دورية أكاديمية

Microbial Degradation of Amino Acid-Containing Compounds Using the Microcystin-Degrading Bacterial Strain B-9

التفاصيل البيبلوغرافية
العنوان: Microbial Degradation of Amino Acid-Containing Compounds Using the Microcystin-Degrading Bacterial Strain B-9
المؤلفون: Haiyan Jin, Yoshiko Hiraoka, Yurie Okuma, Elisabete Hiromi Hashimoto, Miki Kurita, Andrea Roxanne J. Anas, Hitoshi Uemura, Kiyomi Tsuji, Ken-Ichi Harada
المصدر: Marine Drugs, Vol 16, Iss 2, p 50 (2018)
بيانات النشر: MDPI AG, 2018.
سنة النشر: 2018
المجموعة: LCC:Biology (General)
مصطلحات موضوعية: microcystin-degrading bacteria, mycotoxin, protease, esterase, inhibitor, Biology (General), QH301-705.5
الوصف: Strain B-9, which has a 99% similarity to Sphingosinicella microcystinivorans strain Y2, is a Gram-negative bacterium with potential for use in the degradation of microcystin-related compounds and nodularin. We attempted to extend the application area of strain B-9 and applied it to mycotoxins produced by fungi. Among the tested mycotoxins, only ochratoxin A was completely hydrolyzed to provide the constituents ochratoxin α and l-phenylalanine, and levels of fumonisin B1 gradually decreased after 96 h. However, although drugs including antibiotics released into the aquatic environment were applied for microbial degradation using strain B-9, no degradation occurred. These results suggest that strain B-9 can only degrade amino acid-containing compounds. As expected, the tested compounds with amide and ester bonds, such as 3,4-dimethyl hippuric acid and 4-benzyl aspartate, were readily hydrolyzed by strain B-9, although the sulfonamides remained unchanged. The ester compounds were characteristically and rapidly hydrolyzed as soon as they came into contact with strain B-9. Furthermore, the degradation of amide and ester compounds with amino acids was not inhibited by the addition of ethylenediaminetetraacetic acid (EDTA), indicating that the responsible enzyme was not MlrC. These results suggest that strain B-9 possesses an additional hydrolytic enzyme that should be designated as MlrE, as well as an esterase.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1660-3397
Relation: http://www.mdpi.com/1660-3397/16/2/50; https://doaj.org/toc/1660-3397
DOI: 10.3390/md16020050
URL الوصول: https://doaj.org/article/f57a4735fbd44b2ea5463093527ba743
رقم الأكسشن: edsdoj.f57a4735fbd44b2ea5463093527ba743
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:16603397
DOI:10.3390/md16020050