메뉴 건너뛰기




Volumn 37, Issue 5, 2015, Pages 943-954

Recent developments in biocatalysis beyond the laboratory

Author keywords

Biocatalysis; Enzyme expression; Immobilization; Lipases; Protein engineering; Transaminases; Transglutaminase

Indexed keywords

BIOCATALYSTS; CATALYSIS; ENZYME IMMOBILIZATION; GENETIC ENGINEERING; HYDROGELS; LIPASES; PLANTS (BOTANY); RADIOACTIVE WASTE VITRIFICATION;

EID: 84934955293     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-014-1762-4     Document Type: Review
Times cited : (46)

References (73)
  • 1
    • 84876726643 scopus 로고    scopus 로고
    • A robust whole-cell biocatalyst that introduces a thermo- and solvent-tolerant lipase into Aspergillus oryzae cells: characterization and application to enzymatic biodiesel production
    • COI: 1:CAS:528:DC%2BC3sXltVGjtbo%3D
    • Adachi D, Koh F, Hama S, Ogino C, Kondo A (2013) A robust whole-cell biocatalyst that introduces a thermo- and solvent-tolerant lipase into Aspergillus oryzae cells: characterization and application to enzymatic biodiesel production. Enzym Microb Technol 52:331–335
    • (2013) Enzym Microb Technol , vol.52 , pp. 331-335
    • Adachi, D.1    Koh, F.2    Hama, S.3    Ogino, C.4    Kondo, A.5
  • 3
    • 84861657293 scopus 로고    scopus 로고
    • Increased thermostability of microbial transglutaminase by combination of several hot spots evolved by random and saturation mutagenesis
    • COI: 1:CAS:528:DC%2BC38Xhtl2jsLw%3D, PID: 21863232
    • Buettner K, Hertel TC, Pietzsch M (2012) Increased thermostability of microbial transglutaminase by combination of several hot spots evolved by random and saturation mutagenesis. Amino Acids 42:987–996
    • (2012) Amino Acids , vol.42 , pp. 987-996
    • Buettner, K.1    Hertel, T.C.2    Pietzsch, M.3
  • 4
    • 84883391049 scopus 로고    scopus 로고
    • Development of a novel integrated continuous reactor system for biocatalytic production of biodiesel
    • COI: 1:CAS:528:DC%2BC3sXhsFWmt7jF, PID: 24001564
    • Chattopadhyay S, Sen R (2013) Development of a novel integrated continuous reactor system for biocatalytic production of biodiesel. Bioresour Technol 147:395–400
    • (2013) Bioresour Technol , vol.147 , pp. 395-400
    • Chattopadhyay, S.1    Sen, R.2
  • 5
    • 84893516499 scopus 로고    scopus 로고
    • Enzymatic biodiesel: challenges and opportunities
    • COI: 1:CAS:528:DC%2BC2cXivF2nt7w%3D
    • Christopher LP, Kumar H, Zambare VP (2014) Enzymatic biodiesel: challenges and opportunities. Appl Energy 119:497–520
    • (2014) Appl Energy , vol.119 , pp. 497-520
    • Christopher, L.P.1    Kumar, H.2    Zambare, V.P.3
  • 6
    • 79955612452 scopus 로고    scopus 로고
    • Expanded functionality of modified whey protein dispersions after transglutaminase catalysis
    • COI: 1:CAS:528:DC%2BC3MXmslOhsrw%3D, PID: 22417338
    • Clare DA, Daubert CR (2011) Expanded functionality of modified whey protein dispersions after transglutaminase catalysis. J Food Sci 76:C576–C584
    • (2011) J Food Sci , vol.76 , pp. 576-584
    • Clare, D.A.1    Daubert, C.R.2
  • 8
    • 84893370513 scopus 로고    scopus 로고
    • Microbial transglutaminase: general characteristics and performance in food processing technology
    • de Goes-Favoni S, Bueno FR (2014) Microbial transglutaminase: general characteristics and performance in food processing technology. Food Biotechnol 28:1–24
    • (2014) Food Biotechnol , vol.28 , pp. 1-24
    • de Goes-Favoni, S.1    Bueno, F.R.2
  • 9
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: impact on food applications
    • De Jong GAH, Koppelman SJ (2002) Transglutaminase catalyzed reactions: impact on food applications. J Food Sci 67:2798–2806
    • (2002) J Food Sci , vol.67 , pp. 2798-2806
    • De Jong, G.A.H.1    Koppelman, S.J.2
  • 10
    • 84877725469 scopus 로고    scopus 로고
    • Effect of transglutaminase on the mechanical and barrier properties of whey protein/pectin films prepared at complexation pH
