Production, purification and characterization of an extracellular lipase from Mucor hiemalis f. hiemalis

Hiol, Abel; Jonzo, Marie D; Druet, Danièle; Comeau, Louis-Claude

doi:10.1016/s0141-0229(99)00009-5

Cited by 96 publications

(56 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The residual activity was 68% in the presence of hexane, but was less than 40% in that of others. This was similar to other reported lipases which were fairly stable in hydrophobic solvents such as hexane, but were highly denatured in hydrophilic solvents such as acetone, DCM and DMF (Hiol et al, 1999;Kitaguchi and Klibanov, 1989).…”

supporting

confidence: 91%

Growth and lipase production of a psychrotrophic Acinetobacter calcoaceticus in an MSG-containing medium

Mongkolthanaruk

Probnarong

Lertsiri

et al. 2004

J. Gen. Appl. Microbiol.

View full text Add to dashboard Cite

supporting

confidence: 91%

Growth and lipase production of a psychrotrophic Acinetobacter calcoaceticus in an MSG-containing medium

Mongkolthanaruk

Probnarong

Lertsiri

et al. 2004

J. Gen. Appl. Microbiol.

View full text Add to dashboard Cite

“…lipase had good stability in hexane but was highly denatured in hydrophilic solvents, especially methanol. This behaviour was also observed by Hiol et al (1999Hiol et al ( , 2000 for M. hiemalis and R. oryzae lipases. …”

Section: Figuresupporting

confidence: 72%

“…As shown in Figure 3, upon analytical SDS-PAGE, the purified enzyme, appeared as a single band with molecular mass around 40 KDa. Upon gel filtration, a single peak of lipase activity was eluted and corresponded to a protein of molecular mass of 37.5 KDa (Figure 2, (HIOL et al, 1999).…”

Section: Resultsmentioning

confidence: 99%

Purification and biochemical characterization of an extracellular lipase produced by a new strain of Rhizopus sp.

Koblitz

Pastore

2006

Ciênc. agrotec.

View full text Add to dashboard Cite

The present study had as a goal to purify and characterize the lipolytic fraction secreted by a strain of Rhizopus sp. Only 3 steps of purification were necessary to achieve SDS-PAGE homogeneity. One band with 37.5 KDa molecular mass and with 1446 U/ mg specific activity was obtained. The purified fraction presented 2 lipase isoforms; both showed optimum activity at 50ºC, and were stable between 6.5 and 7.5 pH values and at temperatures below 50ºC and also kept their activity in hexane. The lipase was inactivated by Hg +2 and by n-bromosuccinimide and activated by Na + .Index terms: Lipase, Rhizopus sp., purification, biochemical characterization. RESUMOO presente trabalho teve por objetivo purificar e caracterizar a fração lipolítica secretada por uma linhagem de Rhizopus sp. Apenas 3 etapas de purificação foram necessárias para alcançar homogeneidade em eletroforese de proteína desnaturada. Uma única banda com massa molecular de 37,5 KDa e atividade específica de 1446U/mg foi obtida. A fração purificada apresentou 2 isoformas de lipase, ambas com temperatura ótima de atividade igual a 50ºC, mantiveram-se estáveis entre valores de pH entre 6,5 e 7,5 e a temperaturas inferiores a 50ºC e mantiveram sua atividade na presença de hexano. A fração lipolítica foi inativada por Hg + e por nbromosuccinimida e ativada por Na + .Termos para indexação: Lipase, Rhizopus sp., purificação, caracterização bioquímica.

show abstract

“…In the case of lipases from filamentous fungi, chain-length specificity generally varies between C8 and C18 [14,34]. Most zygomycete lipases present maximal activity for medium-or long-chain acids, but some of them have high reaction specificity for C2 to C6 acids as well [33,35].…”

Section: Hydrolysis Of Various Aryl Estersmentioning

confidence: 99%

Purification and Properties of Extracellular Lipases with Transesterification Activity and 1,3-Regioselectivity from Rhizomucor miehei and Rhizopus oryzae

Takó¹,

Kotogán²,

Papp³

et al. 2017

Journal of Microbiology and Biotechnology

View full text Add to dashboard Cite

Production, purification and characterization of an extracellular lipase from Mucor hiemalis f. hiemalis

Cited by 96 publications

References 32 publications

Growth and lipase production of a psychrotrophic Acinetobacter calcoaceticus in an MSG-containing medium

Growth and lipase production of a psychrotrophic Acinetobacter calcoaceticus in an MSG-containing medium

Purification and biochemical characterization of an extracellular lipase produced by a new strain of Rhizopus sp.

Purification and Properties of Extracellular Lipases with Transesterification Activity and 1,3-Regioselectivity from Rhizomucor miehei and Rhizopus oryzae

Contact Info

Product

Resources

About