Feather, as a by-product of the poultry industry, has long been treated as a solid waste, which causes environ- mental and economic problems. In this work, the hydrolyzed feather keratin （HFK） was extracted from the...Feather, as a by-product of the poultry industry, has long been treated as a solid waste, which causes environ- mental and economic problems. In this work, the hydrolyzed feather keratin （HFK） was extracted from the chicken feather using a cost-effective method of alkali-extraction and acid-precipitation by applying urea and sodium sulfide. The aim was development and characterization of the eco-friendly films based on the HFK with variable glycerol contents by a thermoplastic process. The thermal analysis showed that high temperature and high pres- sure improved the compatibility between the glycerol and the HFI（ molecules. Also it was shown that the addi- tion of water is necessary in the hot-pressing process of films, The FT-IR analysis indicated that the formation of the new hydrogen bonds between HFK and glycerol. By increasing the glycerol content, the film tensile strength （orb ） decreases from 10,5 MPa to 5.7 MPa and the solubility increases from 15.3% to 20.9%, while the elongation at break （εb） achieves the maximum value of 63,8% for the film with 35% glycerol. The swelling was just below 16.9% at 25 ℃ for 24 h, suggesting a good stability of the films in water. The water vapor permeability （WVP） varied between 3.02 x 10 ^10g. m 2. s-1 . pa-1 and 4.11 x 10-10g · m-2 · s-1 · Pa-1 for the films with 20%and 40% glycerol, respectively. The HFK film was uniform, translucent and tough, which could be used in packaging and agricultural field.展开更多
Poultry industry produces a vast amount of feather waste annually, which forms a burden for environment protection.However, feathers are valuable bio-resources with high keratinaceous protein content and can be conver...Poultry industry produces a vast amount of feather waste annually, which forms a burden for environment protection.However, feathers are valuable bio-resources with high keratinaceous protein content and can be converted into more valuable materials through some approaches such as biodegradation by microorganism-derived keratinases. The characters of keratinases in microorganisms remain largely undetermined. In this study,it is reported that the morphological change of cell surface and the activities of intracellular and extracellular keratinases in Stenotrophomonas maltophilia( S. maltophilia) DHHJ. S. maltophilia DHHJ was cultured on lysogeny broth( LB) and feather broth(FB) through fermenter technology,and ultrastructure of cell and keratinase activity including extracellular and intracellular enzyme were observed respectively. Ultrastructural change on the cell surface was only observed for the bacteria cultured on FB medium,but not on LB,suggesting that the change could be induced by feather keratin. Therefore, the results showed that extracellular keratinase is a kind of induction enzyme while intracellular keratinase is a kind of constitute enzyme in S. maltophilia DHHJ.展开更多
The aim of this study was to purify and characterize a keratinase produced by a new isolated Bacillus subtilis KD-N2 strain. The keratinase produced by the isolate was purified using ammonium sulphate precipitation, S...The aim of this study was to purify and characterize a keratinase produced by a new isolated Bacillus subtilis KD-N2 strain. The keratinase produced by the isolate was purified using ammonium sulphate precipitation, Sephadex G-75 and DEAE (diethylaminoethyl)-Sepharose chromatographic techniques. The purified enzyme was shown to have a molecular mass of 30.5 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The optimum pH at 50 °C was 8.5 and the optimum temperature at pH 8.5 was 55 °C. The keratinase was partially inactivated by some metal ions, organic solvents and serine protease inhibitor phenylmethanesulfonyl fluoride (PMSF). Sodium dodecyl sulfate (SDS) and ethylene diamine tetraacetic acid (EDTA) had positive effect on the keratinase activity. Reducing agents including dithiothreitol (DTT), mercaptoethanol, L-cysteine, sodium sulphite, as well as chemicals of SDS, ammonium sulfamate and dimethylsulfoxide (DMSO) stimulated the enzyme activity upon a feather meal substrate. Besides feather keratin, the enzyme is active upon the soluble proteins ovalbumin, bovine serum albumin (BSA), casein and insoluble ones as sheep wool and human hair. Calf hair, silk and collagen could not be hydrolyzed by the keratinase.展开更多
