Differential Proteomic Analysis of Secreted Proteins from Cutinase-producing Bacillus sp. SB-007

Ban, Yeon Hee; Jeon, Mi Ri; Yoon, Ji Hee; Park, Jaemin; Um, Hyun Ju; Kim, Dae Soon; Jung, Seung Ki; Kim, Keun Young; Lee, Jee Won; Min, Ji Ho; Kim, Yang Hoon

doi:10.5423/ppj.2008.24.2.191

Cited by 3 publications

(5 citation statements)

References 44 publications

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“…In contrast to Rhodanobacter , which expanded or maintained its population during the entire incubation period, Myxococcus ceased to grow after 10 d. However, only a small fraction of the secretome appeared to be dedicated to lipid metabolism in both bacteria. A similar situation was observed when S. scabiei was grown on suberin (26) or when Bacillus was grown on cutin (2), a polymer bearing structural similarities to suberin. The analysis of Myxococcus and Rhodanobacter proteomes revealed that both bacteria may possess not only the tools to depolymerize the aliphatic fraction of suberin, but also the ability to bind suberin and assimilate fatty acids (Table 4).…”

Section: Discussionsupporting

confidence: 52%

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Proteome Analyses of Soil Bacteria Grown in the Presence of Potato Suberin, a Recalcitrant Biopolymer

et al. 2016

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Suberin is a complex lipidic plant polymer found in various tissues including the potato periderm. The biological degradation of suberin is attributed to fungi. Soil samples from a potato field were used to inoculate a culture medium containing suberin as the carbon source, and a metaproteomic approach was used to identify bacteria that developed in the presence of suberin over a 60-d incubation period. The normalized spectral counts of predicted extracellular proteins produced by the soil bacterial community markedly decreased from day 5 to day 20 and then slowly increased, revealing a succession of bacteria. The population of fast-growing pseudomonads declined and was replaced by species with the ability to develop in the presence of suberin. The recalcitrance of suberin was demonstrated by the emergence of auxotrophic bacteria such as Oscillatoria on the last days of the assay. Nevertheless, two putative lipases from Rhodanobacter thiooxydans (I4WGM2) and Myxococcus xanthus (Q1CWS1) were detected in the culture supernatants, suggesting that at least some bacterial species degrade suberin. When grown in suberin-containing medium, R. thiooxydans strain LCS2 and M. xanthus strain DK 1622 both produced three lipases, including I4WGM2 and Q1CWS1. These strains also produced other proteins linked to lipid metabolism, including fatty acid and lipid transporters and β-oxidation enzymes, suggesting that they participate in the degradation of suberin. However, only the R. thiooxydans strain appeared to retrieve sufficient carbon and energy from this recalcitrant polymer in order to maintain its population over an extended period of time.

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Section: Discussionsupporting

confidence: 52%

“…Nevertheless, bacteria exhibiting cutinase activity have been isolated, including members of the genera Bacillus (2), Pseudomonas (48), and Thermomonospora (12). Bacterial cutinases may also be active on suberin because cutinase production is induced by suberin in Thermomonospora (12).…”

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confidence: 99%

Proteome Analyses of Soil Bacteria Grown in the Presence of Potato Suberin, a Recalcitrant Biopolymer

et al. 2016

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“…Several studies have been carried out on PCL biodegradation in natural environments [1, 8 -10] as well as in the presence of certain microorganisms, such as bacteria (Bacillus sp., Alcaligenes faecalis, and Acinetobacter calcoaceticus var. lwoffi) [11,12], fungi (Aureobasidium pullulans; Penicillium sp., Aspergillus fischeri, A. flavus, Chaetomium globosum, and a Fusarium sp.) [13,14], and yeasts (Pseudozyma jejuensis, Candida cylindracea and Cryptococcus laurentii) [8, 15 -18].…”

Section: Introduction *mentioning

confidence: 99%

Immobilization of cross‐linked lipase aggregates onto magnetic beads for enzymatic degradation of polycaprolactone

Kim

Park

et al. 2010

J. Basic Microbiol.

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Candida rugosa lipase was immobilized on amino-functionalized magnetic supports via cross-linked enzyme aggregates (CLEA) and used to enhance the enzymatic degradation of polycaprolactone (PCL). The maximum amounts of lipase immobilized on the magnetic beads using glutaraldehyde as a coupling agent were determined to be 33.7 mg/g of beads with an 81% recovery of activity after immobilization. Compared to the free enzyme, the immobilized lipase showed the optimum pH at 1 unit higher (pH 8.0) and also retained its enzymatic activity at higher temperatures. There was 62.9% retention of lipase activity after 30 consecutive reuses, indicating its stability and reusability in aqueous media. Moreover, the immobilized lipase maintained more than 80% of its initial activity during 30 days storage period, while the free lipase lost all under same condition. In addition, the immobilized lipase showed a more than 6-fold increase in biodegradability over the free lipase when the immobilized lipase was used to degrade PCL in a batch system. Higher thermal and storage stability, as well as good durability after repeated use of the immobilized lipase CLEA, highlights its potential applicability as large scale continuous systems for the enzymatic degradation of PCL.

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“…The DIDP-degrading bacteria, Bacillus sp. SB-007 [22], was cultivated on a mineral salt medium (MSM) containing (mg 1 -1 O 0.60; supplemented with 50 -500 mg 1 -1 of DIDP (> 99%, Sigma-Aldrich, USA) as the sole source of carbon and energy in a 250 ml flask and continued for 3 -10 d in a dark shaking incubator (200 rpm). The specific growth rate was calculated from three consecutive OD 600 measurements from Δln OD 600 /Δt, where t is time.…”

Section: Growth Condition Of Bacillus Sp Sb-007mentioning

confidence: 99%

“…SB-007 were examined under the following conditions: pH's of 5.0, 5.5, 6.0, 6.5, 7.0, 7.5, and 8.0 at 30 °C; and temperatures of 20,22,24,26,28,30,32,34,36,38, and 40 °C at pH 7.0. The pH and cell growth were measured using a pH meter (Beckman, USA) and spectrophotometer (Boeco, Germany) at 600 nm, respectively.…”

Section: Degradation Of Didp By Bacillus Sp Sb-007mentioning

confidence: 99%

Biodegradation of diisodecyl phthalate (DIDP) by Bacillus sp. SB‐007

Park

Kim

Yoon

et al. 2009

J. Basic Microbiol.

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In this study, diisodecyl phthalate (DIDP) was efficiently degraded by Bacillus sp. SB-007. The optimal conditions for DIDP (100 mg l(-1)) degradation by Bacillus sp. SB-007 in a mineral salts medium were found to be pH 7.0 at 30 degrees C, stirring at 200 rpm. The specific rate of DIDP degradation was found to be concentration dependent with a maximum of 4.87 mg DIDP l(-1) h(-1). DIDP was transformed rapidly by Bacillus sp. SB-007 with the formation of monoisodecyl phthalate and phthalic acid, which subsequently degraded further. These results highlight the potential of this bacterium for removing DIDP contaminated waste in the environment.

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Differential Proteomic Analysis of Secreted Proteins from Cutinase-producing Bacillus sp. SB-007

Cited by 3 publications

References 44 publications

Proteome Analyses of Soil Bacteria Grown in the Presence of Potato Suberin, a Recalcitrant Biopolymer

Proteome Analyses of Soil Bacteria Grown in the Presence of Potato Suberin, a Recalcitrant Biopolymer

Immobilization of cross‐linked lipase aggregates onto magnetic beads for enzymatic degradation of polycaprolactone

Biodegradation of diisodecyl phthalate (DIDP) by Bacillus sp. SB‐007

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