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Preparation of Stable Cross-Linked Enzyme Aggregates (CLEAs) of a Ureibacillus thermosphaericus Esterase for Application in Malathion Removal from Wastewater Научная публикация

Журнал Catalysts
ISSN: 2073-4344
Вых. Данные Год: 2018, Том: 8, Номер: 4, Номер статьи : 154, Страниц : 19 DOI: 10.3390/catal8040154
Ключевые слова molecular chaperones; esterase; Ureibacillus thermosphaericus; cross-linked enzyme aggregates; response surface methodology; malathion hydrolysis
Авторы Samoylova Yuliya V. 1 , Sorokina Ksenia N. 1,2 , Piligaev Alexander V. 1 , Parmon Valentin N. 1,2
Организации
1 Boreskov Institute of Catalysis (BIC), Lavrentieva ave. 5, 630090 Novosibirsk, Russia
2 Novosibirsk State University (NSU), Pirogova str. 2, 630090 Novosibirsk, Russia

Информация о финансировании (1)

1 Российский фонд фундаментальных исследований 18-38-00386

Реферат: In this study, the active and stable cross-linked enzyme aggregates (CLEAs) of the thermostable esterase estUT1 of the bacterium Ureibacillus thermosphaericus were prepared for application in malathion removal from municipal wastewater. Co-expression of esterase with an E. coli chaperone team (KJE, ClpB, and ELS) increased the activity of the soluble enzyme fraction up to 200.7 ± 15.5 U mg–1. Response surface methodology (RSM) was used to optimize the preparation of the CLEA-estUT1 biocatalyst to maximize its activity and minimize enzyme loss. CLEA-estUT1 with the highest activity of 29.4 ± 0.5 U mg–1 (90.6 ± 2.7% of the recovered activity) was prepared with 65.1% (w/v) ammonium sulfate, 120.6 mM glutaraldehyde, and 0.2 mM bovine serum albumin at 5.1 h of cross-linking. The biocatalyst has maximal activity at 80 ºC and pH 8.0. Analysis of the properties of CLEA-estUT1 and free enzyme at 50–80 ºC and pH 5.0–10.0 showed higher stability of the biocatalyst. CLEA-estUT1 showed marked tolerance against a number of chemicals and high operational stability and activity in the reaction of malathion hydrolysis in wastewater (up to 99.5 ± 1.4%). After 25 cycles of malathion hydrolysis at 37 ºC, it retained 55.2 ± 1.1% of the initial activity. The high stability and reusability of CLEA-estUT1 make it applicable for the degradation of insecticides.
Библиографическая ссылка: Samoylova Y.V. , Sorokina K.N. , Piligaev A.V. , Parmon V.N.
Preparation of Stable Cross-Linked Enzyme Aggregates (CLEAs) of a Ureibacillus thermosphaericus Esterase for Application in Malathion Removal from Wastewater
Catalysts. 2018. V.8. N4. 154 :1-19. DOI: 10.3390/catal8040154 WOS Scopus РИНЦ CAPlus OpenAlex
Файлы: Полный текст от издателя
Даты:
Поступила в редакцию: 26 мар. 2018 г.
Принята к публикации: 8 апр. 2018 г.
Опубликована в печати: 11 апр. 2018 г.
Опубликована online: 11 апр. 2018 г.
Идентификаторы БД:
Web of science: WOS:000435186400031
Scopus: 2-s2.0-85045387811
РИНЦ: 35543626
Chemical Abstracts: 2018:1037829
OpenAlex: W2797412097
Цитирование в БД:
БД Цитирований
Web of science 24
Scopus 27
РИНЦ 27
OpenAlex 26
Альметрики: