Trehalose hydrogels for stabilization of enzymes to heat
Enzymes can catalyze various reactions with high selectivity and are involved in many important biological processes. However, the general instability of enzymes against high temperature often limits their application. To address this, we synthesized a trehalose-based hydrogel in two steps from comm...
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| Published in | Polymer chemistry Vol. 6; no. 18; pp. 3443 - 3448 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
14.05.2015
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Enzymes can catalyze various reactions with high selectivity and are involved in many important biological processes. However, the general instability of enzymes against high temperature often limits their application. To address this, we synthesized a trehalose-based hydrogel in two steps from commercial starting materials with minimal purification procedures. Mono- and multi-functional trehalose monomers were cross-linked by redox-initiated radical polymerization to form a hydrogel. Phytase, an important enzyme utilized in animal feedstock, was employed to study the effectiveness of the trehalose hydrogel to stabilize proteins against heat. Addition of the phytase solution to the hydrogel resulted in enzyme internalization as confirmed by confocal microscopy. The phytase in the hydrogel retained 100% activity upon heating at 90 °C compared to 39% when the hydrogel was absent. The enzyme could also be recovered from the hydrogel. The trehalose hydrogel synthesis reported herein should be readily scalable for thermal stabilization of a wide variety of enzymes. |
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| AbstractList | Enzymes can catalyze various reactions with high selectivity and are involved in many important biological processes. However, the general instability of enzymes against high temperature often limits their application. To address this, we synthesized a trehalose-based hydrogel in two steps from commercial starting materials with minimal purification procedures. Mono- and multi-functional trehalose monomers were cross-linked by redox-initiated radical polymerization to form a hydrogel. Phytase, an important enzyme utilized in animal feedstock, was employed to study the effectiveness of the trehalose hydrogel to stabilize proteins against heat. Addition of the phytase solution to the hydrogel resulted in enzyme internalization as confirmed by confocal microscopy. The phytase in the hydrogel retained 100% activity upon heating at 90 °C compared to 39% when the hydrogel was absent. The enzyme could also be recovered from the hydrogel. The trehalose hydrogel synthesis reported herein should be readily scalable for thermal stabilization of a wide variety of enzymes. Enzymes can catalyze various reactions with high selectivity and are involved in many important biological processes. However, the general instability of enzymes against high temperature often limits their application. To address this, we synthesized a trehalose-based hydrogel in two steps from commercial starting materials with minimal purification procedures. Mono- and multi-functional trehalose monomers were cross-linked by redox-initiated radical polymerization to form a hydrogel. Phytase, an important enzyme utilized in animal feedstock, was employed to study the effectiveness of the trehalose hydrogel to stabilize proteins against heat. Addition of the phytase solution to the hydrogel resulted in enzyme internalization as confirmed by confocal microscopy. The phytase in the hydrogel retained 100% activity upon heating at 90 degree C compared to 39% when the hydrogel was absent. The enzyme could also be recovered from the hydrogel. The trehalose hydrogel synthesis reported herein should be readily scalable for thermal stabilization of a wide variety of enzymes. Enzymes can catalyze various reactions with high selectivity and are involved in many important biological processes. However, the general instability of enzymes against high temperature often limits their application. To address this, we synthesized a trehalose-based hydrogel in two steps from commercial starting materials with minimal purification procedures. Mono- and multi-functional trehalose monomers were cross-linked by redox-initiated radical polymerization to form a hydrogel. Phytase, an important enzyme utilized in animal feedstock, was employed to study the effectiveness of the trehalose hydrogel to stabilize proteins against heat. Addition of the phytase solution to the hydrogel resulted in enzyme internalization as confirmed by confocal microscopy. The phytase in the hydrogel retained 100% activity upon heating at 90 °C compared to 39% when the hydrogel was absent. The enzyme could also be recovered from the hydrogel. The trehalose hydrogel synthesis reported herein should be readily scalable for thermal stabilization of a wide variety of enzymes.Enzymes can catalyze various reactions with high selectivity and are involved in many important biological processes. However, the general instability of enzymes against high temperature often limits their application. To address this, we synthesized a trehalose-based hydrogel in two steps from commercial starting materials with minimal purification procedures. Mono- and multi-functional trehalose monomers were cross-linked by redox-initiated radical polymerization to form a hydrogel. Phytase, an important enzyme utilized in animal feedstock, was employed to study the effectiveness of the trehalose hydrogel to stabilize proteins against heat. Addition of the phytase solution to the hydrogel resulted in enzyme internalization as confirmed by confocal microscopy. The phytase in the hydrogel retained 100% activity upon heating at 90 °C compared to 39% when the hydrogel was absent. The enzyme could also be recovered from the hydrogel. The trehalose hydrogel synthesis reported herein should be readily scalable for thermal stabilization of a wide variety of enzymes. |
| Author | Wallace, Peter Ko, Jeong Hoon Maynard, Heather D. Lee, Juneyoung Lin, En-Wei Ruch, Frank |
| AuthorAffiliation | a Department of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive East, Los Angeles, California 90095-1569 b Phytex LLC, 214 S. Main Street, Sheridan, Indiana 46069 |
| AuthorAffiliation_xml | – name: b Phytex LLC, 214 S. Main Street, Sheridan, Indiana 46069 – name: a Department of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive East, Los Angeles, California 90095-1569 |
| Author_xml | – sequence: 1 givenname: Juneyoung surname: Lee fullname: Lee, Juneyoung organization: Department of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, USA – sequence: 2 givenname: Jeong Hoon surname: Ko fullname: Ko, Jeong Hoon organization: Department of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, USA – sequence: 3 givenname: En-Wei surname: Lin fullname: Lin, En-Wei organization: Department of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, USA – sequence: 4 givenname: Peter surname: Wallace fullname: Wallace, Peter organization: Phytex LLC, Sheridan, USA – sequence: 5 givenname: Frank surname: Ruch fullname: Ruch, Frank organization: Phytex LLC, Sheridan, USA – sequence: 6 givenname: Heather D. surname: Maynard fullname: Maynard, Heather D. organization: Department of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26005500$$D View this record in MEDLINE/PubMed |
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| Snippet | Enzymes can catalyze various reactions with high selectivity and are involved in many important biological processes. However, the general instability of... |
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| SubjectTerms | Enzymes Heating Hydrogels Instability Phytase Polymerization Stabilization Trehalose |
| Title | Trehalose hydrogels for stabilization of enzymes to heat |
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