    • Di Pierro P, Rossi Marquez G, Mariniello L, Sorrentino A, Villalonga R, Porta R (2013) Effect of transglutaminase on the mechanical and barrier properties of whey protein/pectin films prepared at complexation pH. J Agr Food Chem 61:4593–4598
    • (2013) J Agr Food Chem , vol.61 , pp. 4593-4598
    • Di Pierro, P.1    Rossi Marquez, G.2    Mariniello, L.3    Sorrentino, A.4    Villalonga, R.5    Porta, R.6
  • 11
    • 84856726076 scopus 로고    scopus 로고
    • The importance of green chemistry in process research and development
    • COI: 1:CAS:528:DC%2BC38XhsVajsb0%3D, PID: 21562677
    • Dunn PJ (2012) The importance of green chemistry in process research and development. Chem Soc Rev 41(4):1452–1461
    • (2012) Chem Soc Rev , vol.41 , Issue.4 , pp. 1452-1461
    • Dunn, P.J.1
  • 12
    • 84859835231 scopus 로고    scopus 로고
    • Functionalizing maize zein in viscoelastic dough systems through fibrous, beta-sheet-rich protein networks: an alternative, physicochemical approach to gluten-free breadmaking
    • COI: 1:CAS:528:DC%2BC38XlvVSntr8%3D
    • Erickson DP, Campanella OH, Hamaker BR (2012) Functionalizing maize zein in viscoelastic dough systems through fibrous, beta-sheet-rich protein networks: an alternative, physicochemical approach to gluten-free breadmaking. Trends Food Sci Technol 24:74–81
    • (2012) Trends Food Sci Technol , vol.24 , pp. 74-81
    • Erickson, D.P.1    Campanella, O.H.2    Hamaker, B.R.3
  • 14
    • 0034853832 scopus 로고    scopus 로고
    • Effects of microbial transglutaminase on the wheat proteins of bread and croissant dough
    • COI: 1:CAS:528:DC%2BD3MXmvV2gsbs%3D
    • Gerrard JA, Fayle SE, Brown PA, Sutton KH, Simmons L, Rasiah I (2001) Effects of microbial transglutaminase on the wheat proteins of bread and croissant dough. J Food Sci 66:782–786
    • (2001) J Food Sci , vol.66 , pp. 782-786
    • Gerrard, J.A.1    Fayle, S.E.2    Brown, P.A.3    Sutton, K.H.4    Simmons, L.5    Rasiah, I.6
  • 17
    • 80053257479 scopus 로고    scopus 로고
    • Biodiesel production using enzymatic transesterification—current state and perspectives
    • COI: 1:CAS:528:DC%2BC3MXht1GrurrF
    • Gog A, Roman M, Tos M, Paizs C, Irimie FD (2012) Biodiesel production using enzymatic transesterification—current state and perspectives. Renew Energy 39:10–16
    • (2012) Renew Energy , vol.39 , pp. 10-16
    • Gog, A.1    Roman, M.2    Tos, M.3    Paizs, C.4    Irimie, F.D.5
  • 18
    • 84915733006 scopus 로고    scopus 로고
    • Chiral amine synthesis using omega-transaminases: an amine donor that displaces equilibria and enables high-throughput screening
    • COI: 1:CAS:528:DC%2BC2cXhtlylsrjP, PID: 25138082
    • Green AP, Turner NJ, O’Reilly E (2014) Chiral amine synthesis using omega-transaminases: an amine donor that displaces equilibria and enables high-throughput screening. Angew Chem Int Ed Engl 53:10714–10717
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 10714-10717
    • Green, A.P.1    Turner, N.J.2    O’Reilly, E.3
  • 19
    • 84876718337 scopus 로고    scopus 로고
    • Enzymatic biodiesel production: an overview of potential feedstocks and process development
    • COI: 1:CAS:528:DC%2BC3sXmt1WhtLw%3D, PID: 22985827
    • Hama S, Kondo A (2013) Enzymatic biodiesel production: an overview of potential feedstocks and process development. Bioresour Technol 135:386–395
    • (2013) Bioresour Technol , vol.135 , pp. 386-395
    • Hama, S.1    Kondo, A.2
  • 20
    • 84872621014 scopus 로고    scopus 로고
    • The effects of vital wheat gluten and transglutaminase on the thermomechanical and dynamic rheological properties of buckwheat dough
    • COI: 1:CAS:528:DC%2BC3sXhtFWrsL4%3D
    • Han LH, Cheng YQ, Qiu S, Tatsumi E, Shen Q, Lu ZH, Li LT (2013) The effects of vital wheat gluten and transglutaminase on the thermomechanical and dynamic rheological properties of buckwheat dough. Food Bioprocess Technol 6:561–569
