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| Main Authors: | , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Current microbiology
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41186749/ |
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| _version_ | 1868266130312790017 |
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| author | Salem, Gad Elsayed Mohamed Arif, Muhammad Idris, Imad A El-Sakhawy, Mohamed A Chavanich, Suchana Alahmad, Waleed Zheng, Yuanzhang Salama, El-Sayed |
| author_facet | Salem, Gad Elsayed Mohamed Arif, Muhammad Idris, Imad A El-Sakhawy, Mohamed A Chavanich, Suchana Alahmad, Waleed Zheng, Yuanzhang Salama, El-Sayed Salem, Gad Elsayed Mohamed Arif, Muhammad Idris, Imad A El-Sakhawy, Mohamed A Chavanich, Suchana Alahmad, Waleed Zheng, Yuanzhang Salama, El-Sayed |
| collection | PubMed - marine biology |
| contents | Microbial Proteases: Integration into Food Products and Industrial Processes. Salem, Gad Elsayed Mohamed Arif, Muhammad Idris, Imad A El-Sakhawy, Mohamed A Chavanich, Suchana Alahmad, Waleed Zheng, Yuanzhang Salama, El-Sayed Peptide Hydrolases Bacteria Fungi Food Handling Yeasts Industrial Microbiology Microbial proteases offer significant advantages over conventional chemical methods due to their non-toxicity, biodegradability, and low energy requirements. This review comprehensively examines the production of proteases from bacteria, fungi, and yeast, and explores their diverse industrial applications. Established uses include food processing, leather processing, bioremediation, detergent formulation, waste management, and textile manufacturing. The review highlights emerging applications such as silk fiber degumming and silver recovery from X-ray film waste. Microbial proteases operate under diverse temperature and pH conditions, enabling their adaptation to a wide range of industrial processes. Notable examples include keratinases for leather and laundry applications, and specialized proteases for gluten-free food production. Future research should focus on identifying polyextremophile sources and developing techniques to improve enzyme efficiency for industrial scalability. |
| format | Artículo científico |
| id | pubmed_41186749 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Current microbiology |
| record_format | pubmed |
| spellingShingle | Microbial Proteases: Integration into Food Products and Industrial Processes. Salem, Gad Elsayed Mohamed Arif, Muhammad Idris, Imad A El-Sakhawy, Mohamed A Chavanich, Suchana Alahmad, Waleed Zheng, Yuanzhang Salama, El-Sayed Peptide Hydrolases Bacteria Fungi Food Handling Yeasts Industrial Microbiology Microbial Proteases: Integration into Food Products and Industrial Processes. Salem, Gad Elsayed Mohamed Arif, Muhammad Idris, Imad A El-Sakhawy, Mohamed A Chavanich, Suchana Alahmad, Waleed Zheng, Yuanzhang Salama, El-Sayed Peptide Hydrolases Bacteria Fungi Food Handling Yeasts Industrial Microbiology Microbial proteases offer significant advantages over conventional chemical methods due to their non-toxicity, biodegradability, and low energy requirements. This review comprehensively examines the production of proteases from bacteria, fungi, and yeast, and explores their diverse industrial applications. Established uses include food processing, leather processing, bioremediation, detergent formulation, waste management, and textile manufacturing. The review highlights emerging applications such as silk fiber degumming and silver recovery from X-ray film waste. Microbial proteases operate under diverse temperature and pH conditions, enabling their adaptation to a wide range of industrial processes. Notable examples include keratinases for leather and laundry applications, and specialized proteases for gluten-free food production. Future research should focus on identifying polyextremophile sources and developing techniques to improve enzyme efficiency for industrial scalability. |
| title | Microbial Proteases: Integration into Food Products and Industrial Processes. |
| topic | Peptide Hydrolases Bacteria Fungi Food Handling Yeasts Industrial Microbiology |
| url | https://pubmed.ncbi.nlm.nih.gov/41186749/ |