http://dx.doi.org/10.1186/s43141-020-00037-7
work_keys_str_mv AT godadoaaa effectivemultifunctionalbiotechnologicalapplicationsofproteasekeratinaseenzymeproducedbynewegyptianisolatelaceyellasacchariyndh
AT bassiounyahmadr effectivemultifunctionalbiotechnologicalapplicationsofproteasekeratinaseenzymeproducedbynewegyptianisolatelaceyellasacchariyndh
AT abdelmonemnihadm effectivemultifunctionalbiotechnologicalapplicationsofproteasekeratinaseenzymeproducedbynewegyptianisolatelaceyellasacchariyndh
AT solimannadiaa effectivemultifunctionalbiotechnologicalapplicationsofproteasekeratinaseenzymeproducedbynewegyptianisolatelaceyellasacchariyndh
AT abdelfattahyasserr effectivemultifunctionalbiotechnologicalapplicationsofproteasekeratinaseenzymeproducedbynewegyptianisolatelaceyellasacchariyndh