Advanced characterization of immobilized enzymes as heterogeneous biocatalysts

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Like in chemical catalysis, there is a clear trend in biocatalysis to carry out synthetic transformations at the manufacturing scale heterogeneously catalyzed. Recycling of insoluble catalysts is simplified, and continuous reactor development thus promoted. Heterogeneous biocatalysis usually involves enzymes immobilized on mesoporous solid supports that offer a large internal surface area. Unraveling enzyme behavior under the confinement of a solid surface and its effect on the catalytic reaction in heterogeneous environment present longstanding core problems of biocatalysis with immobilized enzymes. Progress in deepening the mechanistic understanding of heterogeneous biocatalytic conversions is often restrained by severe limitations in methodology applicable to a direct characterization of solid-supported enzymes. Here we highlight recent evidence from the analysis of protein distribution on porous solid support using microscopic imaging methods with spatiotemporal resolution capability. We also show advance in the use of spectroscopic methods for the analysis of protein conformation on solid support. Methods of direct characterization of activity and stability of immobilized enzymes as heterogeneous biocatalysts are described and their important roles in promoting rational biocatalyst design as well as optimization and control of heterogeneously catalyzed processes are emphasized.

LanguageEnglish
Pages66-80
Number of pages15
JournalCatalysis today
Volume259
DOIs
StatusPublished - 1 Jan 2016

Fingerprint

Immobilized Enzymes
Biocatalysts
Enzymes
Catalyst supports
Proteins
Catalysis
Conformations
Recycling
Catalyst activity
Imaging techniques
Catalysts
Biocatalysis

Keywords

  • Direct characterization
  • Heterogeneous biocatalysis
  • Imaging analysis
  • Immobilized enzymes
  • In operandoa
  • Internal sensing
  • Mesoporous solid support

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Cite this

Advanced characterization of immobilized enzymes as heterogeneous biocatalysts. / Bolivar, Juan M.; Eisl, Ingrid; Nidetzky, Bernd.

In: Catalysis today, Vol. 259, 01.01.2016, p. 66-80.

Research output: Contribution to journalArticleResearchpeer-review

@article{6f40192674dd4889a5c29d79cd73e51b,
title = "Advanced characterization of immobilized enzymes as heterogeneous biocatalysts",
abstract = "Like in chemical catalysis, there is a clear trend in biocatalysis to carry out synthetic transformations at the manufacturing scale heterogeneously catalyzed. Recycling of insoluble catalysts is simplified, and continuous reactor development thus promoted. Heterogeneous biocatalysis usually involves enzymes immobilized on mesoporous solid supports that offer a large internal surface area. Unraveling enzyme behavior under the confinement of a solid surface and its effect on the catalytic reaction in heterogeneous environment present longstanding core problems of biocatalysis with immobilized enzymes. Progress in deepening the mechanistic understanding of heterogeneous biocatalytic conversions is often restrained by severe limitations in methodology applicable to a direct characterization of solid-supported enzymes. Here we highlight recent evidence from the analysis of protein distribution on porous solid support using microscopic imaging methods with spatiotemporal resolution capability. We also show advance in the use of spectroscopic methods for the analysis of protein conformation on solid support. Methods of direct characterization of activity and stability of immobilized enzymes as heterogeneous biocatalysts are described and their important roles in promoting rational biocatalyst design as well as optimization and control of heterogeneously catalyzed processes are emphasized.",
keywords = "Direct characterization, Heterogeneous biocatalysis, Imaging analysis, Immobilized enzymes, In operandoa, Internal sensing, Mesoporous solid support",
author = "Bolivar, {Juan M.} and Ingrid Eisl and Bernd Nidetzky",
year = "2016",
month = "1",
day = "1",
doi = "10.1016/j.cattod.2015.05.004",
language = "English",
volume = "259",
pages = "66--80",
journal = "Catalysis today",
issn = "0920-5861",
publisher = "Elsevier B.V.",

}

TY - JOUR

T1 - Advanced characterization of immobilized enzymes as heterogeneous biocatalysts

AU - Bolivar,Juan M.

AU - Eisl,Ingrid

AU - Nidetzky,Bernd

PY - 2016/1/1

Y1 - 2016/1/1

N2 - Like in chemical catalysis, there is a clear trend in biocatalysis to carry out synthetic transformations at the manufacturing scale heterogeneously catalyzed. Recycling of insoluble catalysts is simplified, and continuous reactor development thus promoted. Heterogeneous biocatalysis usually involves enzymes immobilized on mesoporous solid supports that offer a large internal surface area. Unraveling enzyme behavior under the confinement of a solid surface and its effect on the catalytic reaction in heterogeneous environment present longstanding core problems of biocatalysis with immobilized enzymes. Progress in deepening the mechanistic understanding of heterogeneous biocatalytic conversions is often restrained by severe limitations in methodology applicable to a direct characterization of solid-supported enzymes. Here we highlight recent evidence from the analysis of protein distribution on porous solid support using microscopic imaging methods with spatiotemporal resolution capability. We also show advance in the use of spectroscopic methods for the analysis of protein conformation on solid support. Methods of direct characterization of activity and stability of immobilized enzymes as heterogeneous biocatalysts are described and their important roles in promoting rational biocatalyst design as well as optimization and control of heterogeneously catalyzed processes are emphasized.

AB - Like in chemical catalysis, there is a clear trend in biocatalysis to carry out synthetic transformations at the manufacturing scale heterogeneously catalyzed. Recycling of insoluble catalysts is simplified, and continuous reactor development thus promoted. Heterogeneous biocatalysis usually involves enzymes immobilized on mesoporous solid supports that offer a large internal surface area. Unraveling enzyme behavior under the confinement of a solid surface and its effect on the catalytic reaction in heterogeneous environment present longstanding core problems of biocatalysis with immobilized enzymes. Progress in deepening the mechanistic understanding of heterogeneous biocatalytic conversions is often restrained by severe limitations in methodology applicable to a direct characterization of solid-supported enzymes. Here we highlight recent evidence from the analysis of protein distribution on porous solid support using microscopic imaging methods with spatiotemporal resolution capability. We also show advance in the use of spectroscopic methods for the analysis of protein conformation on solid support. Methods of direct characterization of activity and stability of immobilized enzymes as heterogeneous biocatalysts are described and their important roles in promoting rational biocatalyst design as well as optimization and control of heterogeneously catalyzed processes are emphasized.

KW - Direct characterization

KW - Heterogeneous biocatalysis

KW - Imaging analysis

KW - Immobilized enzymes

KW - In operandoa

KW - Internal sensing

KW - Mesoporous solid support

UR - http://www.scopus.com/inward/record.url?scp=84945485620&partnerID=8YFLogxK

U2 - 10.1016/j.cattod.2015.05.004

DO - 10.1016/j.cattod.2015.05.004

M3 - Article

VL - 259

SP - 66

EP - 80

JO - Catalysis today

T2 - Catalysis today

JF - Catalysis today

SN - 0920-5861

ER -