    • (2013) Food Bioprocess Technol , vol.6 , pp. 561-569
    • Han, L.H.1    Cheng, Y.Q.2    Qiu, S.3    Tatsumi, E.4    Shen, Q.5    Lu, Z.H.6    Li, L.T.7
  • 21
    • 84905002264 scopus 로고    scopus 로고
    • Transamidation of gluten proteins during the bread-making process of wheat flour to produce breads with less immunoreactive gluten
    • COI: 1:CAS:528:DC%2BC2cXht1Wlu7bL, PID: 24917417
    • Heredia-Sandoval NG, Islas-Rubio AR, Cabrera-Chavez F, De la Barca AMC (2014) Transamidation of gluten proteins during the bread-making process of wheat flour to produce breads with less immunoreactive gluten. Food Funct 5:1813–1818
    • (2014) Food Funct , vol.5 , pp. 1813-1818
    • Heredia-Sandoval, N.G.1    Islas-Rubio, A.R.2    Cabrera-Chavez, F.3    De la Barca, A.M.C.4
  • 22
    • 85052409885 scopus 로고    scopus 로고
    • Biofuels and World Agricultural Markets: outlook for 2020 and 2050. In: Bernardes MADS (ed) Economic effects of biofuel production. doi: 10.5772/20581 InTech
    • Hervé G, Agneta F, Yves D (2011) Biofuels and World Agricultural Markets: outlook for 2020 and 2050. In: Bernardes MADS (ed) Economic effects of biofuel production. doi: 10.5772/20581 InTech, Rijeka
    • (2011) Rijeka
    • Hervé, G.1    Agneta, F.2    Yves, D.3
  • 23
    • 84906501330 scopus 로고    scopus 로고
    • Improved production of a recombinant Rhizomucor miehei lipase expressed in Pichia pastoris and its application for conversion of microalgae oil to biodiesel
    • PID: 25788976
    • Huang J, Xia J, Yang Z, Guan F, Cui D, Guan G, Jiang W, Li Y (2014) Improved production of a recombinant Rhizomucor miehei lipase expressed in Pichia pastoris and its application for conversion of microalgae oil to biodiesel. Biotechnol Biofuels 7:111
    • (2014) Biotechnol Biofuels , vol.7 , pp. 111
    • Huang, J.1    Xia, J.2    Yang, Z.3    Guan, F.4    Cui, D.5    Guan, G.6    Jiang, W.7    Li, Y.8
  • 24
    • 84876710917 scopus 로고    scopus 로고
    • On the development of new biocatalytic processes for practical pharmaceutical synthesis
    • COI: 1:CAS:528:DC%2BC3sXivFyqtbg%3D, PID: 23462589
    • Huisman GW, Collier SJ (2013) On the development of new biocatalytic processes for practical pharmaceutical synthesis. Curr Opin Chem Biol 17:284–292
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 284-292
    • Huisman, G.W.1    Collier, S.J.2
  • 25
    • 1642351056 scopus 로고    scopus 로고
    • High-throughput screening method for the identification of active and enantioselective omega-transaminases
    • COI: 1:CAS:528:DC%2BD2cXisVenurk%3D
    • Hwang BY, Kim BG (2004) High-throughput screening method for the identification of active and enantioselective omega-transaminases. Enzyme Micro Technol 34:429–436
    • (2004) Enzyme Micro Technol , vol.34 , pp. 429-436
    • Hwang, B.Y.1    Kim, B.G.2
  • 26
    • 84894281258 scopus 로고    scopus 로고
    • Lipase catalyzed process for biodiesel production: protein engineering and lipase production
    • COI: 1:CAS:528:DC%2BC3sXhvFCjtrjN, PID: 24284881
    • Hwang YT, Qi F, Yuan C, Zhao X, Ramkrishna D, Liu D, Varma A (2014) Lipase catalyzed process for biodiesel production: protein engineering and lipase production. Biotechnol Bioeng 111:639–653
    • (2014) Biotechnol Bioeng , vol.111 , pp. 639-653
    • Hwang, Y.T.1    Qi, F.2    Yuan, C.3    Zhao, X.4    Ramkrishna, D.5    Liu, D.6    Varma, A.7
  • 27
    • 84861458491 scopus 로고    scopus 로고
    • Recent trends in biocatalysis engineering
    • COI: 1:CAS:528:DC%2BC38XnvVOrtrc%3D, PID: 22424920
    • Illanes A, Cauerhff A, Wilson L, Castro GR (2012) Recent trends in biocatalysis engineering. Bioresour Technol 115:48–57
    • (2012) Bioresour Technol , vol.115 , pp. 48-57
    • Illanes, A.1    Cauerhff, A.2    Wilson, L.3    Castro, G.R.4
  • 28
    • 0030139455 scopus 로고    scopus 로고
