{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T05:46:19Z","timestamp":1793339179843,"version":"4.5.0"},"reference-count":43,"publisher":"Springer Science and Business Media LLC","issue":"13","license":[{"start":{"date-parts":[[2019,4,30]],"date-time":"2019-04-30T00:00:00Z","timestamp":1556582400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2019,4,30]],"date-time":"2019-04-30T00:00:00Z","timestamp":1556582400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100009027","name":"Advanced Low Carbon Technology Research and Development Program","doi-asserted-by":"publisher","award":["JPMJAL1106"],"award-info":[{"award-number":["JPMJAL1106"]}],"id":[{"id":"10.13039\/501100009027","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Appl Microbiol Biotechnol"],"published-print":{"date-parts":[[2019,7]]},"DOI":"10.1007\/s00253-019-09848-2","type":"journal-article","created":{"date-parts":[[2019,4,30]],"date-time":"2019-04-30T15:02:38Z","timestamp":1556636558000},"page":"5355-5366","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":78,"title":["The effect of reactive oxygen species (ROS) and ROS-scavenging enzymes, superoxide dismutase and catalase, on the thermotolerant ability of Corynebacterium glutamicum"],"prefix":"10.1007","volume":"103","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5101-8030","authenticated-orcid":false,"given":"Nawarat","family":"Nantapong","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryutarou","family":"Murata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarvitr","family":"Trakulnaleamsai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naoya","family":"Kataoka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshiharu","family":"Yakushi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazunobu","family":"Matsushita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,4,30]]},"reference":[{"key":"9848_CR1","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/S0076-6879(84)05016-3","volume":"105","author":"H Abei","year":"1984","unstructured":"Abei H (1984) Catalase in vitro. Methods Enzymol 105:121\u2013126","journal-title":"Methods Enzymol"},{"key":"9848_CR2","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1016\/j.jprot.2017.06.015","volume":"165","author":"R Chang","year":"2017","unstructured":"Chang R, Lv B, Li B (2017) Quantitative proteomics analysis by iTRAQ revealed underlying changes in thermotolerance of Arthrospira platensis. J Proteome 165:119\u2013131","journal-title":"J Proteome"},{"issue":"8","key":"9848_CR3","doi-asserted-by":"publisher","first-page":"2110","DOI":"10.1073\/pnas.69.8.2110","volume":"69","author":"SN Cohen","year":"1972","unstructured":"Cohen SN, Chang AC, Hsu L (1972) Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci 69(8):2110\u20132114","journal-title":"Proc Natl Acad Sci"},{"issue":"24","key":"9848_CR4","doi-asserted-by":"publisher","first-page":"8483","DOI":"10.1128\/MCB.21.24.8483-8489.2001","volume":"21","author":"JF Davidson","year":"2001","unstructured":"Davidson JF, Schiestl RH (2001) Mitochondrial respiratory electron carriers are involved in oxidative stress during heat stress in Saccharomyces cerevisiae. Mol Cell Biol 21(24):8483\u20138489","journal-title":"Mol Cell Biol"},{"issue":"10","key":"9848_CR5","doi-asserted-by":"publisher","first-page":"5116","DOI":"10.1073\/pnas.93.10.5116","volume":"93","author":"JF Davidson","year":"1996","unstructured":"Davidson JF, Whyte B, Bissinger PH, Schiestl RH (1996) Oxidative stress is involved in heat-induced cell death in Saccharomyces cerevisiae. Proc Natl Acad Sci 93(10):5116\u20135121","journal-title":"Proc Natl Acad Sci"},{"issue":"2","key":"9848_CR6","doi-asserted-by":"publisher","first-page":"629","DOI":"10.1007\/s00253-013-5327-6","volume":"98","author":"H Doi","year":"2014","unstructured":"Doi H, Hoshino Y, Nakase K, Usuda Y (2014) Reduction of hydrogen peroxide stress derived from fatty acid beta-oxidation improves fatty acid utilization in Escherichia coli. Appl Microbiol Biotechnol 98(2):629\u2013639","journal-title":"Appl Microbiol