Valorisation of protein waste: An enzymatic approach to make commodity chemicals? ?

Please wait a minute...

Shopping Cart Email List Chinese

Advanced Search Fig/Tab

Frontiers of Chemical Science and Engineering

ISSN 2095-0179

ISSN 2095-0187(Online)

CN 11-5981/TQ

Postal Subscription Code 80-969

2018 Impact Factor: 2.809

Featured Articles | Most Downloaded | Most Reading

Online Submission Free E-mail Alert Subscribe to Our RSS Content Feed

Front. Chem. Sci. Eng.

2015, Vol. 9

Issue (3) : 295-307 https://doi.org/10.1007/s11705-015-1532-4

REVIEW ARTICLE

Valorisation of protein waste: An enzymatic approach to make commodity chemicals? ?

Madura B. A. Kumar¹,Yuan Gao²,Wei Shen¹,Lizhong He^1,^*(

)

1. Department of Chemical Engineering, Monash University, Clayton, VIC 3800, Australia
2. Manufacturing Flagship, Commonwealth Scientific and Industrial Research Organization, Bayview Avenue, Clayton, VIC 3168, Australia

Download: PDF(310 KB) HTML
Export: BibTeX | EndNote | Reference Manager | ProCite | RefWorks

Abstract

Protein-rich waste is an abundantly available resource that is currently used mainly as animal feed and fertilizers. Valorisation of protein waste to higher value products, particularly commodity chemicals such as precursors for polymers, has attracted significant research efforts. Enzyme-based approaches, being environmentally-friendly compared to their chemical counterparts, promise sustainable processes for conversion of protein waste to valuable chemicals. This review provides a general overview on valorisation of protein waste and then further summarises the use of enzymes in different stages of the valorisation process—protein extraction and hydrolysis, separation of individual amino acids and their ultimate conversion into chemicals. Case studies of enzymatic conversion are presented for different amino acids including glutamic acid, lysine, phenylalanine, tyrosine, arginine and aspartic acid. The review compares the different enzyme reactors and operation modes for amino acid conversion. The emerging opportunities and challenges in the field are discussed: engineering powerful enzymes and integrating innovative processes for industrial application at a low cost.

Keywords amino acids protein waste reactor conversion commodity chemicals enzymes

Corresponding Author(s): Lizhong He

Online First Date: 24 September 2015 Issue Date: 30 September 2015

Cite this article:

Madura B. A. Kumar,Yuan Gao,Wei Shen, et al. Valorisation of protein waste: An enzymatic approach to make commodity chemicals? ?[J]. Front. Chem. Sci. Eng., 2015, 9(3): 295-307.

URL:

https://academic.hep.com.cn/fcse/EN/10.1007/s11705-015-1532-4
https://academic.hep.com.cn/fcse/EN/Y2015/V9/I3/295

Tab.1 Amino acid content of some common protein-rich wastes (mass % of amino acids in protein waste)^a)

Tab.2 Typical enzymes used in protein hydrolysis

Tab.3 A summary of enzymatic conversions of amino acids to chemicals

Fig.1 Conversion of glutamic acid to γ-aminobutyric acid and α-ketoglutaric acid

Fig.2 Conversion of lysine to 5-aminovaleric acid and cadaverine

Fig.3 Conversion of phenylalanine to cinnamic acid and tyrosine to para-hydroxycinnamic acid