    • Application of enzymes in food processing
    • COI: 1:CAS:528:DyaK28XjvFyisrw%3D, PID: 8725673
    • James J, Simpson BK (1996) Application of enzymes in food processing. Crit Rev Food Sci Nutr 36:437–463
    • (1996) Crit Rev Food Sci Nutr , vol.36 , pp. 437-463
    • James, J.1    Simpson, B.K.2
  • 29
    • 84873303091 scopus 로고    scopus 로고
    • Environmental assessment of enzyme use in industrial production: a literature review
    • COI: 1:CAS:528:DC%2BC3sXktFanurg%3D
    • Jegannathan KR, Nielsen PH (2013) Environmental assessment of enzyme use in industrial production: a literature review. J Cleaner Prod 42:228–240
    • (2013) J Cleaner Prod , vol.42 , pp. 228-240
    • Jegannathan, K.R.1    Nielsen, P.H.2
  • 30
    • 84872150185 scopus 로고    scopus 로고
    • Combined utilization of lipase displaying Pichia pastoris whole-cell biocatalysts to improve biodiesel production in co solvent media
    • COI: 1:CAS:528:DC%2BC3sXislWjtrk%3D, PID: 23306117
    • Jin Z, Han SY, Zhang L, Zheng SP, Wang Y, Lin Y (2013) Combined utilization of lipase displaying Pichia pastoris whole-cell biocatalysts to improve biodiesel production in co solvent media. Bioresour Technol 130:102–109
    • (2013) Bioresour Technol , vol.130 , pp. 102-109
    • Jin, Z.1    Han, S.Y.2    Zhang, L.3    Zheng, S.P.4    Wang, Y.5    Lin, Y.6
  • 31
    • 0027223075 scopus 로고
    • Primary structure of microbial transglutaminase from Streptoverticillium sp. strain S-8112
    • COI: 1:CAS:528:DyaK3sXlsFCktbk%3D, PID: 8099353
    • Kanaji T, Ozaki H, Takano T, Ide H, Motoki M, Shimonishi Y (1993) Primary structure of microbial transglutaminase from Streptoverticillium sp. strain S-8112. J Biol Chem 268:11565–11572
    • (1993) J Biol Chem , vol.268 , pp. 11565-11572
    • Kanaji, T.1    Ozaki, H.2    Takano, T.3    Ide, H.4    Motoki, M.5    Shimonishi, Y.6
  • 32
    • 85027927818 scopus 로고    scopus 로고
    • Microbial transglutaminase and its application in the food industry: a review
    • COI: 1:CAS:528:DC%2BC3sXhslelt7bK
    • Kieliszek M, Misiewicz A (2014) Microbial transglutaminase and its application in the food industry: a review. Folia Microbiol 59:241–250
    • (2014) Folia Microbiol , vol.59 , pp. 241-250
    • Kieliszek, M.1    Misiewicz, A.2
  • 33
    • 84897932244 scopus 로고    scopus 로고
    • Recent achievements in developing the biocatalytic toolbox for chiral amine synthesis
    • COI: 1:CAS:528:DC%2BC2cXntFymtbY%3D, PID: 24721252
    • Kohls H, Steffen-Munsberg F, Hohne M (2014) Recent achievements in developing the biocatalytic toolbox for chiral amine synthesis. Curr Opin Chem Biol 19:180–192
    • (2014) Curr Opin Chem Biol , vol.19 , pp. 180-192
    • Kohls, H.1    Steffen-Munsberg, F.2    Hohne, M.3
  • 34
    • 84877077217 scopus 로고    scopus 로고
    • Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution
    • COI: 1:CAS:528:DC%2BC3sXpsFeltLg%3D, PID: 23648063
    • Korman TP, Sahachartsiri B, Charbonneau DM, Huang GL, Beauregard M, Bowie JU (2013) Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution. Biotechnol Biofuels 6:70
    • (2013) Biotechnol Biofuels , vol.6 , pp. 70
    • Korman, T.P.1    Sahachartsiri, B.2    Charbonneau, D.M.3    Huang, G.L.4    Beauregard, M.5    Bowie, J.U.6
  • 36
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: its utilization in the food industry
    • COI: 1:CAS:528:DC%2BD3MXkslWisr8%3D
    • Kuraishi C, Yamazaki K, Susa Y (2001) Transglutaminase: its utilization in the food industry. Food Rev Int 17:221–246
    • (2001) Food Rev Int , vol.17 , pp. 221-246
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 37
    • 84888131404 scopus 로고    scopus 로고
    • Enzymatic biodiesel synthesis in semi-pilot continuous process in near-critical carbon dioxide
    • COI: 1:CAS:528:DC%2BC3sXhslWhsLrP, PID: 23536250
