<abstract xmlns="http://www.w3.org/1999/xhtml"><p>Enzymatic preparation from culture of keratinolytic <italic>Bacillus cereus</italic> PCM 2849 was applied for hydrolysis of whole chicken feathers, after sulphitolytic pretreatment. This process was optimized using a three-factor Box-Behnken design, where the effect of substrate concentration, sulphite concentration during pretreatment and reaction temperature was evaluated on the release of amino acids. Obtained results revealed the highest impact of reaction temperature, followed by substrate content and sulphite during pretreatment. Optimal process conditions were established, i.e. temperature 44.4°C, feathers 4.7% and treatment with 25.3 mM sulphite. Amino acid composition of the obtained hydrolysate was analyzed. Glutamic acid (9.21 g·kg<sup>−1</sup>) and proline were dominant, however significant amount of branched-chain amino acids was also observed. The FTIR analysis of residual substrate revealed the cleavage of disulphide bonds in keratin through the presence of thioester residues. The absence of reduced cysteine residues was confirmed, along with minor changes in proportions of keratin substructures.</p></abstract>

Enzymatic preparation from culture of keratinolytic Bacillus cereus PCM 2849 was applied for hydrolysis of whole chicken feathers, after sulphitolytic pretreatment. This process was optimized using a three-factor Box-Behnken design, where the effect of substrate concentration, sulphite concentration during pretreatment and reaction temperature was evaluated on the release of amino acids. Obtained results revealed the highest impact of reaction temperature, followed by substrate content and sulphite during pretreatment. Optimal process conditions were established, i.e. temperature 44.4°C, feathers 4.7% and treatment with 25.3 mM sulphite. Amino acid composition of the obtained hydrolysate was analyzed. Glutamic acid (9.21 g·kg−1) and proline were dominant, however significant amount of branched-chain amino acids was also observed. The FTIR analysis of residual substrate revealed the cleavage of disulphide bonds in keratin through the presence of thioester residues. The absence of reduced cysteine residues was confirmed, along with minor changes in proportions of keratin substructures.

Enzymatic bioconversion of feather waste with keratinases of <italic>Bacillus cereus</italic> PCM 2849

Wrocław University of Environmental and Life Sciences

Department of Biotechnology and Food Microbiology, Faculty of Biotechnology and Food Science

“Poltegor-Institute”, Opencast Mining Institute

Polish Journal of Chemical Technology

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Enzymatic bioconversion of feather waste with keratinases of  PCM 2849

Enzymatic preparation from culture of keratinolytic Bacillus cereus PCM 2849 was applied for hydrolysis of whole chicken feathers, after sulphitolytic...

Enzymatic bioconversion of feather waste with keratinases of Bacillus cereus PCM 2849

Publicado en línea: 26 sept 2019

Páginas: 53 - 59

DOI: https://doi.org/10.2478/pjct-2019-0030

Palabras clave
feather waste, Box-Behnken design, hydrolysis, thermo-chemical pretreatment

© 2019 Dominika P. Ciurko et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Enzymatic bioconversion of feather waste with keratinases of Bacillus cereus PCM 2849

Publicado en línea: 26 sept 2019

Páginas: 53 - 59

DOI: https://doi.org/10.2478/pjct-2019-0030

Palabras clavefeather waste, Box-Behnken design, hydrolysis, thermo-chemical pretreatment

© 2019 Dominika P. Ciurko et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Palabras clave
feather waste, Box-Behnken design, hydrolysis, thermo-chemical pretreatment