基金Supported by the National Natural Science Foundation of China(21176269,31371880,31401526)Higher School Science and Technology Innovation Project of Guangdong Province(2013KJCX0102)Science and Technology Plan Project of Guangdong Province(2013B010403029)
文摘Feather, as a by-product of the poultry industry, has long been treated as a solid waste, which causes environ- mental and economic problems. In this work, the hydrolyzed feather keratin （HFK） was extracted from the chicken feather using a cost-effective method of alkali-extraction and acid-precipitation by applying urea and sodium sulfide. The aim was development and characterization of the eco-friendly films based on the HFK with variable glycerol contents by a thermoplastic process. The thermal analysis showed that high temperature and high pres- sure improved the compatibility between the glycerol and the HFI（ molecules. Also it was shown that the addi- tion of water is necessary in the hot-pressing process of films, The FT-IR analysis indicated that the formation of the new hydrogen bonds between HFK and glycerol. By increasing the glycerol content, the film tensile strength （orb ） decreases from 10,5 MPa to 5.7 MPa and the solubility increases from 15.3% to 20.9%, while the elongation at break （εb） achieves the maximum value of 63,8% for the film with 35% glycerol. The swelling was just below 16.9% at 25 ℃ for 24 h, suggesting a good stability of the films in water. The water vapor permeability （WVP） varied between 3.02 x 10 ^10g. m 2. s-1 . pa-1 and 4.11 x 10-10g · m-2 · s-1 · Pa-1 for the films with 20%and 40% glycerol, respectively. The HFK film was uniform, translucent and tough, which could be used in packaging and agricultural field.
基金National Natural Science Foundations of China(Nos.31000989,31570106)
文摘Poultry industry produces a vast amount of feather waste annually, which forms a burden for environment protection.However, feathers are valuable bio-resources with high keratinaceous protein content and can be converted into more valuable materials through some approaches such as biodegradation by microorganism-derived keratinases. The characters of keratinases in microorganisms remain largely undetermined. In this study,it is reported that the morphological change of cell surface and the activities of intracellular and extracellular keratinases in Stenotrophomonas maltophilia( S. maltophilia) DHHJ. S. maltophilia DHHJ was cultured on lysogeny broth( LB) and feather broth(FB) through fermenter technology,and ultrastructure of cell and keratinase activity including extracellular and intracellular enzyme were observed respectively. Ultrastructural change on the cell surface was only observed for the bacteria cultured on FB medium,but not on LB,suggesting that the change could be induced by feather keratin. Therefore, the results showed that extracellular keratinase is a kind of induction enzyme while intracellular keratinase is a kind of constitute enzyme in S. maltophilia DHHJ.
文摘The aim of this study was to purify and characterize a keratinase produced by a new isolated Bacillus subtilis KD-N2 strain. The keratinase produced by the isolate was purified using ammonium sulphate precipitation, Sephadex G-75 and DEAE (diethylaminoethyl)-Sepharose chromatographic techniques. The purified enzyme was shown to have a molecular mass of 30.5 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The optimum pH at 50 °C was 8.5 and the optimum temperature at pH 8.5 was 55 °C. The keratinase was partially inactivated by some metal ions, organic solvents and serine protease inhibitor phenylmethanesulfonyl fluoride (PMSF). Sodium dodecyl sulfate (SDS) and ethylene diamine tetraacetic acid (EDTA) had positive effect on the keratinase activity. Reducing agents including dithiothreitol (DTT), mercaptoethanol, L-cysteine, sodium sulphite, as well as chemicals of SDS, ammonium sulfamate and dimethylsulfoxide (DMSO) stimulated the enzyme activity upon a feather meal substrate. Besides feather keratin, the enzyme is active upon the soluble proteins ovalbumin, bovine serum albumin (BSA), casein and insoluble ones as sheep wool and human hair. Calf hair, silk and collagen could not be hydrolyzed by the keratinase.