Biotechnol"},{"issue":"1","key":"9848_CR7","doi-asserted-by":"publisher","first-page":"136","DOI":"10.1016\/0003-2697(75)90415-7","volume":"64","author":"J Dulley","year":"1975","unstructured":"Dulley J, Grieve P (1975) A simple technique for eliminating interference by detergents in the Lowry method of protein determination. Anal Biochem 64(1):136\u2013141","journal-title":"Anal Biochem"},{"issue":"8","key":"9848_CR8","doi-asserted-by":"publisher","first-page":"1817","DOI":"10.1099\/13500872-140-8-1817","volume":"140","author":"BJ Eikmanns","year":"1994","unstructured":"Eikmanns BJ, Thum-Schmitz N, Eggeling L, L\u00fcdtke K-U, Sahm H (1994) Nucleotide sequence, expression and transcriptional analysis of the Corynebacterium glutamicum gltA gene encoding citrate synthase. Microbiol 140(8):1817\u20131828","journal-title":"Microbiol"},{"issue":"1","key":"9848_CR9","doi-asserted-by":"publisher","first-page":"2104","DOI":"10.4238\/2015.March.20.21","volume":"14","author":"HM El Shafey","year":"2015","unstructured":"El Shafey HM, Ghanem S (2015) Regulation of expression of sodA and msrA genes of Corynebacterium glutamicum in response to oxidative and radiative stress. Genet Mol Res 14(1):2104\u20132117","journal-title":"Genet Mol Res"},{"issue":"1","key":"9848_CR10","doi-asserted-by":"publisher","first-page":"80","DOI":"10.1016\/j.micres.2006.05.005","volume":"163","author":"HM El Shafey","year":"2008","unstructured":"El Shafey HM, Ghanem S, Merkamm M, Guyonvarch A (2008) Corynebacterium glutamicum superoxide dismutase is a manganese-strict non-cambialistic enzyme in vitro. Microbiol Res 163(1):80\u201386","journal-title":"Microbiol Res"},{"issue":"1","key":"9848_CR11","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1006\/mpat.1996.0004","volume":"20","author":"V Escuyer","year":"1996","unstructured":"Escuyer V, Haddad N, Frehel C, Berche P (1996) Molecular characterization of a surface-exposed superoxide dismutase of Mycobacterium avium. Microb Pathog 20(1):41\u201355","journal-title":"Microb Pathog"},{"issue":"1","key":"9848_CR12","doi-asserted-by":"publisher","first-page":"2586","DOI":"10.1038\/s41598-017-02736-7","volume":"7","author":"IV Fedoseeva","year":"2017","unstructured":"Fedoseeva IV, Pyatrikas DV, Stepanov AV, Fedyaeva AV, Varakina NN, Rusaleva TM, Borovskii GB, Rikhvanov EG (2017) The role of flavin-containing enzymes in mitochondrial membrane hyperpolarization and ROS production in respiring Saccharomyces cerevisiae cells under heat-shock conditions. Sci Rep 7(1):2586","journal-title":"Sci Rep"},{"key":"9848_CR13","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/S0076-6879(84)05013-8","volume":"105","author":"L Flohe","year":"1984","unstructured":"Flohe L, \u00d6tting F (1984) Superoxide dismutase assays. Methods Enzymol 105:93\u2013104","journal-title":"Methods Enzymol"},{"key":"9848_CR14","doi-asserted-by":"publisher","first-page":"1020","DOI":"10.1126\/science.aat8923","volume":"362","author":"H Gong","year":"2018","unstructured":"Gong H, Li J, Xu A, Tang Y, Ji W, Gao R, Wang S, Yu L, Tian C, Li J, Yen HY, Man Lam S, Shui G, Yang X, Sun Y, Li X, Jia M, Yang C, Jiang B, Lou Z, Robinson CV, Wong LL, Guddat LW, Sun F, Wang Q, Rao Z (2018) An electron transfer path connects subunits of a mycobacterial respiratory supercomplex. Science 362:1020 (eaat8923)","journal-title":"Science"},{"issue":"1","key":"9848_CR15","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/0003-2697(74)90440-0","volume":"58","author":"E Gregory","year":"1974","unstructured":"Gregory E, Fridovich I (1974) Visualization of catalase on acrylamide gels. Anal Biochem 58(1):57\u201362","journal-title":"Anal Biochem"},{"issue":"4","key":"9848_CR16","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1016\/S0022-2836(83)80284-8","volume":"166","author":"D Hanahan","year":"1983","unstructured":"Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166(4):557\u2013580","journal-title":"J Mol Biol"},{"issue":"7","key":"9848_CR17","doi-asserted-by":"publisher","first-page":"4281","DOI":"10.1074\/jbc.274.7.4281","volume":"274","author":"G Harth","year":"1999","unstructured":"Harth G, Horwitz MA (1999) Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery a model for studying export of leaderless proteins by pathogenic mycobacteria. J Biol Chem 274(7):4281\u20134292","journal-title":"J Biol Chem"},{"issue":"10","key":"9848_CR18","doi-asserted-by":"publisher","first-page":"2696","DOI":"10.1128\/JB.182.10.2696-2701.2000","volume":"182","author":"T Hirasawa","year":"2000","unstructured":"Hirasawa T, Wachi M, Nagai K (2000) A mutation in the Corynebacterium glutamicum ltsA gene causes susceptibility to lysozyme, temperature-sensitive growth, and l-glutamate production. J Bacteriol 182(10):2696\u20132701","journal-title":"J Bacteriol"},{"issue":"10","key":"9848_CR19","doi-asserted-by":"publisher","first-page":"1705","DOI":"10.1016\/j.bbabio.2016.07.009","volume":"1857","author":"WC Kao","year":"2016","unstructured":"Kao WC, Kleinschroth T, Nitschke W, Baymann F, Neehaul Y, Hellwig P, Richers S, Vonck J, Bott M, Hunte C (2016) The obligate respiratory supercomplex from Actinobacteria. Biochim Biophys Acta 1857(10):1705\u20131714","journal-title":"Biochim Biophys Acta"},{"issue":"3","key":"9848_CR20","doi-asserted-by":"publisher","first-page":"e31709","DOI":"10.1371\/journal.pone.0031709","volume":"7","author":"J-S Kim","year":"2012","unstructured":"Kim J-S, Holmes RK (2012) Characterization of OxyR as a negative transcriptional regulator that represses catalase production in Corynebacterium diphtheriae. PLoS One 7(3):e31709","journal-title":"PLoS One"},{"issue":"3","key":"9848_CR21","doi-asserted-by":"publisher","first-page":"757","DOI":"10.1016\/j.bbrc.2005.09.115","volume":"337","author":"T-H Kim","year":"2005","unstructured":"Kim T-H, Park J-S, Kim H-J, Kim Y, Kim P, Lee H-S (2005) The whcE gene of Corynebacterium glutamicum is important for survival following heat and oxidative stress. Biochem Biophys Res Commun 337(3):757\u2013764","journal-title":"Biochem Biophys Res Commun"},{"key":"9848_CR22","doi-asserted-by":"publisher","first-page":"193","DOI":"10.2323\/jgam.3.193","volume":"503","author":"S Kinoshita","year":"1957","unstructured":"Kinoshita S, Udaka S, Shimono M (1957) Studies on the amino acid fermentation: I. Production of l-glutamic acid by various microorganisms. J Gen Appl Microbiol 503:193\u2013205","journal-title":"J Gen Appl Microbiol"},{"issue":"11\u201312","key":"9848_CR23","doi-asserted-by":"publisher","first-page":"1332","DOI":"10.1016\/j.bbabio.2013.03.009","volume":"1827","author":"P Lanciano","year":"2013","unstructured":"Lanciano P, Khalfaoui-Hassani B, Selamoglu N, Ghelli A, Rugolo M, Daldal F (2013) Molecular mechanisms of superoxide production by complex III: a bacterial versus human mitochondrial comparative case study. Biochim Biophys Acta 1827(11\u201312):1332\u20131339","journal-title":"Biochim Biophys Acta"},{"key":"9848_CR24","doi-asserted-by":"publisher","first-page":"310","DOI":"10.1016\/j.ymben.2016.07.009","volume":"38","author":"Z Man","year":"2016","unstructured":"Man Z, Rao Z, Xu M, Guo J, Yang T, Zhang X, Xu Z (2016) Improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Metab Eng 38:310\u2013321","journal-title":"Metab Eng"},{"issue":"10","key":"9848_CR25","doi-asserted-by":"publisher","first-page":"e00354","DOI":"10.1128\/AEM.00354-18","volume":"84","author":"N Matsumoto","year":"2018","unstructured":"Matsumoto N, Hattori H, Matsutani M, Matayoshi C, Toyama H, Kataoka N, Yakushi T, Matsushita K (2018) A single-nucleotide insertion in a drug transporter gene induces a thermotolerant phenotype of Gluconobacter frateurii by increasing the NADPH\/NADP+ ratio via metabolic change. Appl Environ Microbiol 84(10):e00354\u2013e00318","journal-title":"Appl Environ Microbiol"},{"issue":"10","key":"9848_CR26","doi-asserted-by":"publisher","first-page":"1968","DOI":"10.1271\/bbb.62.1968","volume":"62","author":"K Matsushita","year":"1998","unstructured":"Matsushita K, Yamamoto T, Toyama H, Adachi O (1998) NADPH oxidase system as a superoxide-generating cyanide-resistant pathway in the respiratory chain of Corynebacterium glutamicum. Biosci Biotechnol Biochem 62(10):1968\u20131977","journal-title":"Biosci Biotechnol