    • Lee M, Lee D, Cho J, Kim S, Park C (2013) Enzymatic biodiesel synthesis in semi-pilot continuous process in near-critical carbon dioxide. Appl Biochem Biotechnol 171:1118–1127
    • (2013) Appl Biochem Biotechnol , vol.171 , pp. 1118-1127
    • Lee, M.1    Lee, D.2    Cho, J.3    Kim, S.4    Park, C.5
  • 38
    • 79955033486 scopus 로고    scopus 로고
    • Development of soy-based cream cheese via the addition of microbial transglutaminase, soy protein isolate and maltodextrin
    • Lim TJ, Easa A-M, Karim A-A, Bhat R, Liong M-T (2011) Development of soy-based cream cheese via the addition of microbial transglutaminase, soy protein isolate and maltodextrin. Br Food J 113:1147–1172
    • (2011) Br Food J , vol.113 , pp. 1147-1172
    • Lim, T.J.1    Easa, A.-M.2    Karim, A.-A.3    Bhat, R.4    Liong, M.-T.5
  • 39
    • 84888043194 scopus 로고    scopus 로고
    • Preparation of reusable bioreactors using reversible immobilization of enzyme on monolithic porous polymer support with attached gold nanoparticles
    • COI: 1:CAS:528:DC%2BC3sXhtlSiurvI, PID: 23860941
    • Lv Y, Lin Z, Tan T, Svec F (2014) Preparation of reusable bioreactors using reversible immobilization of enzyme on monolithic porous polymer support with attached gold nanoparticles. Biotechnol Bioeng 111:50–58
    • (2014) Biotechnol Bioeng , vol.111 , pp. 50-58
    • Lv, Y.1    Lin, Z.2    Tan, T.3    Svec, F.4
  • 40
    • 84863633075 scopus 로고    scopus 로고
    • Enantioselective synthesis of a dual orexin receptor antagonist
    • COI: 1:CAS:528:DC%2BC38XovFaqt70%3D, PID: 22725839
    • Mangion IK, Sherry BD, Yin J, Fleitz FJ (2012) Enantioselective synthesis of a dual orexin receptor antagonist. Org Lett 14:3458–3461
    • (2012) Org Lett , vol.14 , pp. 3458-3461
    • Mangion, I.K.1    Sherry, B.D.2    Yin, J.3    Fleitz, F.J.4
  • 43
    • 84874830968 scopus 로고    scopus 로고
    • High throughput screening methods for ω-transaminases
    • COI: 1:CAS:528:DC%2BC3sXjslejt7g%3D
    • Mathew S, Shin G, Shon M, Yun H (2013) High throughput screening methods for ω-transaminases. Biotech Bioprocess Eng 18:1–7
    • (2013) Biotech Bioprocess Eng , vol.18 , pp. 1-7
    • Mathew, S.1    Shin, G.2    Shon, M.3    Yun, H.4
  • 46
    • 79953305092 scopus 로고    scopus 로고
    • Recent progress in industrial biocatalysis
    • COI: 1:CAS:528:DC%2BC3MXksFKnt74%3D, PID: 21195018
    • Nestl BM, Nebel BA, Hauer B (2011) Recent progress in industrial biocatalysis. Curr Opin Chem Biol 15:187–193
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 187-193
    • Nestl, B.M.1    Nebel, B.A.2    Hauer, B.3
  • 47
    • 84896353052 scopus 로고    scopus 로고
    • New generation of biocatalysts for organic synthesis
    • COI: 1:CAS:528:DC%2BC2cXisVantbk%3D, PID: 24520044
    • Nestl BM, Hammer SC, Nebel BA, Hauer B (2014) New generation of biocatalysts for organic synthesis. Angew Chem Int Ed Engl 53:3070–3095
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 3070-3095
    • Nestl, B.M.1    Hammer, S.C.2    Nebel, B.A.3    Hauer, B.4
  • 48
    • 84883447335 scopus 로고    scopus 로고
    • Efficient transformation of grease to biodiesel using highly active and easily recyclable magnetic nanobiocatalyst aggregates
    • COI: 1:CAS:528:DC%2BC3sXltVWnsA%3D%3D, PID: 23298767
    • Ngo TPN, Li A, Tiew KW, Li Z (2013) Efficient transformation of grease to biodiesel using highly active and easily recyclable magnetic nanobiocatalyst aggregates. Bioresour Technol 145:233–239
    • (2013) Bioresour Technol , vol.145 , pp. 233-239
    • Ngo, T.P.N.1    Li, A.2    Tiew, K.W.3    Li, Z.4
  • 49
    • 84868296111 scopus 로고    scopus 로고
    • In search of a tolerance-induction strategy for cow’s milk allergies: significant reduction of beta-lactoglobulin allergenicity via transglutaminase/cysteine polymerization
    • PID: 23070344
