A two-step response surface methodology (RSM) study was conducted for the optimization of keratinase production and enzyme activity from poultry feather by Streptomyces sp7. Initially different combinations of salts were screened for maximal production of keratinase at a constant pH of 6.5 and feather meal concentration of 5 g/L. A combination of K2HPO4, KH2PO4, and NaCl gave a maximum yield of keratinase (70.9 U/mL) production. In the first step of the RSM study, the selected five variables (feather meal, K2HPO4, KH2PO4, NaCl, and pH) were optimized by a 25 full-factorial rotatable central composite design (CCD) that resulted in 95 U/mL of keratinase production. The results of analysis of variance and regression of a second-order model showed that the linear effects of feather meal concentration (p<0.005) and NaCl (p<0.029) and the interactive effects of all variables were more significant and that values of the quadratic effects of feather meal (p<1.72e-5), K2HPO4 (p<4.731e-6), KH2PO4 (p<1.01e-10), and pH (p 7.63e-7) were more significant than the linear and interactive effects of the process variables. In the second step, a 23 rotatable full-factorial CCD and response surface analysis were used for the selection of optimal process parameters (pH, temperature, and rpm) for keratinase enzyme activity. These optima were pH 11.0, 45 degrees C, and 300 rpm.
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http://dx.doi.org/10.1007/BF02729061 | DOI Listing |
J Agric Food Chem
January 2025
College of Light Industry and Food Engineering, Guangxi University, Nanning 530004, People's Republic of China.
Keratinases are valuable enzymes for converting feather keratin waste into bioactive products but often suffer from poor substrate specificity and low catalytic efficiency. This study reported the creating of a novel keratinase with targeted adherence and specific degradation on feather keratins by fusing prepeptidase C-Terminal (PPC) domain. A PPC domain of metalloprotease E423 specifically adsorbed feather keratins by hydrogen bonds and hydrophobic interactions in a time- and temperature-dependent manner.
View Article and Find Full Text PDFWorld J Microbiol Biotechnol
December 2024
Facultad de Ciencias Exactas, Instituto de Investigaciones para la Industria Química (INIQUI), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Universidad Nacional de Salta, Salta, 4400, Argentina.
Leather industry is traditionally characterized by the use of large amounts of chemical agents, some of which are toxic to human health and the environment. However, during the last years, many efforts have been made with the aim of successfully implement enzymes as agents for different leather production stages. The lipopeptides produced by the Bacillus spp.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Faculty of Life Science and Technology, Kunming University of Science and Technology, Kunming 650500, China. Electronic address:
PLoS One
October 2024
Laboratory for Genetics and Biochemistry of Microorganisms, National Center for Biotechnology, Astana, Kazakhstan.
Keratinases, a subclass of proteases, are used to degrade keratin thereby forming peptones and free amino acids. Bacillus paralicheniformis strain T7 was isolated from soil and exhibited high keratinase, protease, collagenase, amylase, xylanase, lipase, and phosphatase activities. Keratinases of the strain showed maximum activity at 70°C and pH 9.
View Article and Find Full Text PDFFront Biosci (Elite Ed)
July 2024
School of Biochemistry and Biotechnology, University of the Punjab, 54590 Lahore, Pakistan.
Background: Chicken feathers contribute to large quantities of keratinaceous wastes that pose serious environmental problems and must be catered to properly. Chicken feathers are also a potential source of vital proteins, peptides, and amino acids, which could be used as low-cost animal feeds. Therefore, there has been increasing interest in keratinase-producing microbes for reprocessing and using keratinous biomaterials.
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