Biochem"},{"issue":"4","key":"9848_CR27","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1080\/09168451.2015.1104235","volume":"80","author":"K Matsushita","year":"2016","unstructured":"Matsushita K, Azuma Y, Kosaka T, Yakushi T, Hoshida H, Akada R, Yamada M (2016) Genomic analyses of thermotolerant microorganisms used for high-temperature fermentations. Biosci Biotechnol Biochem 80(4):655\u2013668","journal-title":"Biosci Biotechnol Biochem"},{"issue":"1","key":"9848_CR28","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1186\/1477-5956-11-45","volume":"11","author":"M McNamara","year":"2013","unstructured":"McNamara M, Tzeng S-C, Maier C, Wu M, Bermudez LE (2013) Surface-exposed proteins of pathogenic mycobacteria and the role of cu-zn superoxide dismutase in macrophages and neutrophil survival. Proteome Sci 11(1):45","journal-title":"Proteome Sci"},{"issue":"4","key":"9848_CR29","doi-asserted-by":"publisher","first-page":"1284","DOI":"10.1128\/JB.2001.183.4.1284-1295.2001","volume":"183","author":"M Merkamm","year":"2001","unstructured":"Merkamm M, Guyonvarch A (2001) Cloning of the sodA gene from Corynebacterium melassecola and role of superoxide dismutase in cellular viability. J Bacteriol 183(4):1284\u20131295","journal-title":"J Bacteriol"},{"issue":"15","key":"9848_CR30","doi-asserted-by":"publisher","first-page":"10119","DOI":"10.1074\/jbc.274.15.10119","volume":"274","author":"KR Messner","year":"1999","unstructured":"Messner KR, Imlay JA (1999) The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. J Biol Chem 274(15):10119\u201310128","journal-title":"J Biol Chem"},{"issue":"45","key":"9848_CR31","doi-asserted-by":"publisher","first-page":"42563","DOI":"10.1074\/jbc.M204958200","volume":"277","author":"KR Messner","year":"2002","unstructured":"Messner KR, Imlay JA (2002) Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase. J Biol Chem 277(45):42563\u201342571","journal-title":"J Biol Chem"},{"issue":"2\u20133","key":"9848_CR32","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1016\/S0168-1656(02)00136-0","volume":"98","author":"A Muffler","year":"2002","unstructured":"Muffler A, Bettermann S, Haushalter M, H\u00f6rlein A, Neveling U, Schramm M, Sorgenfrei O (2002) Genome-wide transcription profiling of Corynebacterium glutamicum after heat shock and during growth on acetate and glucose. J Biotechnol 98(2\u20133):255\u2013268","journal-title":"J Biotechnol"},{"issue":"1","key":"9848_CR33","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1271\/bbb.69.149","volume":"69","author":"N Nantapong","year":"2005","unstructured":"Nantapong N, Otofuji A, Migita TC, Adachi O, Toyama H, Matsushita K (2005) Electron transfer ability from NADH to menaquinone and from NADPH to oxygen of type II NADH dehydrogenase of Corynebacterium glutamicum. Biosci Biotechnol Biochem 69(1):149\u2013159","journal-title":"Biosci Biotechnol Biochem"},{"issue":"7","key":"9848_CR34","doi-asserted-by":"publisher","first-page":"1572","DOI":"10.1101\/gr.1285603","volume":"13","author":"Y Nishio","year":"2003","unstructured":"Nishio Y, Nakamura Y, Kawarabayasi Y, Usuda Y, Kimura E, Sugimoto S, Matsui K, Yamagishi A, Kikuchi H, Ikeo K (2003) Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens. Genome Res 13(7):1572\u20131579","journal-title":"Genome Res"},{"issue":"1","key":"9848_CR35","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1007\/s00253-003-1254-2","volume":"62","author":"J Ohnishi","year":"2003","unstructured":"Ohnishi J, Hayashi M, Mitsuhashi S, Ikeda M (2003) Efficient 40\u00a0\u00b0C fermentation of L-lysine by a new Corynebacterium glutamicum mutant developed by genome breeding. Appl Microbiol Biotechnol 62(1):69\u201375","journal-title":"Appl Microbiol Biotechnol"},{"key":"9848_CR36","doi-asserted-by":"crossref","unstructured":"Oka A, Sugisaki H, Takanami M (1981) Nucleotide sequence of the kanamycin resistance transposon Tn903. J Mol Biol 147(2):217\u2013226","DOI":"10.1016\/0022-2836(81)90438-1"},{"issue":"12","key":"9848_CR37","doi-asserted-by":"publisher","first-page":"fnv082","DOI":"10.1093\/femsle\/fnv082","volume":"362","author":"DV