    • Olivier CE, Lima RP, Pinto DG, Santos RA, Silva GK, Lorena SL, Villas-Boas MB, Netto FM, Zollner Rde L (2012) In search of a tolerance-induction strategy for cow’s milk allergies: significant reduction of beta-lactoglobulin allergenicity via transglutaminase/cysteine polymerization. Clinics 67:1171–1179
    • (2012) Clinics , vol.67 , pp. 1171-1179
    • Olivier, C.E.1    Lima, R.P.2    Pinto, D.G.3    Santos, R.A.4    Silva, G.K.5    Lorena, S.L.6    Villas-Boas, M.B.7    Netto, F.M.8    Zollner Rde, L.9
  • 50
    • 84873080431 scopus 로고    scopus 로고
    • Improved thermostability of lipase B from Candida antarctica by directed evolution and display on yeast surface
    • COI: 1:CAS:528:DC%2BC3sXhsVKqtr8%3D, PID: 23188656
    • Peng X (2013) Improved thermostability of lipase B from Candida antarctica by directed evolution and display on yeast surface. Appl Biochem Biotechnol 169:351–358
    • (2013) Appl Biochem Biotechnol , vol.169 , pp. 351-358
    • Peng, X.1
  • 51
    • 84901038191 scopus 로고    scopus 로고
    • Biotechnological applications of transglutaminases
    • PID: 24970194
    • Rachel NM, Pelletier JN (2013) Biotechnological applications of transglutaminases. Biomolecules 3:870–888
    • (2013) Biomolecules , vol.3 , pp. 870-888
    • Rachel, N.M.1    Pelletier, J.N.2
  • 52
    • 85012855636 scopus 로고    scopus 로고
    • Food-grade enzymes
    • Moo-Young M, Butler M, Webb BC, (eds), Academic Press, Burlington:
    • Ramos OS, Malcata FX (2011) Food-grade enzymes. In: Moo-Young M, Butler M, Webb BC et al (eds) Comprehensive Biotechnology. Academic Press, Burlington
    • (2011) Comprehensive Biotechnology
    • Ramos, O.S.1    Malcata, F.X.2
  • 53
    • 81855164780 scopus 로고    scopus 로고
    • Transglutaminase treatment of brown rice flour: a chromatographic, electrophoretic and spectroscopic study of protein modifications
    • COI: 1:CAS:528:DC%2BC3MXhsVyksbfF
    • Renzetti S, Behr J, Vogel RF, Barbiroli A, Iametti S, Bonomi F, Arendt EK (2012) Transglutaminase treatment of brown rice flour: a chromatographic, electrophoretic and spectroscopic study of protein modifications. Food Chem 131:1076–1085
    • (2012) Food Chem , vol.131 , pp. 1076-1085
    • Renzetti, S.1    Behr, J.2    Vogel, R.F.3    Barbiroli, A.4    Iametti, S.5    Bonomi, F.6    Arendt, E.K.7
  • 54
    • 3142603469 scopus 로고    scopus 로고
    • Chiral chemistry: traditional methods thrive despite numerous hurdles, including tough luck, slow commercialization of catalytic processes
    • Rouhi AM (2004) Chiral chemistry: traditional methods thrive despite numerous hurdles, including tough luck, slow commercialization of catalytic processes. Chem Eng News 82:47–62
    • (2004) Chem Eng News , vol.82 , pp. 47-62
    • Rouhi, A.M.1
  • 55
    • 84857581433 scopus 로고    scopus 로고
    • Transaminases for the synthesis of enantiopure beta-amino acids
    • PID: 22293122
    • Rudat J, Brucher BR, Syldatk C (2012) Transaminases for the synthesis of enantiopure beta-amino acids. AMB Express 2:11
    • (2012) AMB Express , vol.2 , pp. 11
    • Rudat, J.1    Brucher, B.R.2    Syldatk, C.3
  • 57
    • 84871098691 scopus 로고    scopus 로고
    • Optimisation of bread quality produced from wheat and proso millet (Panicum miliaceum L.) by adding emulsifiers, transglutaminase and xylanase
    • COI: 1:CAS:528:DC%2BC38XhvVCrs7vO
    • Schoenlechner R, Szatmari M, Bagdi A, Tomoskozi S (2013) Optimisation of bread quality produced from wheat and proso millet (Panicum miliaceum L.) by adding emulsifiers, transglutaminase and xylanase. Lwt-Food Sci Technol 51:361–366
    • (2013) Lwt-Food Sci Technol , vol.51 , pp. 361-366
    • Schoenlechner, R.1    Szatmari, M.2    Bagdi, A.3    Tomoskozi, S.4
  • 58
    • 78650209065 scopus 로고    scopus 로고
    • Necessary and sufficient conditions for the asymmetric synthesis of chiral amines using omega-aminotransferases
    • COI: 1:CAS:528:DC%2BC3cXhsFOjsb7M, PID: 20824676
