{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T20:52:23Z","timestamp":1768337543176,"version":"3.49.0"},"reference-count":51,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2009,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            A triphasic process was developed for the production of \u03b2 dipeptides from cyanophycin (CGP) on a large scale. Phase I comprises an optimized acid extraction method for technical isolation of CGP from biomass. It yielded highly purified CGP consisting of aspartate, arginine, and a little lysine. Phase II comprises the fermentative production of an extracellular CGPase (CphE\n            <jats:sub>al<\/jats:sub>\n            ) from\n            <jats:italic>Pseudomonas alcaligenes<\/jats:italic>\n            strain DIP1 on a 500-liter scale in mineral salts medium, with citrate as the sole carbon source and CGP as an inductor. During optimization, it was shown that 2 g liter\n            <jats:sup>\u22121<\/jats:sup>\n            citrate, pH 6.5, and 37\u00b0C are ideal parameters for CphE\n            <jats:sub>al<\/jats:sub>\n            production. Maximum enzyme yields were obtained after induction in the presence of 50 mg liter\n            <jats:sup>\u22121<\/jats:sup>\n            CGP or CGP dipeptides for 5 or 3 h, respectively. Aspartate at a concentration of 4 g liter\n            <jats:sup>\u22121<\/jats:sup>\n            induced CphE\n            <jats:sub>al<\/jats:sub>\n            production with only about 30% efficiency in comparison to that with CGP. CphE\n            <jats:sub>al<\/jats:sub>\n            was purified utilizing its affinity for the substrate and its specific binding to CGP. CphE\n            <jats:sub>al<\/jats:sub>\n            turned out to be a serine protease with maximum activity at 50\u00b0C and at pH 7 to 8.5. Phase III comprises degradation of CGP to \u03b2-aspartate-arginine and \u03b2-aspartate-lysine dipeptides with a purity of over 99% (by thin-layer chromatography and high-performance liquid chromatography), employing a crude CphE\n            <jats:sub>al<\/jats:sub>\n            preparation. Optimum degradation parameters were 100 g liter\n            <jats:sup>\u22121<\/jats:sup>\n            CGP, 10 g liter\n            <jats:sup>\u22121<\/jats:sup>\n            crude CphE\n            <jats:sub>al<\/jats:sub>\n            powder, and 4 h of incubation at 50\u00b0C. The overall efficiency of phase III was 91%, while 78% (wt\/wt) of the used CphE\n            <jats:sub>al<\/jats:sub>\n            powder with sustained activity toward CGP was recovered. The optimized process was performed with industrial materials and equipment and is applicable to any desired scale.\n          <\/jats:p>","DOI":"10.1128\/aem.01344-08","type":"journal-article","created":{"date-parts":[[2008,11,1]],"date-time":"2008-11-01T00:56:19Z","timestamp":1225500979000},"page":"29-38","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":52,"title":["Biotechnological Process for Production of \u03b2-Dipeptides from Cyanophycin on a Technical Scale and Its Optimization"],"prefix":"10.1128","volume":"75","author":[{"given":"Ahmed","family":"Sallam","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Molekulare Mikrobiologie und Biotechnologie, Westf\u00e4lische Wilhelms-Universit\u00e4t M\u00fcnster, D-48149 M\u00fcnster, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alene","family":"Kast","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Molekulare Mikrobiologie und Biotechnologie, Westf\u00e4lische Wilhelms-Universit\u00e4t M\u00fcnster, D-48149 M\u00fcnster, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Simon","family":"Przybilla","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Molekulare Mikrobiologie und Biotechnologie, Westf\u00e4lische Wilhelms-Universit\u00e4t M\u00fcnster, D-48149 M\u00fcnster, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tobias","family":"Meiswinkel","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Molekulare Mikrobiologie und Biotechnologie, Westf\u00e4lische Wilhelms-Universit\u00e4t M\u00fcnster, D-48149 M\u00fcnster, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexander","family":"Steinb\u00fcchel","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Molekulare Mikrobiologie und Biotechnologie, Westf\u00e4lische Wilhelms-Universit\u00e4t M\u00fcnster, D-48149 M\u00fcnster, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_1_2_2","doi-asserted-by":"publisher","DOI":"10.1007\/s002030000206"},{"key":"e_1_3_1_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/bm010075a"},{"key":"e_1_3_1_4_2","unstructured":"Lipases with improved surfactant resistance. 1995"},{"key":"e_1_3_1_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.141.2.687-693.1980"},{"key":"e_1_3_1_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(88)67022-4"},{"key":"e_1_3_1_7_2","first-page":"28","volume":"1","year":"1887","unstructured":"Borzi, A. 1887. 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