The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Enzymes and Bioconversions of Industrial, Pharmaceutical, and Biotechnological Significance
Abstract
Enzymes are an important part of industry due to their many favorable properties. The development of industrial enzymes has depended heavily on the use of microbial sources. Microbes are useful because they can be produced economically in short fermentations and inexpensive media. Screening is simple, and strain improvement for increased production has been very successful. In the 1980s and 1990s, microbial enzymes replaced many plant and animal enzymes. They have found use in many industries including food, detergents, textiles, leather, pulp and paper, diagnostics, and therapy. The development of recombinant DNA technology had a major effect on production levels of enzymes as their genes were transferred from native species into industrial strains. Over 50% of the enzyme market is provided by recombinant enzymes. In many cases, enzymes have also been used to carry out conversions that were synthetic in previous years. Accompanying this trend is the use of whole cells to carry out bioconversions. Bioconversions have become very important to industry especially because of the demand for single isomer intermediates.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Further, recombinant enzymes and/or their immobilisation is possible to improve the performance 108-111 .”
From Degradation of anthraquinone dyes from effluents: A review focusing on enzymatic dye degradation with industrial potential (2020) · cites this paper as [109]
In the citing paper
“On the other hand, some enzymes may require co-factors or mediators 17 and may be too specific/selective to degrade multiple dyes simultaneously 108, 109 .”
From Degradation of anthraquinone dyes from effluents: A review focusing on enzymatic dye degradation with industrial potential (2020) · cites this paper as [109]
Citations
Cites
Improving enzymes by using them in organic solvents
Klibanov, A. M. (2001) · Nature · doi:10.1038/35051719 · Cited by 2,172
Bacterial alkaline proteases: molecular approaches and industrial applications
R., G., Q., B., & P., L. (2002) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-002-0975-y · Cited by 1,603
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
Microbial lipases form versatile tools for biotechnology
Jaeger, K. (1998) · Trends in Biotechnology · doi:10.1016/s0167-7799(98)01195-0 · Cited by 1,041
Enzymes for chemical synthesis
Koeller, K. M., & Wong, C.-H. (2001) · Nature · doi:10.1038/35051706 · Cited by 894
Enzymatic catalysis in monophasic organic solvents
Dordick, J. S. (1989) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(89)90094-x · Cited by 870
Biotechnology—a sustainable alternative for chemical industry
Gavrilescu, M., & Chisti, Y. (2005) · Biotechnology Advances · doi:10.1016/j.biotechadv.2005.03.004 · Cited by 713
Metagenomics and industrial applications
Lorenz, P., & Eck, J. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1161 · Cited by 559
Microbial alkaline pectinases and their industrial applications: a review
Hoondal, G. S., Tiwari, R., Tewari, R., Dahiya, N., & Beg, Q. K. (2002) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-002-1061-1 · Cited by 459
A green-by-design biocatalytic process for atorvastatin intermediate
Ma, S. K., Gruber, J., Davis, C., Newman, L., Gray, D., Wang, A., Grate, J., Huisman, G. W., & Sheldon, R. A. (2010) · Green Chem. · doi:10.1039/b919115c · Cited by 440
Phytases: Microbial Sources, Production, Purification, and Potential Biotechnological Applications
Vohra, A., & Satyanarayana, T. (2003) · Critical Reviews in Biotechnology · doi:10.1080/713609297 · Cited by 422
Encyclopedia of chemical processing
(2006) · Choice Reviews Online · doi:10.5860/choice.43-5632 · Cited by 416
Directed enzyme evolution: climbing fitness peaks one amino acid at a time
Tracewell, C. A., & Arnold, F. H. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.01.017 · Cited by 321
Biotechnological production and applications of phytases
Haefner, S., Knietsch, A., Scholten, E., Braun, J., Lohscheidt, M., & Zelder, O. (2005) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-005-0005-y · Cited by 284
Asymmetric Catalysis on Industrial Scale
(2003) · Wiley eBooks · doi:10.1002/3527602151 · Cited by 278