Fig.4 Conversion of arginine to ornithine to diaminobutane

Fig.5 Conversion of aspartic acid to β-alanine

1	Tuck C O, Pérez E, Horváth I T, Sheldon R A, Poliakoff M. Valorization of biomass: Deriving more value from waste. Science, 2012, 337(6095): 695–699 https://doi.org/10.1126/science.1218930
2	Lammens T M, Franssen M C R, Scott E L, Sanders J P M. Availability of protein-derived amino acids as feedstock for the production of bio-based chemicals. Biomass and Bioenergy, 2012, 44: 168–181 https://doi.org/10.1016/j.biombioe.2012.04.021
3	Sanders J, Scott E, Weusthuis R, Mooibroek H. Bio-refinery as the bio-inspired process to bulk chemicals. Macromolecular Bioscience, 2007, 7(2): 105–117 https://doi.org/10.1002/mabi.200600223
4	Nyachoti C M, House J D, Slominski B A, Seddon I R. Energy and nutrient digestibilities in wheat dried distillers’ grains with solubles fed to growing pigs. Journal of the Science of Food and Agriculture, 2005, 85(15): 2581–2586 https://doi.org/10.1002/jsfa.2305
5	Gunkel G, Kosmol J, Sobral M, Rohn H, Montenegro S, Aureliano J. Sugar cane industry as a source of water pollution—Case study on the situation in Ipojuca river, Pernambuco, Brazil. Water, Air, and Soil Pollution, 2007, 180(1-4): 261–269 https://doi.org/10.1007/s11270-006-9268-x
6	Regulation (EC) No 1069/2009 of the European Parliament and of the Council, <day>21</day> <month>October</month> 2009. Laying down health rules as regards animal by-products and derived products not intended for human consumption and repealing Regulation (EC) No 1774/2002 (Animal by-products Regulation)
7	Bals B D, Dale B E. Developing a model for assessing biomass processing technologies within a local biomass processing depot. Bioresource Technology, 2012, 106: 161–169 https://doi.org/10.1016/j.biortech.2011.12.024
8	Simon R D, Weathers P. Determination of the structure of the novel polypeptide containing aspartic acid and arginine which is found in cyanobacteria. BBA—Protein Structure, 1976, 420(1): 165–176
9	Obst M, Steinbüchel A. Microbial degradation of poly (amino acid)s. Biomacromolecules, 2004, 5(4): 1166–1176 https://doi.org/10.1021/bm049949u
10	Könst P M, Turras P M C C D, Franssen M C R, Scott E L, Sanders J P M. Stabilized and immobilized Bacillus subtilis arginase for the biobased production of nitrogen-containing chemicals. Advanced Synthesis & Catalysis, 2010, 352(9): 1493–1502 https://doi.org/10.1002/adsc.201000034
11	Yasmin A, Sadiq Butt M, Sameen A, Shahid M. Physicochemical and amino acid profiling of cheese whey. Pakistan Journal of Nutrition, 2013, 12(5): 455–459 https://doi.org/10.3923/pjn.2013.455.459
12	Sari Y W, Alting A C, Floris R, Sanders J P M, Bruins M E. Glutamic acid production from wheat by-products using enzymatic and acid hydrolysis. Biomass and Bioenergy, 2014, 67: 451–459 https://doi.org/10.1016/j.biombioe.2014.05.018
13	Karr-Lilienthal L K, Grieshop C M, Spears J K, Fahey G C Jr. Amino acid, carbohydrate, and fat composition of soybean meals prepared at 55 commercial U.S. soybean processing plants. Journal of Agricultural and Food Chemistry, 2005, 53(6): 2146–2150 https://doi.org/10.1021/jf048385i
14	Latshaw J D, Musharaf N, Retrum R. Processing of feather meal to maximize its nutritional value for poultry. Animal Feed Science and Technology, 1994, 47(3-4): 179–188 https://doi.org/10.1016/0377-8401(94)90122-8
15	Chang S K, Ismail A, Yanagita T, Esa N M, Baharuldin M T H. Biochemical characterisation of the soluble proteins, protein isolates and hydrolysates from oil palm (Elaeis guineensis) kernel. Food Bioscience, 2014, 7: 1–10 https://doi.org/10.1016/j.fbio.2014.05.003
