Biodiesel Technology and Applications. Группа авторов

Чтение книги онлайн.

СКАЧАТЬ target="_blank" rel="nofollow" href="https://doi.org/10.1016/j.bcab.2016.02.005">https://doi.org/10.1016/j.bcab.2016.02.005.

      171. M. Adamczak, W. Bednarski, Enhanced activity of intracellular lipases from Rhizomucor miehei and Yarrowia lipolytica by immobilization on biomass support particles, Process Biochem., 2004. https://doi.org/10.1016/S0032-9592(03)00266-8.

      172. L. Ping, X. Yuan, M. Zhang, Y. Chai, S. Shan, Improvement of extracellular lipase production by a newly isolated Yarrowia lipolytica mutant and its application in the biosynthesis of L-ascorbyl palmitate, Int. J. Biol. Macromol., 2018. https://doi.org/10.1016/j.ijbiomac.2017.08.016.

      173. J. Huang, J. Xia, W. Jiang, Y. Li, J. Li, Biodiesel production from microalgae oil catalyzed by a recombinant lipase, Bioresour. Technol. 180, 47–53, 2015. https://doi.org/10.1016/j.biortech.2014.12.072.

      174. D. Adachi, F. Koh, S. Hama, C. Ogino, A. Kondo, A robust whole-cell bio-catalyst that introduces a thermo- and solvent-tolerant lipase into Aspergillus oryzae cells: Characterization and application to enzymatic biodiesel production, Enzyme Microb. Technol. 52, 331–335, 2013. https://doi.org/10.1016/j.enzmictec.2013.03.005.

      175. Y. Luo, Y. Zheng, Z. Jiang, Y. Ma, D. Wei, A novel psychrophilic lipase from Pseudomonas fluorescens with unique property in chiral resolution and bio-diesel production via transesterification, Appl. Microbiol. Biotechnol. 73, 349–355, 2006. https://doi.org/10.1007/s00253-006-0478-3.

      176. J. Yan, X. Zheng, S. Li, A novel and robust recombinant Pichia pastoris yeast whole cell biocatalyst with intracellular overexpression of a Thermomyces lanuginosus lipase: Preparation, characterization and application in biodiesel production, Bioresour. Technol. 151, 43–48, 2014. https://doi.org/10.1016/j.biortech.2013.10.037.

      177. G.-C. Lee, L.-C. Lee, V. Sava, J.-F. Shaw, Multiple mutagenesis of non-universal serine codons of the Candida rugosa LIP2 gene and biochemical characterization of purified recombinant LIP2 lipase overexpressed in Pichia pastoris., Biochem. J. 366, 603–611, 2002. https://doi.org/10.1042/BJ20020404.

      178. A. Yoshida, S. Hama, N. Tamadani, H. Noda, H. Fukuda, A. Kondo, Continuous production of biodiesel using whole-cell biocatalysts: Sequential conversion of an aqueous oil emulsion into anhydrous product, Biochem. Eng. J. 68, 7–11, 2012. https://doi.org/10.1016/j.bej.2012.07.002.

      179. D. Adachi, S. Hama, T. Numata, K. Nakashima, C. Ogino, H. Fukuda, A. Kondo, Development of an Aspergillus oryzae whole-cell biocatalyst coexpressing triglyceride and partial glyceride lipases for biodiesel production, Bioresour. Technol. 102, 6723–6729, 2011. https://doi.org/10.1016/j.biortech.2011.03.066.

180. M. Raita, V. Champreda, N. Laosiripojana, Biocatalytic ethanolysis of palm oil for biodiesel production using microcrystalline lipase in tert-butanol system, Process Biochem. 45, 829–834, 2010. https://doi.org/10.1016/j.procbio.2010.02.002.

      181. T.P. Korman, B. Sahachartsiri, D.M. Charbonneau, G.L. Huang, M. Beauregard, J.U. Bowie, Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution, Biotechnol. Biofuels. 6, 70, 2013. https://doi.org/10.1186/1754-6834-6-70.

      182. S.H. Kim, S.J. Kim, S. Park, H.K. Kim, Biodiesel production using cross-linked Staphylococcus haemolyticus lipase immobilized on solid polymeric carriers, J. Mol. Catal. B Enzym. 85–86, 10–16, 2013. https://doi.org/10.1016/j.molcatb.2012.08.012.

      183. A. Li, T.P.N. Ngo, J. Yan, K. Tian, Z. Li, Whole-cell based solvent-free system for one-pot production of biodiesel from waste grease, Bioresour. Technol. 114, 725–729, 2012. https://doi.org/10.1016/j.biortech.2012.03.034.

      184. F. Guan, P. Peng, G. Wang, T. Yin, Q. Peng, J. Huang, G. Guan, Y. Li, Combination of two lipases more efficiently catalyzes methanolysis of soybean oil for biodiesel production in aqueous medium, Process Biochem. 45, 1677–1682, 2010. https://doi.org/10.1016/j.procbio.2010.06.021.

      185. T. Takaya, R. Koda, D. Adachi, K. Nakashima, J. Wada, T. Bogaki, C. Ogino, A. Kondo, Highly efficient biodiesel production by a whole-cell biocatalyst employing a system with high lipase expression in Aspergillus oryzae, Appl. Microbiol. Biotechnol. 90, 1171–1177, 2011. https://doi.org/10.1007/s00253-011-3186-6.

      186. D. Huang, S. Han, Z. Han, Y. Lin, Biodiesel production catalyzed by Rhizomucor miehei lipase-displaying Pichia pastoris whole cells in an isooctane system, Biochem. Eng. J. 63, 10–14, 2012. https://doi.org/10.1016/j.bej.2010.08.009.

      187. Z.L. Huang, T.X. Yang, J.Z. Huang, Z. Yang, Enzymatic production of bio-diesel from Millettia pinnata seed oil in ionic liquids, Bioenergy Res. 7, 1519–1528, 2014. https://doi.org/10.1007/s12155-014-9489-6.

      188. T. Matsumoto, S. Takahashi, M. Kaieda, M. Ueda, A. Tanaka, H. Fukuda, A. Kondo, Yeast whole-cell biocatalyst constructed by intracellular overproduction of Rhizopus oryzae lipase is applicable to biodiesel fuel production, Appl. Microbiol. Biotechnol. 57, 515–520, 2001. https://doi.org/10.1007/s002530100733.

      189. B. Zhang, Y. Weng, H. Xu, Z. Mao, Enzyme immobilization for biodiesel production, Appl. Microbiol. Biotechnol. 93, 61–70, 2012. https://doi.org/10.1007/s00253-011-3672-x.

      190. R. Pogaku, A. Bono, C. Chu, Developments in sustainable chemical and bioprocess technology, Springer US, Boston, MA, 2013. https://doi.org/10.1007/978-1-4614-6208-8.

      191. S.K. Narwal, R. Gupta, Biodiesel production by transesterification using immobilized lipase, Biotechnol. Lett. 35, 479–490, 2013. https://doi.org/10.1007/s10529-012-1116-z.

192. D. Brady, J. Jordaan, Advances in enzyme immobilisation, Biotechnol. Lett. 31, 1639–1650, 2009. https://doi.org/10.1007/s10529-009-0076-4.

      193. M. Kalantari, M. Kazemeini, A. Arpanaei, Evaluation of biodiesel production using lipase immobilized on magnetic silica nanocomposite particles of various structures, Biochem. Eng. J. 79, 267–273, 2013. https://doi.org/10.1016/j.bej.2013.09.001.

СКАЧАТЬ