    • Seo JH, Kyung D, Joo K, Lee J, Kim BG (2011) Necessary and sufficient conditions for the asymmetric synthesis of chiral amines using omega-aminotransferases. Biotechnol Bioeng 108:253–263
    • (2011) Biotechnol Bioeng , vol.108 , pp. 253-263
    • Seo, J.H.1    Kyung, D.2    Joo, K.3    Lee, J.4    Kim, B.G.5
  • 59
    • 84875701703 scopus 로고    scopus 로고
    • Biocatalytic synthesis of enantiopure building blocks for pharmaceuticals
    • PID: 24050228
    • Simon RC, Mutti FG, Kroutil W (2013) Biocatalytic synthesis of enantiopure building blocks for pharmaceuticals. Drug Discov Today Technol 10:e37–e44
    • (2013) Drug Discov Today Technol , vol.10 , pp. e37-e44
    • Simon, R.C.1    Mutti, F.G.2    Kroutil, W.3
  • 60
    • 84870764794 scopus 로고    scopus 로고
    • Improvement of gluten-free bread quality using transglutaminase, various extruded flours and protein isolates
    • COI: 1:CAS:528:DC%2BC3sXitFalur0%3D
    • Smerdel B, Pollak L, Novotni D, Cukelj N, Benkovic M, Lusic D, Curic D (2012) Improvement of gluten-free bread quality using transglutaminase, various extruded flours and protein isolates. J Food Nut Res 51:242–253
    • (2012) J Food Nut Res , vol.51 , pp. 242-253
    • Smerdel, B.1    Pollak, L.2    Novotni, D.3    Cukelj, N.4    Benkovic, M.5    Lusic, D.6    Curic, D.7
  • 61
    • 84901929607 scopus 로고    scopus 로고
    • Analysis of the effect of heating on rheological attributes of washed mechanically recovered chicken meat modified with transglutaminase
    • COI: 1:CAS:528:DC%2BC2cXhtFWisrnE
    • Stangierski J, Rezler R, Lesnierowski G (2014) Analysis of the effect of heating on rheological attributes of washed mechanically recovered chicken meat modified with transglutaminase. J Food Eng 141:13–19
    • (2014) J Food Eng , vol.141 , pp. 13-19
    • Stangierski, J.1    Rezler, R.2    Lesnierowski, G.3
  • 62
    • 79957694192 scopus 로고    scopus 로고
    • Reversed enantiopreference of an omega-transaminase by a single-point mutation
    • COI: 1:CAS:528:DC%2BC3cXpslCgtbc%3D
    • Svedendahl M, Branneby C, Lindberg L, Berglund P (2010) Reversed enantiopreference of an omega-transaminase by a single-point mutation. Chemcatchem 2:976–980
    • (2010) Chemcatchem , vol.2 , pp. 976-980
    • Svedendahl, M.1    Branneby, C.2    Lindberg, L.3    Berglund, P.4
  • 63
    • 77149171446 scopus 로고    scopus 로고
    • Efficient production of enantiomerically pure chiral amines at concentrations of 50 g/L using transaminases
    • COI: 1:CAS:528:DC%2BD1MXhs1SrurrO
    • Truppo MD, Rozzell JD, Turner NJ (2010) Efficient production of enantiomerically pure chiral amines at concentrations of 50 g/L using transaminases. Org Process Res Dev 14:234–237
    • (2010) Org Process Res Dev , vol.14 , pp. 234-237
    • Truppo, M.D.1    Rozzell, J.D.2    Turner, N.J.3
  • 64
    • 84864357731 scopus 로고    scopus 로고
    • Development of an immobilized transaminase capable of operating in organic solvent
    • COI: 1:CAS:528:DC%2BC38Xos1ejtr4%3D
    • Truppo MD, Strotman H, Hughes G (2012) Development of an immobilized transaminase capable of operating in organic solvent. ChemCatChem 4:1071–1074
    • (2012) ChemCatChem , vol.4 , pp. 1071-1074
    • Truppo, M.D.1    Strotman, H.2    Hughes, G.3
  • 65
    • 79956112929 scopus 로고    scopus 로고
    • Process considerations for the asymmetric synthesis of chiral amines using transaminases
    • COI: 1:CAS:528:DC%2BC3MXmtFyls7s%3D, PID: 21455931
    • Tufvesson P, Lima-Ramos J, Jensen JS, Al-Haque N, Neto W, Woodley JM (2011) Process considerations for the asymmetric synthesis of chiral amines using transaminases. Biotechnol Bioeng 108:1479–1493
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1479-1493
    • Tufvesson, P.1    Lima-Ramos, J.2    Jensen, J.S.3    Al-Haque, N.4    Neto, W.5    Woodley, J.M.6
  • 66
    • 84876726128 scopus 로고    scopus 로고
    • Protein engineering of enzymes for process applications