16	Han J, Liu K. Changes in composition and amino acid profile during dry grind ethanol processing from corn and estimation of yeast contribution toward DDGS proteins. Journal of Agricultural and Food Chemistry, 2010, 58(6): 3430–3437 https://doi.org/10.1021/jf9034833
17	Meussen B J, van Zeeland A N T, Bruins M E, Sanders J P M. A fast and accurate UPLC method for analysis of proteinogenic amino acids. Food Analytical Methods, 2014, 7(5): 1047–1055 https://doi.org/10.1007/s12161-013-9712-7
18	Scott E, Peter F, Sanders J. Biomass in the manufacture of industrial products-the use of proteins and amino acids. Applied Microbiology and Biotechnology, 2007, 75(4): 751–762 https://doi.org/10.1007/s00253-007-0932-x
19	Hu C, Reddy N, Luo Y, Yan K, Yang Y. Thermoplastics from acetylated zein-and-oil-free corn distillers dried grains with solubles. Biomass and Bioenergy, 2011, 35(2): 884–892 https://doi.org/10.1016/j.biombioe.2010.11.006
20	Lammens T M, Nôtre J L, Franssen M C R, Scott E L, Sanders J P M. Synthesis of biobased succinonitrile from glutamic acid and glutamine. ChemSusChem, 2011, 4(6): 785–791 https://doi.org/10.1002/cssc.201100030
21	Ogata K, Uchiyama K, Yamada H. Microbial formation of cinnamic acid from phenylalanine. Agricultural and Biological Chemistry, 1966, 30(3): 311–312 https://doi.org/10.1271/bbb1961.30.311
22	Schneider J, Wendisch V F. Biotechnological production of polyamines by Bacteria: Recent achievements and future perspectives. Applied Microbiology and Biotechnology, 2011, 91(1): 17–30 https://doi.org/10.1007/s00253-011-3252-0
23	Schneider J, Wendisch V F. Putrescine production by engineered Corynebacterium glutamicum. Applied Microbiology and Biotechnology, 2010, 88(4): 859–868 https://doi.org/10.1007/s00253-010-2778-x
24	Arifin B, Bono A, Farm Y Y, Ling A L L, Fui S Y. Protein extraction from palm kernel meal. Journal of Applied Sciences, 2009, 9(17): 2996–3004 https://doi.org/10.3923/jas.2009.2996.3004
25	Bals B, Teachworth L, Dale B, Balan V. Extraction of proteins from switchgrass using aqueous ammonia within an integrated biorefinery. Applied Biochemistry and Biotechnology, 2007, 143(2): 187–198 https://doi.org/10.1007/s12010-007-0045-0
26	Gu Z, Glatz C E. Aqueous two-phase extraction for protein recovery from corn extracts. Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, 2007, 845(1): 38–50 https://doi.org/10.1016/j.jchromb.2006.07.025
27	Fountoulakis M, Lahm H W. Hydrolysis and amino acid composition analysis of proteins. Journal of Chromatography. A, 1998, 826(2): 109–134 https://doi.org/10.1016/S0021-9673(98)00721-3
28	Ozols J. Amino acid analysis. Methods in Enzymology, 1990, 182: 587–601 https://doi.org/10.1016/0076-6879(90)82046-5
29	Provansal M M P, Cuq J L A, Cheftel J C. Chemical and nutritional modifications of sunflower proteins due to alkaline processing formation of amino acid cross-links and isomerization of lysine residues. Journal of Agricultural and Food Chemistry, 1975, 23(5): 938–943 https://doi.org/10.1021/jf60201a030
30	Sari Y W, Bruins M E, Sanders J P M. Enzyme assisted protein extraction from rapeseed, soybean, and microalgae meals. Industrial Crops and Products, 2013, 43(1): 78–83 https://doi.org/10.1016/j.indcrop.2012.07.014
31	Bals B, Brehmer B, Dale B, Sanders J. Protease digestion from wheat stillage within a dry grind ethanol facility. Biotechnology Progress, 2011, 27(2): 428–434 https://doi.org/10.1002/btpr.521
32	Brandelli A, Daroit D J, Riffel A. Biochemical features of microbial keratinases and their production and applications. Applied Microbiology and Biotechnology, 2010, 85(6): 1735–1750 https://doi.org/10.1007/s00253-009-2398-5
33	Tavano O L. Protein hydrolysis using proteases: An important tool for food biotechnology. Journal of Molecular Catalysis. B, Enzymatic, 2013, 90: 1–11 https://doi.org/10.1016/j.molcatb.2013.01.011
