Understanding the Basis of Occurrence, Biosynthesis, and Implications of Thermostable Alkaline Proteases

التفاصيل البيبلوغرافية
العنوان: Understanding the Basis of Occurrence, Biosynthesis, and Implications of Thermostable Alkaline Proteases
المؤلفون: Rakeshkumar Ramanlal Panchal, Prashant Arya, Shivani M Yagnik, Vikram H Raval, Kiransinh N. Rajput
المصدر: Applied Biochemistry and Biotechnology. 193:4113-4150
بيانات النشر: Springer Science and Business Media LLC, 2021.
سنة النشر: 2021
مصطلحات موضوعية: Proteases, Hot Temperature, medicine.medical_treatment, Bioengineering, Biology, Protein Engineering, Applied Microbiology and Biotechnology, Biochemistry, chemistry.chemical_compound, Biosynthesis, Enzyme Stability, medicine, Molecular Biology, chemistry.chemical_classification, Protease, Hydrolysis, Thermophile, Proteolytic enzymes, General Medicine, Protein engineering, Industrial enzymes, Cysteine Endopeptidases, Enzyme, chemistry, Biochemical engineering, Biotechnology
الوصف: The group of hydrolytic enzymes synonymously known as proteases is predominantly most favored for the class of industrial enzymes. The present work focuses on the thermostable nature of these proteolytic enzymes that occur naturally among mesophilic and thermophilic microbes. The broad thermo-active feature (40-80 °C), ease of cultivation, maintenance, and bulk production are the key features associated with these enzymes. Detailing of contemporary production technologies, and controllable operational parameters including the purification strategies, are the key features that justify their industrial dominance as biocatalysts. In addition, the rigorous research inputs by protein engineering and enzyme immobilization studies add up to the thermo-catalytic features and application capabilities of these enzymes. The work summarizes key features of microbial proteases that make them numero-uno for laundry, biomaterials, waste management, food and feed, tannery, and medical as well as pharmaceutical industries. The quest for novel and/or designed and engineered thermostable protease from unexplored sources is highly stimulating and will address the ever-increasing industrial demands.
تدمد: 1559-0291
0273-2289
DOI: 10.1007/s12010-021-03701-x
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18ee9c862ba405755695318964ae028a
https://doi.org/10.1007/s12010-021-03701-x
Rights: CLOSED
رقم الانضمام: edsair.doi.dedup.....18ee9c862ba405755695318964ae028a
قاعدة البيانات: OpenAIRE
الوصف
تدمد:15590291
02732289
DOI:10.1007/s12010-021-03701-x