Environmentally benign process for the preparation of antimicrobial α-methylene-β-hydroxy-γ-butyrolactone (tulipalin B) from tulip biomass

Nomura, Taiji; Hayashi, Emiko; Kawakami, Shohei; Ogita, Shinjiro; Kato, Yasuo

doi:10.1080/09168451.2014.946395

Cited by 14 publications

(10 citation statements)

References 42 publications

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“…The mixture was then centrifuged at 15 000 g for 10 min at 4°C, and the supernatant was diluted with water and subjected to reversed‐phase high performance liquid chromatography (HPLC) analysis according to Nomura et al . (). To examine the localization of Pos/Pa, the stamens were divided into their constituent parts as described above in ‘Crude enzyme extraction’.…”

Section: Methodsmentioning

confidence: 97%

“…PosA, PosB and PaB were prepared as described previously (Nomura et al ., , ). PaA (α‐methylene‐γ‐butyrolactone) was purchased from Tokyo Chemical Industry (http://www.tcichemicals.com/).…”

Section: Methodsmentioning

confidence: 99%

“…Although very little information is known about the biosynthetic pathways of Pos, the biochemical basis for the formation of Pa from Pos is currently being researched in our laboratory. In tulip, large amounts of Pos accumulate in every tissue, although the amount and the type of the major Pos species can vary considerably depending on the tissue and the developmental stage (Christensen and Kristiansen, ; Shoji et al ., ; Nomura et al ., ). In contrast, biologically active PaA and PaB are far less abundant and sometimes barely detectable (Beijersbergen and Lemmers, ; Christensen and Kristiansen, ).…”

Section: Introductionmentioning

confidence: 97%

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Molecular identification of tuliposide B‐converting enzyme: a lactone‐forming carboxylesterase from the pollen of tulip

et al. 2015

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SUMMARY6-Tuliposides A (PosA) and B (PosB), which are the major secondary metabolites in tulip (Tulipa gesneriana), are enzymatically converted to the antimicrobial lactonized aglycons, tulipalins A (PaA) and B (PaB), respectively. We recently identified a PosA-converting enzyme (TCEA) as the first reported member of the lactone-forming carboxylesterases. Herein, we describe the identification of another lactone-forming carboxylesterase, PosB-converting enzyme (TCEB), which preferentially reacts with PosB to give PaB. This enzyme was isolated from tulip pollen, which showed high PosB-converting activity. Purified TCEB exhibited greater activity towards PosB than PosA, which was contrary to that of the TCEA. Novel cDNA (TgTCEB1) encoding the TCEB was isolated from tulip pollen. TgTCEB1 belonged to the carboxylesterase family and was approximately 50% identical to the TgTCEA polypeptides. Functional characterization of the recombinant enzyme verified that TgTCEB1 catalyzed the conversion of PosB to PaB with an activity comparable with the native TCEB. RT-qPCR analysis of each part of plant revealed that TgTCEB1 transcripts were limited almost exclusively to the pollen. Furthermore, the immunostaining of the anther cross-section using anti-TgTCEB1 polyclonal antibody verified that TgTCEB1 was specifically expressed in the pollen grains, but not in the anther cells. N-terminal transit peptide of TgTCEB1 was shown to function as plastid-targeted signal. Taken together, these results indicate that mature TgTCEB1 is specifically localized in plastids of pollen grains. Interestingly, PosB, the substrate of TgTCEB1, accumulated on the pollen surface, but not in the intracellular spaces of pollen grains.

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Section: Methodsmentioning

confidence: 97%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

See 1 more Smart Citation

Molecular identification of tuliposide B‐converting enzyme: a lactone‐forming carboxylesterase from the pollen of tulip

et al. 2015

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“…1). [15][16][17][18][19][20][21] Although all parts of the tulip show TCE activity, the activity ratios toward PosA and PosB in crude extracts differ from tissue to tissue and correlate well with the ratios of PosA to PosB in each tissue. This was demonstrated to be attributable to the presence of two distinct types of TCE, a PosA-converting enzyme (TCEA) and a PosB-converting enzyme (TCEB), with the former preferentially catalyzing PosA conversion to PaA and the latter PosB conversion to PaB (Fig.…”

mentioning

confidence: 89%

“…PosA, PosB, and PaB were prepared as described previously. 17,19) PaA (α-methylene-γbutyrolactone) was purchased from Tokyo Chemical Industry.…”

Section: Chemicalsmentioning

confidence: 99%

Molecular diversity of tuliposide B-converting enzyme in tulip (Tulipa gesneriana): identification of the root-specific isozyme

Nomura

Ueno

Ogita

et al. 2017

Bioscience, Biotechnology, and Biochemistry

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6-Tuliposide B (PosB) is a glucose ester accumulated in tulip (Tulipa gesneriana) as a major secondary metabolite. PosB serves as the precursor of the antimicrobial lactone tulipalin B (PaB), which is formed by PosB-converting enzyme (TCEB). The gene TgTCEB1, encoding a TCEB, is transcribed in tulip pollen but scarcely transcribed in other tissues (e.g. roots) even though those tissues show high TCEB activity. This led to the prediction of the presence of a TCEB isozyme with distinct tissue specificity. Herein, we describe the identification of the TgTCEB-R gene from roots via native enzyme purification; this gene is a paralog of TgTCEB1. Recombinant enzyme characterization verified that TgTCEB-R encodes a TCEB. Moreover, TgTCEB-R was localized in tulip plastids, as found for pollen TgTCEB1. TgTCEB-R is transcribed almost exclusively in roots, indicating a tissue preference for the transcription of TCEB isozyme genes.

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Production and Polymerization of Biobased Acrylates and Analogs

Fouilloux

Thomas

2021

Macromol. Rapid Commun.

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To prepare biobased polymers, particular attention must be paid to the obtention of the monomers from which they are derived. (Meth)acrylates and their analogs constitute such a class of monomers that have been extensively studied due to the wide range of polymers accessible from them. This review therefore aims to highlight the progresses made in the production and polymerization of (meth)acrylates and their analogs. Acrylic acid production from biomass is close to commercialization, as three different high‐potential intermediates are identified: glycerol, lactic acid, and 3‐hydroxypropionic acid. Biobased methacrylic acid is less common, but several promising options are available, such as the decarboxylation of itaconic acid or the dehydration of 2‐hydroxyisobutyric acid. Itaconic acid is also a vinylic monomer of great interest, and polymers derived from it have already found commercial applications. Methylene butyrolactones are promising monomers, obtained from bioresources via three different intermediates: levulinic, succinic, or itaconic acid. Although expensive, methylene butyrolactones have a strong potential for the production of high‐performance polymers. Finally, β‐substituted acrylic monomers, such as cinnamic, fumaric, muconic, or crotonic acid, are also examined, as they provide an original access to biobased materials from various renewable raw materials, such as protein waste, lignin, or wastewater.

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Environmentally benign process for the preparation of antimicrobial α-methylene-β-hydroxy-γ-butyrolactone (tulipalin B) from tulip biomass

Cited by 14 publications

References 42 publications

Molecular identification of tuliposide B‐converting enzyme: a lactone‐forming carboxylesterase from the pollen of tulip

Molecular identification of tuliposide B‐converting enzyme: a lactone‐forming carboxylesterase from the pollen of tulip

Molecular diversity of tuliposide B-converting enzyme in tulip (Tulipa gesneriana): identification of the root-specific isozyme

Production and Polymerization of Biobased Acrylates and Analogs

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