34	O’Loughlin I B, Murray B A, Kelly P M, FitzGerald R J, Brodkorb A. Enzymatic hydrolysis of heat-induced aggregates of whey protein isolate. Journal of Agricultural and Food Chemistry, 2012, 60(19): 4895–4904 https://doi.org/10.1021/jf205213n
35	Hara Y. The separation of amino acids with an ion-exchange membrane. Bulletin of the Chemical Society of Japan, 1963, 36(11): 1373–1376 https://doi.org/10.1246/bcsj.36.1373
36	Sandeaux J, Fares A, Sandeaux R, Gavach C. Transport properties of electrodialysis membranes in the presence of arginine I. Equilibrium properties of a cation exchange membrane in an aqueous solution of arginine chlorhydrate and sodium chloride. Journal of Membrane Science, 1994, 89(1-2): 73–81 https://doi.org/10.1016/0376-7388(93)E0204-W
37	Kattan Readi O M, Gironès M, Nijmeijer K. Separation of complex mixtures of amino acids for biorefinery applications using electrodialysis. Journal of Membrane Science, 2013, 429: 338–348 https://doi.org/10.1016/j.memsci.2012.11.053
38	Readi O M K, Gironès M, Wiratha W, Nijmeijer K. On the isolation of single basic amino acids with electrodialysis for the production of biobased chemicals. Industrial & Engineering Chemistry Research, 2013, 52(3): 1069–1078 https://doi.org/10.1021/ie202634v
39	Teng Y, Scott E L, Van Zeeland A N T, Sanders J P M. The use of L-lysine decarboxylase as a means to separate amino acids by electrodialysis. Green Chemistry, 2011, 13(3): 624–630 https://doi.org/10.1039/c0gc00611d
40	Kattan Readi O M, Rolevink E, Nijmeijer K. Mixed matrix membranes for process intensification in electrodialysis of amino acids. Journal of Chemical Technology and Biotechnology (Oxford, Oxfordshire), 2014, 89(3): 425–435 https://doi.org/10.1002/jctb.4135
41	Yvon M, Rijnen L. Cheese flavour formation by amino acid catabolism. International Dairy Journal, 2001, 11(4–7): 185–201 https://doi.org/10.1016/S0958-6946(01)00049-8
42	Lammens T M, De Biase D, Franssen M C R, Scott E L, Sanders J P M. The application of glutamic acid α-decarboxylase for the valorization of glutamic acid. Green Chemistry, 2009, 11(10): 1562–1567 https://doi.org/10.1039/b913741f
43	De Biase D, Tramonti A, John R A, Bossa F. Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli. Protein Expression and Purification, 1996, 8(4): 430–438 https://doi.org/10.1006/prep.1996.0121
44	Kang T J, Ho N A T, Pack S P. Buffer-free production of gamma-aminobutyric acid using an engineered glutamate decarboxylase from Escherichia coli. Enzyme and Microbial Technology, 2013, 53(3): 200–205 https://doi.org/10.1016/j.enzmictec.2013.04.006
45	Thu Ho N A, Hou C Y, Kim W H, Kang T J. Expanding the active pH range of Escherichia coli glutamate decarboxylase by breaking the cooperativeness. Journal of Bioscience and Bioengineering, 2013, 115(2): 154–158 https://doi.org/10.1016/j.jbiosc.2012.09.002
46	Dinh T H, Ho N A T, Kang T J, McDonald K A, Won K. Salt-free production of γ-aminobutyric acid from glutamate using glutamate decarboxylase separated from Escherichia coli. Journal of Chemical Technology and Biotechnology (Oxford, Oxfordshire), 2014, 89(9): 1432–1436 https://doi.org/10.1002/jctb.4251
47	Park H, Ahn J, Lee J, Lee H, Kim C, Jung J K, Lee H, Lee E G. Expression, immobilization and enzymatic properties of glutamate decarboxylase fused to a cellulose-binding domain. International Journal of Molecular Sciences, 2012, 13(1): 358–368
48	Hossain G S, Li J, Shin H D, Chen R R, Du G, Liu L, Chen J. Bioconversion of L-glutamic acid to α-ketoglutaric acid by an immobilized whole-cell biocatalyst expressing L-amino acid deaminase from Proteus mirabilis. Journal of Biotechnology, 2014, 169(1): 112–120 https://doi.org/10.1016/j.jbiotec.2013.10.026