Biocatalysis in development of green pharmaceutical processes
Tao, J., & Xu, J. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.01.018 · Cited by 239
Advances in laboratory evolution of enzymes
Bershtein, S., & Tawfik, D. S. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.01.027 · Cited by 227
Mining enzymes from extreme environments
Ferrer, M., Golyshina, O. V., Beloqui, A., & Golyshin, P. N. (2007) · Current Opinion in Microbiology · doi:10.1016/j.mib.2007.05.004 · Cited by 223
Directed evolution of enzymes and biosynthetic pathways
Johannes, T. W., & Zhao, H. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.03.003 · Cited by 207
Handbook of Industrial Mycology
(2004) · CRC Press eBooks · doi:10.1201/9780203970553 · Cited by 204
Laboratory-Directed Protein Evolution
Yuan, L., Kurek, I., English, J., & Keenan, R. J. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.3.373-392.2005 · Cited by 200
Microbial transformations of nitriles
NAGASAWA, T. (1989) · Trends in biotechnology · doi:10.1016/0167-7799(89)90026-7 · Cited by 194
Enzyme Applications in Detergency and in Manufacturing Industries
Galante, Y. M., & Formantici, C. (2003) · Current Organic Chemistry · doi:10.2174/1385272033486468 · Cited by 177
Mayer, A. F., Hellmuth, K., Schlieker, H., Lopez‐Ulibarri, R., Oertel, S., Dahlems, U. M., Strasser, A., & van Loon, A. P. G. M. (1999) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19990505)63:3<373::aid-bit14>3.0.co;2-t · Cited by 148
Enhanced vanillin production from ferulic acid using adsorbent resin
Hua, D., Ma, C., Song, L., Lin, S., Zhang, Z., Deng, Z., & Xu, P. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0735-5 · Cited by 146
Synthesis of an aspartame precursor by immobilized thermolysin in an organic solvent
Oyama, K., Nishimura, S., Nonaka, Y., Kihara, K., & Hashimoto, T. (1981) · The Journal of Organic Chemistry · doi:10.1021/jo00338a045 · Cited by 128
Hummel, W., Sch�tte, H., Schmidt, E., Wandrey, C., & Kula, M. (1987) · Applied Microbiology and Biotechnology · doi:10.1007/bf00253523 · Cited by 127
Solbak, A. I., Richardson, T. H., Mccann, R. T., Kline, K., Bartnek, F., Tomlinson, G., Tan, X., Parra-Gessert, L., Frey, G., Podar, M., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411838200 · Cited by 121
Hua, D., Ma, C., Lin, S., Song, L., Deng, Z., Maomy, Z., Zhang, Z., Yu, B., & Xu, P. (2007) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2007.05.003 · Cited by 115
Little, D. B., & Croteau, R. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00068-1 · Cited by 109
Cowan, D. A. (1996) · Trends in biotechnology · doi:10.1016/0167-7799(96)30009-7 · Cited by 107
Production and characterization of a milk-clotting enzyme from Aspergillus oryzae MTCC 5341
Vishwanatha, K. S., Rao, A. G. A., & Singh, S. A. (2009) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-009-2197-z · Cited by 102
Piddington, C. S., Houston, C. S., Paloheimo, M., Cantrell, M. A., Miettinen‐Oinonen, A., Nevalainen, H. K. M., & Rambosek, J. A. (1993) · Gene · doi:10.1016/0378-1119(93)90224-q · Cited by 101
Reetz, M. T. (2009) · The Journal of Organic Chemistry · doi:10.1021/jo901046k · Cited by 100
‘Designer reagents’ recombinant microorganisms: new and powerful tools for organic synthesis
Kayser, M. M. (2008) · Tetrahedron · doi:10.1016/j.tet.2008.10.039 · Cited by 97
Manufacture of l-amino acids with bioreactors
Hamilton, B. K., Hsiao, H., Swann, W. E., Anderson, D. M., & Delente, J. J. (1985) · Trends in biotechnology · doi:10.1016/0167-7799(85)90079-4 · Cited by 89
LEE, E.-G., Yoon, S., Das, A., Lee, S., Li, C., Kim, J., Choi, M., Oh, D., & Kim, S.-W. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.22040 · Cited by 86
Continuous production of L-malic acid by immobilized cells
Chibata, I., Tosa, T., & Takata, I. (1983) · Trends in biotechnology · doi:10.1016/0167-7799(83)90019-7 · Cited by 72
Zhao, L., Sun, Z., Zheng, P., & He, J. (2006) · Process Biochemistry · doi:10.1016/j.procbio.2006.02.007 · Cited by 71
Hydratases involved in nitrile conversion: Screening, characterization and application
Yamada, H., Shimizu, S., & Kobayashi, M. (2001) · The Chemical Record · doi:10.1002/tcr.5 · Cited by 69
Yamada, M. C., Okada, Y., Yoshida, T., & Nagasawa, T. (2007) · Biotechnology Letters · doi:10.1007/s10529-007-9602-4 · Cited by 67
Siehl, D. L., Castle, L. A., Gorton, R., Chen, Y. H., Bertain, S., Cho, H., Keenan, R. J., Liu, D., & Lassner, M. (2005) · Pest Management Science · doi:10.1002/ps.1014 · Cited by 60