    • COI: 1:CAS:528:DC%2BC3sXlsFerurc%3D, PID: 23562542
    • Woodley JM (2013) Protein engineering of enzymes for process applications. Curr Opin Chem Biol 17:310–316
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 310-316
    • Woodley, J.M.1
  • 67
    • 84896306148 scopus 로고    scopus 로고
    • Enhanced enzyme kinetic stability by increasing rigidity within the active site
    • COI: 1:CAS:528:DC%2BC2cXktlWru7Y%3D, PID: 24448805
    • Xie Y, An J, Yang G, Wu G, Zhan Y, Cui L, Feng Y (2014) Enhanced enzyme kinetic stability by increasing rigidity within the active site. J Biol Chem 289:7994–8006
    • (2014) J Biol Chem , vol.289 , pp. 7994-8006
    • Xie, Y.1    An, J.2    Yang, G.3    Wu, G.4    Zhan, Y.5    Cui, L.6    Feng, Y.7
  • 68
    • 84899479578 scopus 로고    scopus 로고
    • Integrated lipase production and in situ biodiesel synthesis in a recombinant Pichia pastoris yeast: an efficient dual biocatalytic system composed of cell free enzymes and whole cell catalysts
    • PID: 24713071
    • Yan J, Zheng X, Du L, Li S (2014) Integrated lipase production and in situ biodiesel synthesis in a recombinant Pichia pastoris yeast: an efficient dual biocatalytic system composed of cell free enzymes and whole cell catalysts. Biotechnol Biofuels 7:55
    • (2014) Biotechnol Biofuels , vol.7 , pp. 55
    • Yan, J.1    Zheng, X.2    Du, L.3    Li, S.4
  • 69
    • 79954994752 scopus 로고    scopus 로고
    • Development of a probiotic delivery system from agrowastes, soy protein isolate, and microbial transglutaminase
    • COI: 1:CAS:528:DC%2BC3MXlt1Sit7o%3D, PID: 21535834
    • Yew SE, Lim TJ, Lew LC, Bhat R, Mat-Easa A, Liong MT (2011) Development of a probiotic delivery system from agrowastes, soy protein isolate, and microbial transglutaminase. J Food Sci 76:H108–H115
    • (2011) J Food Sci , vol.76 , pp. 108-115
    • Yew, S.E.1    Lim, T.J.2    Lew, L.C.3    Bhat, R.4    Mat-Easa, A.5    Liong, M.T.6
  • 70
    • 77955559551 scopus 로고    scopus 로고
    • Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis
    • COI: 1:CAS:528:DC%2BC3cXptlWqsbo%3D, PID: 20521043
    • Yokoyama K, Utsumi H, Nakamura T, Ogaya D, Shimba N, Suzuki E, Taguchi S (2010) Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis. Appl Microbiol Biotechnol 87:2087–2096
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 2087-2096
    • Yokoyama, K.1    Utsumi, H.2    Nakamura, T.3    Ogaya, D.4    Shimba, N.5    Suzuki, E.6    Taguchi, S.7
  • 71
    • 84867028197 scopus 로고    scopus 로고
    • Engineering a disulfide bond in the lid hinge region of Rhizopus chinensis lipase: increased thermostability and altered acyl chain length specificity
    • COI: 1:CAS:528:DC%2BC38XhsFWgsL3I, PID: 23056295
    • Yu XW, Tan NJ, Xiao R, Xu Y (2012a) Engineering a disulfide bond in the lid hinge region of Rhizopus chinensis lipase: increased thermostability and altered acyl chain length specificity. Plos one 7:e46388
    • (2012) Plos one , vol.7
    • Yu, X.W.1    Tan, N.J.2    Xiao, R.3    Xu, Y.4
  • 72
    • 84864518283 scopus 로고    scopus 로고
    • Enhanced thermostability of a Rhizopus chinensis lipase by in vivo recombination in Pichia pastoris
    • Yu XW, Wang R, Zhang M, Xu Y, Xiao R (2012b) Enhanced thermostability of a Rhizopus chinensis lipase by in vivo recombination in Pichia pastoris. Microb Cell Fact 11:1–11
    • (2012) Microb Cell Fact , vol.11 , pp. 1-11
    • Yu, X.W.1    Wang, R.2    Zhang, M.3    Xu, Y.4    Xiao, R.5
  • 73
    • 77749268141 scopus 로고    scopus 로고
    • Microbial transglutaminase production: understanding the mechanism
    • COI: 1:CAS:528:DC%2BD1MXhtlSmsbvI
    • Zhang D, Zhu Y, Chen J (2009) Microbial transglutaminase production: understanding the mechanism. Biotechnol Gen Eng Rev 26:205–222
    • (2009) Biotechnol Gen Eng Rev , vol.26 , pp. 205-222
    • Zhang, D.1    Zhu, Y.2    Chen, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.