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Application of Bacterial Thermostable Lipolytic Enzymes in the Modern Biotechnological Processes: A Review Review

Journal Catalysis in Industry
ISSN: 2070-0504 , E-ISSN: 2070-0555
Output data Year: 2019, Volume: 11, Number: 2, Pages: 168-178 Pages count : 11 DOI: 10.1134/S2070050419020107
Tags bacterial enzymes; biocatalysis; esterase; immobilization; lipase
Authors Samoylova Yu.V. 1 , Sorokina K.N. 1 , Piligaev A.V. 1 , Parmon V.N. 1
Affiliations
1 Boreskov Institute of Catalysis, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russian Federation

Funding (1)

1 Federal Agency for Scientific Organizations 0303-2016-0012 (V.47.1.4.)

Abstract: Review focuses on the modern applications of bacterial lipolytic enzymes in biotechnology and covers the scope of their properties including their activity and functional stability at different temperatures, pH, substrate specificity, and activity in the presence of different chemicals. The recent data on the production of genetically engineered strains producing the bacterial lipolytic enzymes and approaches to improving their productivity are presented. The applications of bacterial lipases in biotechnological processes used in the production of biofuel, chemicals and detergents, in the food industry, and in wastewater treatment are considered. © 2019, Pleiades Publishing, Ltd.
Cite: Samoylova Y.V. , Sorokina K.N. , Piligaev A.V. , Parmon V.N.
Application of Bacterial Thermostable Lipolytic Enzymes in the Modern Biotechnological Processes: A Review
Catalysis in Industry. 2019. V.11. N2. P.168-178. DOI: 10.1134/S2070050419020107 WOS Scopus РИНЦ OpenAlex
Original: Самойлова Ю.В. , Сорокина К.Н. , Пилигаев А.В. , Пармон В.Н.
Применение бактериальных термостабильных липолитических ферментов в современных биотехнологических процессах: обзор
Катализ в промышленности. 2018. Т.18. №6. С.61-73. DOI: 10.18412/1816-0387-2018-6-61-73RSCI РИНЦ AN OpenAlex
Dates:
Submitted: Sep 13, 2018
Accepted: Oct 18, 2018
Published print: Apr 1, 2019
Published online: Jun 25, 2019
Identifiers:
Web of science: WOS:000472891400011
Scopus: 2-s2.0-85067911242
Elibrary: 41685250
OpenAlex: W2954283581
Citing:
DB Citing
Scopus 9
Web of science 9
Elibrary 10
OpenAlex 13
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