Pyatrikas","year":"2015","unstructured":"Pyatrikas DV, Fedoseeva IV, Varakina NN, Rusaleva TM, Stepanov AV, Fedyaeva AV, Borovskii GB, Rikhvanov EG (2015) Relation between cell death progression, reactive oxygen species production and mitochondrial membrane potential in fermenting Saccharomyces cerevisiae cells under heat-shock conditions. FEMS Microbiol Lett 362(12):fnv082","journal-title":"FEMS Microbiol Lett"},{"key":"9848_CR38","volume-title":"Molecular cloning: a laboratory manual","author":"J Sambrook","year":"2001","unstructured":"Sambrook J, Russell DW (2001) Molecular cloning: a laboratory manual. Coldspring-Harbour Laboratory Press, United Kingdom"},{"issue":"24","key":"9848_CR39","doi-asserted-by":"publisher","first-page":"7643","DOI":"10.1128\/AEM.01490-08","volume":"74","author":"C Schulte","year":"2008","unstructured":"Schulte C, Arensk\u00f6tter M, Berekaa MM, Arensk\u00f6tter Q, Priefert H, Steinb\u00fcchel A (2008) Possible involvement of an extracellular superoxide dismutase (SodA) as a radical scavenger in poly (cis-1, 4-isoprene) degradation. Appl Environ Microbiol 74(24):7643\u20137653","journal-title":"Appl Environ Microbiol"},{"issue":"12","key":"9848_CR40","doi-asserted-by":"publisher","first-page":"1380","DOI":"10.1007\/s00299-006-0199-1","volume":"25","author":"L Tang","year":"2006","unstructured":"Tang L, Kwon SY, Kim SH, Kim JS, Choi JS, Cho KY, Sung CK, Kwak SS, Lee HS (2006) Enhanced tolerance of transgenic potato plants expressing both superoxide dismutase and ascorbate peroxidase in chloroplasts against oxidative stress and high temperature. Plant Cell Rep 25(12):1380\u20131386","journal-title":"Plant Cell Rep"},{"issue":"2","key":"9848_CR41","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1111\/j.1462-2920.2012.02848.x","volume":"15","author":"ZL Wang","year":"2013","unstructured":"Wang ZL, Zhang LB, Ying SH, Feng MG (2013) Catalases play differentiated roles in the adaptation of a fungal entomopathogen to environmental stresses. Environ Microbiol 15(2):409\u2013418","journal-title":"Environ Microbiol"},{"key":"9848_CR42","unstructured":"Yokoi H, Ohnishi J, Ochiai K, Yonetani Y, Ozaki A (2000) Novel desensitized aspartokinase. Patent WO 00\/63388"},{"issue":"2","key":"9848_CR43","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1099\/mic.0.25913-0","volume":"149","author":"T Yoshida","year":"2003","unstructured":"Yoshida T, Ayabe Y, Yasunaga M, Usami Y, Habe H, Nojiri H, Omori T (2003) Genes involved in the synthesis of the exopolysaccharide methanolan by the obligate methylotroph Methylobacillus sp. strain 12S. Microbiol 149(2):431\u2013444","journal-title":"Microbiol"}],"container-title":["Applied Microbiology and Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00253-019-09848-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s00253-019-09848-2\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00253-019-09848-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,5,16]],"date-time":"2020-05-16T06:23:42Z","timestamp":1589610222000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s00253-019-09848-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,4,30]]},"references-count":43,"journal-issue":{"issue":"13","published-print":{"date-parts":[[2019,7]]}},"alternative-id":["9848"],"URL":"https:\/\/doi.org\/10.1007\/s00253-019-09848-2","relation":{},"ISSN":["0175-7598","1432-0614"],"issn-type":[{"value":"0175-7598","type":"print"},{"value":"1432-0614","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,4,30]]},"assertion":[{"value":"7 January 2019","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 April 2019","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 April 2019","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 April 2019","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with ethical standards"}},{"value":"The authors declare that they have no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"This article does not contain any studies with human participants or animals performed by any of the authors.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical statement"}}]}}