The DOI matches its Crossref record; 92 of the 92 references it cites were found in a registry or an index.
Review: Engineering of thermostable enzymes for industrial applications
Open accessAbstract
The catalytic properties of some selected enzymes have long been exploited to carry out efficient and cost-effective bioconversions in a multitude of research and industrial sectors, such as food, health, cosmetics, agriculture, chemistry, energy, and others. Nonetheless, for several applications, naturally occurring enzymes are not considered to be viable options owing to their limited stability in the required working conditions. Over the years, the quest for novel enzymes with actual potential for biotechnological applications has involved various complementary approaches such as mining enzyme variants from organisms living in extreme conditions (extremophiles), mimicking evolution in the laboratory to develop more stable enzyme variants, and more recently, using rational, computer-assisted enzyme engineering strategies. In this review, we provide an overview of the most relevant enzymes that are used for industrial applications and we discuss the strategies that are adopted to enhance enzyme stability and/or activity, along with some of the most relevant achievements. In all living species, many different enzymes catalyze fundamental chemical reactions with high substrate specificity and rate enhancements. Besides specificity, enzymes also possess many other favorable properties, such as, for instance, cost-effectiveness, good stability under mild pH and temperature conditions, generally low toxicity levels, and ease of termination of activity. As efficient natural biocatalysts, enzymes provide great opportunities to carry out important chemical reactions in several research and industrial settings, ranging from food to pharmaceutical, cosmetic, agricultural, and other crucial economic sectors.
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1 retracted
RETRACTED: Strategies for design of improved biocatalysts for industrial applications
Madhavan, A., Sindhu, R., Binod, P., Sukumaran, R. K., & Pandey, A. (2017) · Bioresource Technology · doi:10.1016/j.biortech.2017.05.031 · Cited by 204
RetractedEnvironmental, economic, and energetic costs and benefits of biodiesel and ethanol biofuels
Hill, J., Nelson, E., Tilman, D., Polasky, S., & Tiffany, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604600103 · Cited by 2,871
Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability
Vieille, C., & Zeikus, G. J. (2001) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.65.1.1-43.2001 · Cited by 2,123
Industrial applications of microbial lipases
Hasan, F., Shah, A. A., & Hameed, A. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2005.10.016 · Cited by 1,951
A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis
Kendrew, J. C., Bodo, G., Dintzis, H. M., Parrish, R. G., Wyckoff, H., & Phillips, D. C. (1958) · Nature · doi:10.1038/181662a0 · Cited by 1,669
Programming cells by multiplex genome engineering and accelerated evolution
Wang, H. H., Isaacs, F. J., Carr, P. A., Sun, Z. Z., Xu, G., Forest, C. R., & Church, G. M. (2009) · Nature · doi:10.1038/nature08187 · Cited by 1,529
Jaeger, K.-E., & Eggert, T. (2002) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(02)00341-5 · Cited by 1,376
Industrial and biotechnological applications of laccases: A review
Rodríguez Couto, S., & Toca Herrera, J. L. (2006) · Biotechnology Advances · doi:10.1016/j.biotechadv.2006.04.003 · Cited by 1,296
Protein stability promotes evolvability
Bloom, J. D., Labthavikul, S. T., Otey, C. R., & Arnold, F. H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510098103 · Cited by 1,211
De Novo Protein Design: Fully Automated Sequence Selection
Dahiyat, B. I., & Mayo, S. L. (1997) · Science · doi:10.1126/science.278.5335.82 · Cited by 1,145
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Scarabelli, G., Oloo, E. O., Maier, J. K. X., & Rodriguez-Granillo, A. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167375 · Cited by 33
Platero-Rochart, D., Krivobokova, T., Gastegger, M., Reibnegger, G., & Sánchez-Murcia, P. A. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c00772 · Cited by 15
(2022) · doi:10.1002/pro.4557 · Cited by 12
Metadata
- Authors
- Rigoldi, F., Donini, S., Redaelli, A., Parisini, E., & Gautieri, A.
- Venue
- APL Bioengineering
- Publisher
- AIP Publishing
- Published
- 2018-01-11
- Volume
- 2
- Issue
- 1
- Pages
- 011501-011501
- ISSN
- 2473-2877 (ISSN-L)
- OpenAlex
- W2782655885
- Cited by
- 313
- References
- 92
- FWCI
- 10.12
- Type
- journal article
- Language
- en
- Open access
- gold
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- Rigoldi, F., Donini, S., Redaelli, A., Parisini, E., & Gautieri, A. (2018). Review: Engineering of thermostable enzymes for industrial applications. APL Bioengineering. https://doi.org/10.1063/1.4997367
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.