Catalytic properties of a lipase from Photobacterium lipolyticum for biodiesel production containing a high methanol concentration

Yang, Kyung Seok; Sohn, Jung‐Hoon; Kim, Hyung Kwoun

doi:10.1016/j.jbiosc.2009.01.009

Cited by 65 publications

(35 citation statements)

References 26 publications

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“…This tendency is also comparable with RL74 [15]. Similar pattern of the stability and activity enhancement was reported from Photobacterium lipolyticum and other commercial lipases [18]. In 30 min incubation, lipases from Pseudomonas cepacia, Candida rugosa and Candida antarctica were reported to be inactivated even by 10% methanol [18]; therefore, LP28 has better methanol tolerance than those lipases.…”

Section: Effect Of Methanol and Various Effectorssupporting

confidence: 80%

“…Similar pattern of the stability and activity enhancement was reported from Photobacterium lipolyticum and other commercial lipases [18]. In 30 min incubation, lipases from Pseudomonas cepacia, Candida rugosa and Candida antarctica were reported to be inactivated even by 10% methanol [18]; therefore, LP28 has better methanol tolerance than those lipases. Biodiesel production is generally carried out by methylation of various oils; therefore, a latent enzyme must be stable in methanol.…”

Section: Effect Of Methanol and Various Effectorssupporting

confidence: 71%

“…Potential of LP28 in biodiesel production Biodiesel production was carried out according to methods described elsewhere [18] with minor modifications [15]. In Brief, lipase sample (200 U, pNPP spectrophotometric assay) was added to the mixture of palm oil or soybean oil (7.89 mL) and methanol (0.99 mL) kept in a screw-capped glass vial (20 mL).…”

Section: Determination Of Kinetic Parametersmentioning

confidence: 99%

See 2 more Smart Citations

A novel cold-adapted lipase, LP28, from a mesophilic Streptomyces strain

Simkhada

Yoo²,

Cho

et al. 2011

Bioprocess Biosyst Eng

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Fossil fuel is limited but its usage has been growing rapidly, thus the fuel is predicted to be completely running out and causing an unbearable global energy crisis in the near future. To solve this potential crisis, incorporating with increasing environmental concerns, significant attentions have been given to biofuel production in the recent years. With the aim of isolating a microbial biocatalyst with potential application in the field of biofuel, a lipase from Streptomyces sp. CS628, LP28, was purified using hydroxyapatite column chromatography followed by a gel filtration. Molecular weight of LP28 was estimated to be 32,400 Da by SDS-PAGE. The activity was the highest at 30 °C and pH 8.0 and was stable at pH 6.0-8.0 and below 25 °C. The enzyme preferentially hydrolyzed p-nitrophenyl decanoate (C10), a medium chain substrate. Furthermore, LP28 non-specifically hydrolyzed triolein releasing both 1,2- and 1,3-diolein. More importantly, LP28 manifestly catalyzed biodiesel production using palm oil and methanol; therefore, it can be a potential candidate in the field of biofuel.

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Section: Effect Of Methanol and Various Effectorssupporting

confidence: 80%

Section: Effect Of Methanol and Various Effectorssupporting

confidence: 71%

Section: Determination Of Kinetic Parametersmentioning

confidence: 99%

See 1 more Smart Citation

A novel cold-adapted lipase, LP28, from a mesophilic Streptomyces strain

Simkhada

Yoo²,

Cho

et al. 2011

Bioprocess Biosyst Eng

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show abstract

“…Addition of 70% methanol showed maximum lipolytic activity while 2-propanol showed the minimum activity by lipase from Microbacterium sp isolated from marble mining rock, New Delhi [5]. Methanol also improved the stability of lipase sourced from Photobacterium lipolyticum [69]. The reason maybe be attributed to the hydrophilicty or reduced bulkiness of methanol which imposed flexible attributes on the lid of the enzymes.…”

Section: Effect Of Solventsmentioning

confidence: 98%

Microbial Lipases: A Prospect for Biotechnological Industrial Catalysis for Green Products: A Review

Ugo¹,

Amara²,

Cn³

et al. 2017

Ferment Technol

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Microbes have been novel hosts for suitable industrial enzymes including lipases. With the rapid increase in biotechnological industries, there is need for improvement of bioproducts, enhance environmental safety and product yield. Microbes are qualified biological arsenal for the achievement of the above mentioned targets in the industrial sectors. Lipases as versatile biological catalyst has given a promising prospect in meeting the needs for most industries such as biodiesel, foods and drinks, leather, textile, detergents, pharmaceuticals and medicals. Catalytic importance of lipases includes hydrolysis, esterification and transesterification. Each of the mentioned reactions has their industrial applications. Lipases exhibit various properties, with respect to its source. Immobilization has made the use of microbial lipases attain its optimum performance and hence suitable for various reaction and the need to add flavor to the immobilization processes.

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“…Biodiesel production was carried out according to previously described method [11] with modifications [6]. A screw capped glass vial with 20 mL capacity contained soybean oil (7.89 mL) and methanol (0.99 mL) with lipase sample (300 U).…”

Section: Application Study In Biodiesel Productionmentioning

confidence: 99%

A neutral lipase applicable in biodiesel production from a newly isolated Streptomyces sp. CS326

Cho

Park

Simkhada

et al. 2011

Bioprocess Biosyst Eng

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In an attempt to isolate a biocatalyst able to catalyze biodiesel production from microbial source, Streptomyces sp. CS326 was screened from hundreds of soil isolates collected from various parts of Korea. In 16S rRNA sequence analysis, the strain showed high degree of similarity with Streptomyces xanthocidicus (99.79%); therefore, it is classified as Streptomyces sp. CS326. An extracellular lipase produced by the strain (LP326) was purified using a single step gel permeation chromatography on Sepharose CL-6B. Molecular weight of LP326 was estimated to be 17,000 Da by SDS-PAGE. The activity was optimum at 40 °C and pH 7.0 and was stable at pH 5.0-8.0 and below 50 °C. It preferred p-nitrophenyl palmitate (C16), a long chain substrate; and K (m) and V (max) for the substrate were determined to be 0.24 mM and 4.6 mM/min mg, respectively. First 10 N-terminal amino acid sequences were APDLVALQSE, which are different from so far reported lipases. LP326 catalyzed biodiesel production using methanol and various oils; therefore, the enzyme can be applicable in the field of biofuel.

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Catalytic properties of a lipase from Photobacterium lipolyticum for biodiesel production containing a high methanol concentration

Cited by 65 publications

References 26 publications

A novel cold-adapted lipase, LP28, from a mesophilic Streptomyces strain

A novel cold-adapted lipase, LP28, from a mesophilic Streptomyces strain

Microbial Lipases: A Prospect for Biotechnological Industrial Catalysis for Green Products: A Review

A neutral lipase applicable in biodiesel production from a newly isolated Streptomyces sp. CS326

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