Design and characterization of alcalase-chitosan conjugates as potential biocatalysts
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2017
Authors
Zuza, Milena G.Milasinovic, Nikola Z.
Jonović, Marko

Jovanovic, Jelena R.

Kalagasidis Krušić, Melina

Bugarski, Branko

Knežević-Jugović, Zorica

Article (Published version)

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In this study, alcalase (protease from Bacillus licheniformis) immobilization by adsorption, enzyme crosslinking and covalent enzyme binding to activated chitosan microbeads were examined. The biocatalysts highest activity was obtained by covalent immobilization of alcalase onto a solid support. The alcalase covalent immobilization onto different types of chitosan beads obtained by inverse emulsion technique and electrostatic extrusion was studied. Parameters examined under different conditions were beads diameter, enzyme loading, enzyme capacity yield, and biocatalyst activity. The highest activity and enzyme loading of 23.6 IU/mg protein and 340.2 mg/g, respectively, were achieved by the enzyme immobilized onto chitosan microbeads obtained by the electrostatic extrusion technique. FT-IR analysis was used to confirm formation of alcalase-chitosan conjugates. The activity of optimally produced alcalase-chitosan microbeads was then verified in the industrially feasible reaction systems ...of egg white and soy protein hydrolysis. The high degree of hydrolysis of 29.85 +/- 0.967% after 180 min and five successive reuses obtained under real conditions (50 A degrees C, pH 8) verified the covalently bound alcalase to chitosan beads a promising candidate for use in industrial egg white protein hydrolysis process.
Keywords:
Alcalase / Chitosan microbeads / Emulsion technique / Electrostatic extrusion / ImmobilizationSource:
Bioprocess and Biosystems Engineering, 2017, 40, 11, 1713-1723Publisher:
- Springer, New York
Funding / projects:
- Ministry of Education, Science and Technological Development of Serbia
- Ministry of Interior of the Republic of Serbia - 242/16-4-2014
DOI: 10.1007/s00449-017-1826-7
ISSN: 1615-7591
PubMed: 28801712
WoS: 000411189800013
Scopus: 2-s2.0-85027300125
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IHTMTY - JOUR AU - Zuza, Milena G. AU - Milasinovic, Nikola Z. AU - Jonović, Marko AU - Jovanovic, Jelena R. AU - Kalagasidis Krušić, Melina AU - Bugarski, Branko AU - Knežević-Jugović, Zorica PY - 2017 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/2128 AB - In this study, alcalase (protease from Bacillus licheniformis) immobilization by adsorption, enzyme crosslinking and covalent enzyme binding to activated chitosan microbeads were examined. The biocatalysts highest activity was obtained by covalent immobilization of alcalase onto a solid support. The alcalase covalent immobilization onto different types of chitosan beads obtained by inverse emulsion technique and electrostatic extrusion was studied. Parameters examined under different conditions were beads diameter, enzyme loading, enzyme capacity yield, and biocatalyst activity. The highest activity and enzyme loading of 23.6 IU/mg protein and 340.2 mg/g, respectively, were achieved by the enzyme immobilized onto chitosan microbeads obtained by the electrostatic extrusion technique. FT-IR analysis was used to confirm formation of alcalase-chitosan conjugates. The activity of optimally produced alcalase-chitosan microbeads was then verified in the industrially feasible reaction systems of egg white and soy protein hydrolysis. The high degree of hydrolysis of 29.85 +/- 0.967% after 180 min and five successive reuses obtained under real conditions (50 A degrees C, pH 8) verified the covalently bound alcalase to chitosan beads a promising candidate for use in industrial egg white protein hydrolysis process. PB - Springer, New York T2 - Bioprocess and Biosystems Engineering T1 - Design and characterization of alcalase-chitosan conjugates as potential biocatalysts VL - 40 IS - 11 SP - 1713 EP - 1723 DO - 10.1007/s00449-017-1826-7 ER -
@article{ author = "Zuza, Milena G. and Milasinovic, Nikola Z. and Jonović, Marko and Jovanovic, Jelena R. and Kalagasidis Krušić, Melina and Bugarski, Branko and Knežević-Jugović, Zorica", year = "2017", abstract = "In this study, alcalase (protease from Bacillus licheniformis) immobilization by adsorption, enzyme crosslinking and covalent enzyme binding to activated chitosan microbeads were examined. The biocatalysts highest activity was obtained by covalent immobilization of alcalase onto a solid support. The alcalase covalent immobilization onto different types of chitosan beads obtained by inverse emulsion technique and electrostatic extrusion was studied. Parameters examined under different conditions were beads diameter, enzyme loading, enzyme capacity yield, and biocatalyst activity. The highest activity and enzyme loading of 23.6 IU/mg protein and 340.2 mg/g, respectively, were achieved by the enzyme immobilized onto chitosan microbeads obtained by the electrostatic extrusion technique. FT-IR analysis was used to confirm formation of alcalase-chitosan conjugates. The activity of optimally produced alcalase-chitosan microbeads was then verified in the industrially feasible reaction systems of egg white and soy protein hydrolysis. The high degree of hydrolysis of 29.85 +/- 0.967% after 180 min and five successive reuses obtained under real conditions (50 A degrees C, pH 8) verified the covalently bound alcalase to chitosan beads a promising candidate for use in industrial egg white protein hydrolysis process.", publisher = "Springer, New York", journal = "Bioprocess and Biosystems Engineering", title = "Design and characterization of alcalase-chitosan conjugates as potential biocatalysts", volume = "40", number = "11", pages = "1713-1723", doi = "10.1007/s00449-017-1826-7" }
Zuza, M. G., Milasinovic, N. Z., Jonović, M., Jovanovic, J. R., Kalagasidis Krušić, M., Bugarski, B.,& Knežević-Jugović, Z.. (2017). Design and characterization of alcalase-chitosan conjugates as potential biocatalysts. in Bioprocess and Biosystems Engineering Springer, New York., 40(11), 1713-1723. https://doi.org/10.1007/s00449-017-1826-7
Zuza MG, Milasinovic NZ, Jonović M, Jovanovic JR, Kalagasidis Krušić M, Bugarski B, Knežević-Jugović Z. Design and characterization of alcalase-chitosan conjugates as potential biocatalysts. in Bioprocess and Biosystems Engineering. 2017;40(11):1713-1723. doi:10.1007/s00449-017-1826-7 .
Zuza, Milena G., Milasinovic, Nikola Z., Jonović, Marko, Jovanovic, Jelena R., Kalagasidis Krušić, Melina, Bugarski, Branko, Knežević-Jugović, Zorica, "Design and characterization of alcalase-chitosan conjugates as potential biocatalysts" in Bioprocess and Biosystems Engineering, 40, no. 11 (2017):1713-1723, https://doi.org/10.1007/s00449-017-1826-7 . .