l-Amino acid oxidases from microbial sources: types,properties, functions,and applications |
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Authors: | Gazi Sakir Hossain Jianghua Li Hyun-dong Shin Guocheng Du Long Liu Jian Chen |
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Affiliation: | 1. Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi, 214122, China 2. State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, 200237, China 3. Synergetic Innovation Center of Food Safety and Nutrition, Wuxi, 214122, China 4. School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, 30332, USA 5. National Engineering of Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi, 214122, China
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Abstract: | l-Amino acid oxidases (LAAOs), which catalyze the stereospecific oxidative deamination of l-amino acids to α-keto acids and ammonia, are flavin adenine dinucleotide-containing homodimeric proteins. l-Amino acid oxidases are widely distributed in diverse organisms and have a range of properties. Because expressing LAAOs as recombinant proteins in heterologous hosts is difficult, their biotechnological applications have not been thoroughly advanced. LAAOs are thought to contribute to amino acid catabolism, enhance iron acquisition, display antimicrobial activity, and catalyze keto acid production, among other roles. Here, we review the types, properties, structures, biological functions, heterologous expression, and applications of LAAOs obtained from microbial sources. We expect this review to increase interest in LAAO studies. |
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