Immobilization with Ca–Alg@gelatin hydrogel beads enhances the activity and stability of recombinant thermoalkalophilic lipase

• Autorzy: Yildiz Dalginli Kezban , Atakisi Onur

Identyfikatory

DOI

10.24425/cpe.2023.142291

• Języki publikacji: EN

Abstrakty

EN

This study aims at the immobilization and characterization of thermoalkalophilic lipases produced recombinantly from Bacillus thermocatenulatus BTL2 and Bacillus pumilus MBB03. For this purpose, immobilization of the produced enzymes in calcium-alginate@gelatin (Ca–Alg@gelatin) hydrogel beads, immobilization optimization and characterization measurements of the immobilized-enzyme hydrogels were conducted. Optimum temperature and pH values were determined for B. thermocatenulatus and B. pumilus MBB03 immobilized-enzyme hydrogels (60–70 °C, 55 °C and pH 9.5, pH 8.5). Thermal stability was determined between 65 °C and 60 °C of B. thermocatenulatus and B. pumilus MBB03 immobilized enzymes, respectively. The pH stability was determined between pH 7.0–11.0 at +4°C and pH 8.0–10.0 at +4 °C, respectively. In conclusion, the entrapment technique provided controlled production of small diameter hydrogel beads (~ 0:19 and ~ 0:29) with negligible loss of enzyme. These beads retained high lipase activity at high pH and temperature. The activity of Ca–Alg@gelatin-immobilized lipase remained relatively stable for up to three cycles and then markedly decreased. With this enzyme immobilization, it may have a potential for use in esterification and transesterification reactions carried out in organic solvent environments. We can conclude that it is one of the most promising techniques for highly efficient and economically competent biotechnological processes in the field of biotransformation, diagnostics, pharmaceutical, food and detergent industries.

Słowa kluczowe

EN

alginate; gelatin; hydrogel beads; thermoalkalophilic lipase; immobilization; characterization

PL

alginian; żelatyna; koraliki hydrożelowe; unieruchomienie; charakteryzacja

• Wydawca: Komitet Inżynierii Chemicznej i Procesowej Polskiej Akademii Nauk
• Czasopismo: Chemical and Process Engineering : New Frontiers
• Rocznik: 2023
• Tom: Vol. 44, nr 1
• Strony: art. no. e2
• Opis fizyczny: Bibliogr. 49 poz., rys., tab.

Twórcy

autor

Yildiz Dalginli Kezban

• Department of Chemistry and Chemical Processing Technologies, Kars Vocational High School Kafkas University, Kars, Turkey

• https://orcid.org/0000-0002-1483-348X

autor

Atakisi Onur

• Department of Chemistry, Faculty Science and Letter, Kafkas University, Kars, Turkey

• https://orcid.org/0000-0003-1183-6076

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Uwagi

Opracowanie rekordu ze środków MEiN, umowa nr SONP/SP/546092/2022 w ramach programu "Społeczna odpowiedzialność nauki" - moduł: Popularyzacja nauki i promocja sportu (2022-2023).