Bacillus licheniformis protease-catalyzed peptide synthesis via the kinetically controlled approach using the carbamoylmethyl ester as an acyl donor in anhydrous acetonitrile |
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Authors: | Miyazawa Toshifumi Hiramatsu Makoto Murashima Takashi Yamada Takashi |
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Affiliation: | (1) Department of Chemistry, Faculty of Science and Engineering, Konan University, 658-8501 Kobe, Japan |
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Abstract: | Summary The couplings ofN-protected amino acid esters with amino acid amides proved to be carried out in anhydrous acetonitrile in the presence ofBacillus licheniformis protease (subtilisin Carlsberg) immobilized on Celite. The maximal peptide yields were obtained with the immobilized enzyme prepared through lyophilization from a pH 10.7 buffer solution. A series of dipeptide syntheses and several segment condensations were achieved generally in high yields by the combined use of the immobilized enzyme prepared from this pH and the carbamoylmethyl ester as the acyl donor. |
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Keywords: | Bacillus licheniformis protease carbamoylmethyl ester pH effect protease-catalyzed peptide synthesis |
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