Optimization of the process of enzymatic hydrolysis of keratin-containing stock aimed at obtaining hydrolysates of high biological value has been performed. The increasing of the stock/water weight ratio, the amount of the alkaline protease preparation from Acremonium chrysogenium added and the temperature of the reaction mixture resulted in an increase in the yield and antioxidant capacity of hydrolysis products. The molecular masses of soluble products obtained under optimal hydrolysis conditions ranged from 3.55 to 3.60 kDa. High antioxidant capacity, 100% bioavailability and a well-balanced amino acid composition was characteristic of the hydrolysis products.
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Polymers (Basel)
November 2022
Department of Applied Chemistry, College of Chemistry and Chemical Engineering, Qinghai Normal University, 38 Wusi West Road, Xining 810008, China.
The recycling, development, and application of keratin-containing waste (e.g., hair, wool, feather, and so on) provide an important means to address related environmental pollution and energy shortage issues.
View Article and Find Full Text PDFJ Biosci Bioeng
April 2014
Laboratory of Applied Biochemistry and Microbiology (LABM), Faculty of Science of Annaba (FSA), Badji Mokhtar-Annaba University, P.O. Box 12, 23000 Annaba, Algeria. Electronic address:
An extracellular thermostable keratinase (KERAK-29) was purified and biochemically characterized from a thermophilic actinomycete Actinomadura keratinilytica strain Cpt29 newly isolated from Algerian poultry compost. The isolate exhibited high keratinase production when grown in chicken feather meal media (24,000 U/ml). Based on matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis, the purified enzyme is a monomer with a molecular mass of 29,233.
View Article and Find Full Text PDFJ Basic Microbiol
February 2013
Department of Biotechnology, Shivaji University, Kolhapur, India.
In the present study, a feather degrading bacterial strain was isolated from poultry waste disposal site, Kolhapur, India. The bacterium was identified as Chryseobacterium sp. RBT using 16S rRNA gene sequence analysis.
View Article and Find Full Text PDFInt J Trichology
January 2010
Department of Medicine, University of Melbourne, St Vincent's Hospital, Melbourne 3065, Australia 5005.
The concept of bioprospecting for bioactive peptides from keratin-containing materials such as wool, hair, skin and feathers presents an exciting opportunity for discovery of novel functional food ingredients and nutraceuticals, while value-adding to cheap and plentiful natural sources. The published literature reports multiple examples of proline-rich peptides with productive bio-activity in models of human disease including tumour formation, hypertension control and Alzheimer's disease. Bioactive peptides have been identified from food and other protein sources however the bioactivity of keratin-related proteins and peptides is largely unknown.
View Article and Find Full Text PDFPrikl Biokhim Mikrobiol
February 2010
Optimization of the process of enzymatic hydrolysis of keratin-containing stock aimed at obtaining hydrolysates of high biological value has been performed. The increasing of the stock/water weight ratio, the amount of the alkaline protease preparation from Acremonium chrysogenium added and the temperature of the reaction mixture resulted in an increase in the yield and antioxidant capacity of hydrolysis products. The molecular masses of soluble products obtained under optimal hydrolysis conditions ranged from 3.
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