49	Ödman P, Wellborn W B, Bommarius A S. An enzymatic process to α-ketoglutarate from L-glutamate: The coupled system L-glutamate dehydrogenase/NADH oxidase. Tetrahedron, Asymmetry, 2004, 15(18): 2933–2937 https://doi.org/10.1016/j.tetasy.2004.07.055
50	Pukin A V, Boeriu C G, Scott E L, Sanders J P M, Franssen M C R. An efficient enzymatic synthesis of 5-aminovaleric acid. Journal of Molecular Catalysis. B, Enzymatic, 2010, 65(1-4): 58–62 https://doi.org/10.1016/j.molcatb.2009.12.006
51	Liu P, Zhang H, Lv M, Hu M, Li Z, Gao C, Xu P, Ma C. Enzymatic production of 5-aminovalerate from L-lysine using L-lysine monooxygenase and 5-aminovaleramide amidohydrolase. Scientific Reports, 2014, 4: 5657
52	Nishi K, Endo S, Mori Y, Totsuka K, Hirao Y. US Patent, 0003497, 2005-<month>01</month>-<day>06</day>
53	Ben-Bassat A, Huang L L, Lowe D J, Patnaik R, Sariaslani F S. US Patent, 8003356, 2011-<month>08</month>-<day>23</day>
54	Xue Z, McCluskey M, Cantera K, Ben-Bassat A, Sariaslani F S, Huang L. Improved production of p-hydroxycinnamic acid from tyrosine using a novel thermostable phenylalanine/tyrosine ammonia lyase enzyme. Enzyme and Microbial Technology, 2007, 42(1): 58–64 https://doi.org/10.1016/j.enzmictec.2007.07.025
55	Nakamura N, Fujita M, Kimura K. Purification and properties of Larginase from Bacillus subtilis. Agricultural and Biological Chemistry, 1973, 37(12): 2827–2833 https://doi.org/10.1271/bbb1961.37.2827
56	Könst P M, Franssen M C R, Scott E L, Sanders J P M. A study on the applicability of L-aspartate α-decarboxylase in the biobased production of nitrogen containing chemicals. Green Chemistry, 2009, 11(10): 1646–1652 https://doi.org/10.1039/b902731a
57	Williamson J M, Brown G M. Purification and properties of L-aspartate-α-decarboxylase, an enzyme that catalyzes the formation of β-alanine in Escherichia coli. Journal of Biological Chemistry, 1979, 254(16): 8074–8082
58	Shen Y, Zhao L, Li Y, Zhang L, Shi G. Synthesis of β-alanine from L-aspartate using L-aspartate-α-decarboxylase from Corynebacterium glutamicum. Biotechnology Letters, 2014, 36(8): 1681–1686 https://doi.org/10.1007/s10529-014-1527-0
59	Zisapel N. Drugs for insomnia. Expert Opinion on Emerging Drugs, 2012, 17(3): 299–317 https://doi.org/10.1517/14728214.2012.690735
60	Le Nôtre J, Scott E L, Franssen M C R, Sanders J P M. Biobased synthesis of acrylonitrile from glutamic acid. Green Chemistry, 2011, 13(4): 807–809 https://doi.org/10.1039/c0gc00805b
61	Lammens T M, Franssen M C R, Scott E L, Sanders J P M. Synthesis of biobased N-methylpyrrolidone by one-pot cyclization and methylation of γ-aminobutyric acid. Green Chemistry, 2010, 12(8): 1430–1436 https://doi.org/10.1039/c0gc00061b
62	Bhattacharya R, Vijayaraghavan R. Promising role of α-ketoglutarate in protecting against the lethal effects of cyanide. Human and Experimental Toxicology, 2002, 21(6): 297–303 https://doi.org/10.1191/0960327102ht255oa
63	Aussel C, Coudray-Lucas C, Lasnier E, Cynober L, Ekindjian O G. α-Ketoglutarate uptake in human fibroblasts. Cell Biology International, 1996, 20(5): 359–363 https://doi.org/10.1006/cbir.1996.0042
64	Barrett D G, Yousaf M N. Poly(triol α-ketoglutarate) as biodegradable, chemoselective, and mechanically tunable elastomers. Macromolecules, 2008, 41(17): 6347–6352 https://doi.org/10.1021/ma8009728
65	Ueno H. Enzymatic and structural aspects on glutamate decarboxylase. Journal of Molecular Catalysis. B, Enzymatic, 2000, 10(1-3): 67–79 https://doi.org/10.1016/S1381-1177(00)00114-4