Production of Vanillin by Metabolically Engineered Escherichia coli
Yoon, S., Li, C., Kim, J., Lee, S.-H., Yoon, J., Choi, M.-S., Seo, W. T., Yang, J., Kim, J.-Y., & Kim, S.-W. (2005) · Biotechnology Letters · doi:10.1007/s10529-005-3561-4 · Cited by 59
Microbial Biocatalytic Processes and Their Development
Woodley, J. M. (2006) · Advances in applied microbiology · doi:10.1016/s0065-2164(06)60001-4 · Cited by 59
The Production of L–Phenylalanine by Polyazetidine Immobilized Microbes
Calton, G. J., Wood, L. L., Updike, M. H., Lantz, L., & Hamman, J. P. (1986) · Nature Biotechnology · doi:10.1038/nbt0486-317 · Cited by 56
Dehydrogenation of ribitol with Gluconobacter oxydans: Production and stability of l-ribulose
Muynck, C. D., Pereira, C., Soetaert, W., & Vandamme, E. J. M. C. (2006) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2006.03.017 · Cited by 54
Directed evolution and characterization of Escherichia coli glucosamine synthase
Deng, M.-D., Grund, A. D., Wassink, S. L., Peng, S. S., Nielsen, K. L., Huckins, B. D., Walsh, B. L., & Burlingame, R. P. (2005) · Biochimie · doi:10.1016/j.biochi.2005.10.002 · Cited by 48
L-Phenylalanine formation from acetamidocinnamic acid by newly isolated bacteria
Nakamichi, K., Nabe, K., Yamada, S., Tosa, T., & Chibata, I. (1984) · Applied Microbiology and Biotechnology · doi:10.1007/bf00302448 · Cited by 35
Enzymatic production of L ‐serine with a feedback control system for formaldehyde addition
Hsiao, H., & WEI, T. T. (1986) · Biotechnology and Bioengineering · doi:10.1002/bit.260281009 · Cited by 30
Outer membrane mutation effects on UDP-glucose permeability and whole-cell catalysis rate
Ni, Y., Mao, Z., & Chen, R. R. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0485-4 · Cited by 29
Development of bioreactor system for L-tyrosine synthesis using thermostable tyrosine phenol-lyase.
Kim, D. Y., Rha, E., Choi, S., Song, J., Hong, S.-P., Sung, M., & Lee, S. (2007) · PubMed · Cited by 26
Wiebe, M. G., Mojžita, D., Hilditch, S., Ruohonen, L., & Penttilä, M. E. (2010) · BMC Biotechnology · doi:10.1186/1472-6750-10-63 · Cited by 25
Effects of magnesium ion and chelating agents on enzymatic production of ATP from adenine
Fujio, T., & Furuya, A. (1985) · Applied Microbiology and Biotechnology · doi:10.1007/bf00295109 · Cited by 22
A Novel, Efficient Biotransformation for the Production of L–Phenylalanine
Evans, C. T., Bellamy, W., Gleeson, M. A. G., Aoki, H., Hanna, K., Peterson, W., Conrad, D., & Misawa, M. (1987) · Nature Biotechnology · doi:10.1038/nbt0887-818 · Cited by 18
Enzymatic production of L ‐serine
Hsiao, H., WEI, T. T., & Campbell, K. (1986) · Biotechnology and Bioengineering · doi:10.1002/bit.260280613 · Cited by 15
Companies Turn To Biocatalysis
ROGERS, R. S. (1999) · Chemical & Engineering News · doi:10.1021/cen-v077n029.p087 · Cited by 13
Stabilization of anE. coli plasmid by a mini-F fragment of DNA
Yukawa, H., Kurusu, Y., Shimazu, M., et al. (1988) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/bf01569570 · Cited by 10
Microbial process for L-cysteine production
Dhillon, G. S., Nagasawa, T., & Yamada, H. (1987) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(87)90003-2 · Cited by 9
Izumi, Y., Nath, P. K., Yamamoto, H., & Yamada, H. (1989) · Applied Microbiology and Biotechnology · doi:10.1007/bf00296621 · Cited by 3
Research works printed but not linked: 9
- Hasan F., 2010, African J. Biotechnol., 9, 4836
- Kim D. Y., 2007, J. Microbiol. Biotechnol., 17, 116
- Vandamme E. J., 2006, Chem. Today, 24, 57
- Guagliardi A., 1989, Chim. Oggi./Chem. Today, 31
- Yokozeki K., 1987, Agric. Biol. Chem., 51, 29
- Calton G. J., 1986, Bio/Technology, 4, 317
- Evans C. T., 1987, Bio/Technology, 5, 818
- Fujio T., 1983, J. Ferm. Technol., 61, 261
- Fujio T., 1984, J. Ferm. Technol., 62, 131
Cited by
Routoula, E., & Patwardhan, S. V. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.9b03737 · Cited by 579
Metadata
- Authors
- Sanchez, S., & Demain, A. L.
- Venue
- Organic Process Research & Development
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-12-10
- Volume
- 15
- Issue
- 1
- Pages
- 224-230
- ISSN
- 1083-6160
- 1520-586X
- Cited by
- 189
- References
- 59
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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.