Details
| Original language | English |
|---|---|
| Pages (from-to) | 527-538 |
| Number of pages | 12 |
| Journal | Engineering in life sciences |
| Volume | 21 |
| Issue number | 8-9 |
| Early online date | 9 Jul 2021 |
| Publication status | Published - 22 Sept 2021 |
Abstract
As an alternative to classical batch processes, enzyme-catalyzed hydrolysis can also be carried out continuously. To facilitate this, a continuous ceramic capillary membrane reactor system (CCCMRS) was developed which can be operated with various proteolytic enzymes immobilized on the porous ceramic capillary membranes. This system has several advantages over common batch processes regarding stability, reproducibility and controllability and can easily be adapted to optimal reaction conditions and individual preferences. Two exemplary applications utilizing the CCCMRS were carried out and investigated in long-term stability studies. In the first application the continuous enzymatic cleavage of human IgG into the antibody fragments Fab and Fc by immobilized papain was performed. A total volume of 22 mL of 1 mg mL-1 IgG-solution was enzymatically cleaved over a period of 33.3 h. The antibody cleavage products could be detected in an SEC-HPLC over the whole process time thus indicating long-term stability of the continuous hydrolysis process. The second application investigated the continuous digestion of pea and almond protein isolates by immobilized Alcalase resulting in the generation of a large variety of different peptides. This peptide fingerprint remains constant over a long period of time enabling fractionation and thus making the peptides accessible for further bioactivity studies in sufficient quantities. The constant peptide fingerprint could be shown in the RP-HPLC analysis for all 30 samples with a total volume of 29.7 mL collected over a period of 45 h.
Keywords
- antibody fragments, bioactive peptides, food proteins, immobilized enzymes, proteolysis
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
- Environmental Science(all)
- Environmental Engineering
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In: Engineering in life sciences, Vol. 21, No. 8-9, 22.09.2021, p. 527-538.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A versatile ceramic capillary membrane reactor system for continuous enzyme-catalyzed hydrolysis
AU - Messner, Lorn
AU - Antink, Marieke H.
AU - Guo, Tongwei
AU - Maas, Michael
AU - Beutel, Sascha
N1 - Funding Information: This project was funded by the German Research Foundation (DFG Project Number 278836263 “Proteolytic ceramic capillary membranes for the preparative production of bioactive peptides”)
PY - 2021/9/22
Y1 - 2021/9/22
N2 - As an alternative to classical batch processes, enzyme-catalyzed hydrolysis can also be carried out continuously. To facilitate this, a continuous ceramic capillary membrane reactor system (CCCMRS) was developed which can be operated with various proteolytic enzymes immobilized on the porous ceramic capillary membranes. This system has several advantages over common batch processes regarding stability, reproducibility and controllability and can easily be adapted to optimal reaction conditions and individual preferences. Two exemplary applications utilizing the CCCMRS were carried out and investigated in long-term stability studies. In the first application the continuous enzymatic cleavage of human IgG into the antibody fragments Fab and Fc by immobilized papain was performed. A total volume of 22 mL of 1 mg mL-1 IgG-solution was enzymatically cleaved over a period of 33.3 h. The antibody cleavage products could be detected in an SEC-HPLC over the whole process time thus indicating long-term stability of the continuous hydrolysis process. The second application investigated the continuous digestion of pea and almond protein isolates by immobilized Alcalase resulting in the generation of a large variety of different peptides. This peptide fingerprint remains constant over a long period of time enabling fractionation and thus making the peptides accessible for further bioactivity studies in sufficient quantities. The constant peptide fingerprint could be shown in the RP-HPLC analysis for all 30 samples with a total volume of 29.7 mL collected over a period of 45 h.
AB - As an alternative to classical batch processes, enzyme-catalyzed hydrolysis can also be carried out continuously. To facilitate this, a continuous ceramic capillary membrane reactor system (CCCMRS) was developed which can be operated with various proteolytic enzymes immobilized on the porous ceramic capillary membranes. This system has several advantages over common batch processes regarding stability, reproducibility and controllability and can easily be adapted to optimal reaction conditions and individual preferences. Two exemplary applications utilizing the CCCMRS were carried out and investigated in long-term stability studies. In the first application the continuous enzymatic cleavage of human IgG into the antibody fragments Fab and Fc by immobilized papain was performed. A total volume of 22 mL of 1 mg mL-1 IgG-solution was enzymatically cleaved over a period of 33.3 h. The antibody cleavage products could be detected in an SEC-HPLC over the whole process time thus indicating long-term stability of the continuous hydrolysis process. The second application investigated the continuous digestion of pea and almond protein isolates by immobilized Alcalase resulting in the generation of a large variety of different peptides. This peptide fingerprint remains constant over a long period of time enabling fractionation and thus making the peptides accessible for further bioactivity studies in sufficient quantities. The constant peptide fingerprint could be shown in the RP-HPLC analysis for all 30 samples with a total volume of 29.7 mL collected over a period of 45 h.
KW - antibody fragments
KW - bioactive peptides
KW - food proteins
KW - immobilized enzymes
KW - proteolysis
UR - http://www.scopus.com/inward/record.url?scp=85109390770&partnerID=8YFLogxK
U2 - 10.1002/elsc.202100027
DO - 10.1002/elsc.202100027
M3 - Article
AN - SCOPUS:85109390770
VL - 21
SP - 527
EP - 538
JO - Engineering in life sciences
JF - Engineering in life sciences
SN - 1618-0240
IS - 8-9
ER -