{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,7,27]],"date-time":"2024-07-27T10:00:17Z","timestamp":1722074417197},"reference-count":34,"publisher":"Oxford University Press (OUP)","issue":"1","license":[{"start":{"date-parts":[[2012,1,1]],"date-time":"2012-01-01T00:00:00Z","timestamp":1325376000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2012,1,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>A novel enzymatic route for the synthesis of 2-amino-2,3-dimethylbutyramide (ADBA), important intermediate of highly potent and broad-spectrum imidazolinone herbicides, from 2-amino-2,3-dimethylbutyronitrile (ADBN) was developed. Strain Rhodococcus boritolerans CCTCC M 208108 harboring nitrile hydratase (NHase) towards ADBN was screened through a sophisticated colorimetric screening method and was found to be resistant to cyanide (5\u00a0mM). Resting cells of R. boritolerans CCTCC M 208108 also proved to be tolerant against high product concentration (40\u00a0g\u00a0l\u22121) and alkaline pH (pH 9.3). A preparative scale process for continuous production of ADBA in both aqueous and biphasic systems was developed and some key parameters of the biocatalytic process were optimized. Inhibition of NHase by cyanide dissociated from ADBN was successfully overcome by temperature control (at 10\u00b0C). The product concentration, yield and catalyst productivity were further improved to 50\u00a0g\u00a0l\u22121, 91% and 6.3\u00a0g product\/g catalyst using a 30\/70 (v\/v) n-hexane\/water biphasic system. Furthermore, cells of R. boritolerans CCTCC M 208108 could be reused for at lease twice by stopping the continuous reaction before cyanide concentration rose to 2\u00a0mM, with the catalyst productivity increasing to 12.3\u00a0g product\/g catalyst. These results demonstrated that enzymatic synthesis of ADBA using whole cells of R. boritolerans CCTCC M 208108 showed potential for industrial application.<\/jats:p>","DOI":"10.1007\/s10295-011-1008-6","type":"journal-article","created":{"date-parts":[[2011,7,1]],"date-time":"2011-07-01T01:12:02Z","timestamp":1309482722000},"page":"133-141","source":"Crossref","is-referenced-by-count":8,"title":["Enzymatic production of 2-amino-2,3-dimethylbutyramide by cyanide-resistant nitrile hydratase"],"prefix":"10.1093","volume":"39","author":[{"given":"Zhi-Jian","family":"Lin","sequence":"first","affiliation":[{"name":"grid.413273.0 0000000105748737 Institute of Bioengineering Zhejiang University of Technology 18 Chaowang Road 310014 Hangzhou People\u2019s Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ren-Chao","family":"Zheng","sequence":"additional","affiliation":[{"name":"grid.413273.0 0000000105748737 Institute of Bioengineering Zhejiang University of Technology 18 Chaowang Road 310014 Hangzhou People\u2019s Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ya-Jun","family":"Wang","sequence":"additional","affiliation":[{"name":"grid.413273.0 0000000105748737 Institute of Bioengineering Zhejiang University of Technology 18 Chaowang Road 310014 Hangzhou People\u2019s Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yu-Guo","family":"Zheng","sequence":"additional","affiliation":[{"name":"grid.413273.0 0000000105748737 Institute of Bioengineering Zhejiang University of Technology 18 Chaowang Road 310014 Hangzhou People\u2019s Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yin-Chu","family":"Shen","sequence":"additional","affiliation":[{"name":"grid.413273.0 0000000105748737 Institute of Bioengineering Zhejiang University of Technology 18 Chaowang Road 310014 Hangzhou People\u2019s Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2012,1,1]]},"reference":[{"key":"2021033103273328700_CR1","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1016\/j.cropro.2004.09.011","article-title":"Efficacy of imidazolinone herbicides applied to imidazolinone-resistant maize and their carryover effect on rotational crops","volume":"24","author":"Alister","year":"2005","journal-title":"Crop Prot"},{"key":"2021033103273328700_CR2","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1007\/s00253-002-1062-0","article-title":"The nitrile-degrading enzymes: current status and future prospects","volume":"60","author":"Banerjee","year":"2002","journal-title":"Appl Microbiol Biotechnol"},{"key":"2021033103273328700_CR3"},{"key":"2021033103273328700_CR4","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1007\/s00253-003-1495-0","article-title":"Characterisation of nitrilase and nitrile hydratase biocatalytic systems","volume":"64","author":"Brady","year":"2004","journal-title":"Appl Microbiol Biotechnol"},{"key":"2021033103273328700_CR5","doi-asserted-by":"publisher","first-page":"547","DOI":"10.1002\/elsc.200402153","article-title":"Bioconversion of D, L-tert-leucine nitrile to D-tert-leucine by recombinant cells expressing nitrile hydratase and D-selective amidase","volume":"4","author":"Brand\u00e3o","year":"2004","journal-title":"Eng Life Sci"},{"key":"2021033103273328700_CR6","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1007\/s10295-004-0200-3","article-title":"Nitrile bioconversion by Microbacterium imperiale CBS 498\u201374 resting cells in batch and ultrafiltration membrane bioreactors","volume":"33","author":"Cantarella","year":"2006","journal-title":"J Ind Microbiol Biotechnol"},{"key":"2021033103273328700_CR7","doi-asserted-by":"publisher","first-page":"1405","DOI":"10.1002\/adsc.200700085","article-title":"Enzymatic transformations 63. 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