66	Zweers J C, Barák I, Becher D, Driessen A J M, Hecker M, Kontinen V P, Saller M J, Vavrová L, van Dijl J M. Towards the development of Bacillus subtilis as a cell factory for membrane proteins and protein complexes. Microbial Cell Factories, 2008, 7(1): 10 https://doi.org/10.1186/1475-2859-7-10
67	Park S J, Kim E Y, Noh W, Park H M, Oh Y H, Lee S H, Song B K, Jegal J, Lee S Y. Metabolic engineering of Escherichia coli for the production of 5-aminovalerate and glutarate as C5 platform chemicals. Metabolic Engineering, 2013, 16(1): 42–47 https://doi.org/10.1016/j.ymben.2012.11.011
68	Kind S, Wittmann C. Bio-based production of the platform chemical 1,5-diaminopentane. Applied Microbiology and Biotechnology, 2011, 91(5): 1287–1296 https://doi.org/10.1007/s00253-011-3457-2
69	Kaneko T, Thi T H, Shi D J, Akashi M. Environmentally degradable, high-performance thermoplastics from phenolic phytomonomers. Nature Materials, 2006, 5(12): 966–970 https://doi.org/10.1038/nmat1778
70	Sariaslani F S. Development of a combined biological and chemical process for production of industrial aromatics from renewable resources. Annual Review of Microbiology, 2007, 61(1): 51–69 https://doi.org/10.1146/annurev.micro.61.080706.093248
71	Könst P M, Franssen M C R, Scott E L, Sanders J P M. Stabilization and immobilization of Trypanosoma brucei ornithine decarboxylase for the biobased production of 1,4-diaminobutane. Green Chemistry, 2011, 13(5): 1167–1174 https://doi.org/10.1039/c0gc00564a
72	Mateo C, Palomo J M, Fernandez-Lorente G, Guisan J M, Fernandez-Lafuente R. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme and Microbial Technology, 2007, 40(6): 1451–1463 https://doi.org/10.1016/j.enzmictec.2007.01.018
73	Sheldon R A. Enzyme immobilization: The quest for optimum performance. Advanced Synthesis & Catalysis, 2007, 349(8-9): 1289–1307 https://doi.org/10.1002/adsc.200700082
74	Weetall H H, Pitcher W H Jr. Scaling up an immobilized enzyme system. Science, 1986, 232(4756): 1396–1403 https://doi.org/10.1126/science.232.4756.1396
75	Rios G M, Belleville M P, Paolucci D, Sanchez J. Progress in enzymatic membrane reactors—A review. Journal of Membrane Science, 2004, 242(1-2): 189–196 https://doi.org/10.1016/j.memsci.2003.06.004
76	Howaldt M W, Kulbe K D, Chmiel H. Choice of reactor to minimize enzyme requirement: 1. Mathematical model for one-substrate Michaelis-Menten type kinetics in continuous reactors. Enzyme and Microbial Technology, 1986, 8(10): 627–631 https://doi.org/10.1016/0141-0229(86)90124-9
77	Safdar M, Sproß J, Jänis J. Microscale immobilized enzyme reactors in proteomics: Latest developments. Journal of Chromatography. A, 2014, 1324: 1–10 https://doi.org/10.1016/j.chroma.2013.11.045
78	Zhang Z, Donaldson A A, Ma X. Advancements and future directions in enzyme technology for biomass conversion. Biotechnology Advances, 2012, 30(4): 913–919 https://doi.org/10.1016/j.biotechadv.2012.01.020
79	Teng Y, Scott E L, Sanders J P M. The selective conversion of glutamic acid in amino acid mixtures using glutamate decarboxylase—A means of separating amino acids for synthesizing biobased chemicals. Biotechnology Progress, 2014, 30(3): 681–688 https://doi.org/10.1002/btpr.1895
80	Bornscheuer U T, Huisman G W, Kazlauskas R J, Lutz S, Moore J C, Robins K. Engineering the third wave of biocatalysis. Nature, 2012, 484(7397): 185–194 https://doi.org/10.1038/nature11117
81	Agyei D, Shanbhag B K, He L. Enzyme engineering (immobilization) for food applications. In: Improving and Tailoring Enzymes for Food Quality and Functionality. Amsterdam: Elsevier, 2015, 213–235
82	Bornscheuer U T, Huisman G W, Kazlauskas R J, Lutz S, Moore J C, Robins K. Engineering the third wave of biocatalysis. Nature, 2012, 485(7397): 185–194 https://doi.org/10.1038/nature11117

[1]	Ling Tan, Kipkorir Peter, Jing Ren, Baoyang Du, Xiaojie Hao, Yufei Zhao, Yu-Fei Song. Photocatalytic syngas synthesis from CO₂ and H₂O using ultrafine CeO₂-decorated layered double hydroxide nanosheets under visible-light up to 600 nm[J]. Front. Chem. Sci. Eng., 2021, 15(1): 99-108.
[2]	Fenghua Liu, Yijian Lai, Binyuan Zhao, Robert Bradley, Weiping Wu. Photothermal materials for efficient solar powered steam generation[J]. Front. Chem. Sci. Eng., 2019, 13(4): 636-653.
[3]	J. Christopher Whitehead. Plasma-catalysis: Is it just a question of scale?[J]. Front. Chem. Sci. Eng., 2019, 13(2): 264-273.
[4]	Shewei Hu, Qian Gao, Xin Wang, Jianming Yang, Nana Xu, Kequan Chen, Sheng Xu, Pingkai Ouyang. *Efficient production of D-1,2,4-butanetriol from D-xylose by engineered Escherichia coli* whole-cell biocatalysts**[J]. Front. Chem. Sci. Eng., 2018, 12(4): 772-779.
[5]	M Helal Uddin, Nesrin Ozalp, Jens Heylen, Cedric Ophoff. A new approach for fuel injection into a solar receiver/reactor: Numerical and experimental investigation[J]. Front. Chem. Sci. Eng., 2018, 12(4): 683-696.
[6]	Alberto T. Penteado, Mijin Kim, Hamid R. Godini, Erik Esche, Jens-Uwe Repke. Techno-economic evaluation of a biogas-based oxidative coupling of methane process for ethylene production[J]. Front. Chem. Sci. Eng., 2018, 12(4): 598-618.
[7]	Jian Zhang, Liang Wang, Yanyan Ji, Fang Chen, Feng-Shou Xiao. Mesoporous zeolites for biofuel upgrading and glycerol conversion[J]. Front. Chem. Sci. Eng., 2018, 12(1): 132-144.
[8]	Hongbo Li, Bo Zheng, Zhiyong Pan, Baoning Zong, Minghua Qiao. Advances in the slurry reactor technology of the anthraquinone process for H₂O₂ production[J]. Front. Chem. Sci. Eng., 2018, 12(1): 124-131.
[9]	Tao Lu, Qilei Zhang, Shanjing Yao. Removal of dyes from wastewater by growing fungal pellets in a semi-continuous mode[J]. Front. Chem. Sci. Eng., 2017, 11(3): 338-345.
[10]	Sophie L. Pirard, Sigrid Douven, Jean-Paul Pirard. Large-scale industrial manufacturing of carbon nanotubes in a continuous inclined mobile-bed rotating reactor via the catalytic chemical vapor deposition process[J]. Front. Chem. Sci. Eng., 2017, 11(2): 280-289.
[11]	Xiaojie Zhang,Lei Wang,Shuqing Chen,Yi Huang,Zhuonan Song,Miao Yu. Facile synthesis and enhanced visible-light photocatalytic activity of Ti³⁺-doped TiO₂ sheets with tunable phase composition? ?[J]. Front. Chem. Sci. Eng., 2015, 9(3): 349-358.
[12]	Huiquan Wu, Erik Read, Maury White, Brittany Chavez, Kurt Brorson, Cyrus Agarabi, Mansoor Khan. Real time monitoring of bioreactor mAb IgG3 cell culture process dynamics via Fourier transform infrared spectroscopy: Implications for enabling cell culture process analytical technology? ?[J]. Front. Chem. Sci. Eng., 2015, 9(3): 386-406.
[13]	Anton ALVAREZ-MAJMUTOV,Jinwen CHEN. Analyzing the energy intensity and greenhouse gas emission of Canadian oil sands crude upgrading through process modeling and simulation[J]. Front. Chem. Sci. Eng., 2014, 8(2): 212-218.
[14]	A. F. D’ Intino,B. de Caprariis,M.L. Santarelli,N. Verdone,A. Chianese. Best operating conditions to produce hydroxyapatite nanoparticles by means of a spinning disc reactor[J]. Front. Chem. Sci. Eng., 2014, 8(2): 156-160.
[15]	M. S. Shalaby, H. Abdallah. Preparation of manganese (III) acetylacetonate nanoparticles via an environmentally benign route[J]. Front Chem Sci Eng, 2013, 7(3): 329-337.

Viewed

Full text

Abstract

Cited

Shared

Discussed