Molecular Diversity of Tuliposide A-Converting Enzyme in the Tulip

Nomura, Taiji; Tsuchigami, Aya; Ogita, Shinjiro; Kato, Yasuo

doi:10.1271/bbb.130021

Cited by 11 publications

(23 citation statements)

References 29 publications

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“…20) Although the TCE expressed predominantly in bulbs is TCEA, the bulb crude extracts have PosB-converting activity because the TCEA also has PosB-converting activity, although it is approximately 10 times lower than the PosA-converting activity. [19][20][21] Nevertheless, the PosBconverting activity in the bulb crude extracts is higher than that in the crude extracts from other tissues because TCE activities are very high in bulbs. 20) Thus, bulbs are suitable as a source of TCE for PaB preparation.…”

Section: Preparation Of Flower Extracts As a Substrate For The Enzymementioning

confidence: 94%

“…In all cultivars tested, TCE activities were detected, and the PosA-converting activity was higher than the PosB-converting activity (Table S2), which was consistent with our previous observation for a single cultivar ("Murasakizuisho"). [19][20][21]35) On average, specific activities for PosA and PosB were 26.9 ± 2.55 U/mg protein and 4.42 ± 0.618 U/mg protein (mean ± SE), respectively. Although the PosB-converting activity of the cultivar "Rosy Wings" was considerably lower than those of other cultivars, considering that the bulbs of various cultivars are used in bulk as enzyme source, the presence of such cultivar with a low frequency does not make a severe impact on the PosB-converting activity of the immobilized enzyme.…”

Section: Preparation Of Flower Extracts As a Substrate For The Enzymementioning

confidence: 99%

“…20,21) The establishment of a heterologous expression system in E. coli permits the use of recombinant enzyme instead of the natural bulb enzyme. The use of recombinant enzyme would not be preferable for certain uses of PaB, e.g.…”

Section: Purification Of Pab From the Enzyme Reaction Mixturementioning

confidence: 99%

“…1). [19][20][21] PosA and PosB are converted to the corresponding Pa by PosA-converting enzyme (TCEA) and PosB-converting enzyme (TCEB), respectively. Genes for TCEA (EC 4.2.99.22) have been isolated from petals and bulbs, 20,21) and recently, we have identified the gene for TCEB, the details of which will be published elsewhere in due course.…”

mentioning

confidence: 99%

“…Although its PosB-converting activity is approximately one-tenth of its PosA-converting activity, the PosB-converting activity in the bulb crude extracts is higher than that in the crude extracts from other tissues. 20,21) Thus, the bulbs remain a viable source of TCE.…”

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confidence: 99%

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

Nomura

Hayashi

Kawakami

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Tulipalin B (α-methylene-β-hydroxy-γ-butyrolactone, PaB) is an antimicrobial natural product occurring in tulip (Tulipa gesneriana). PaB is directly formed from the precursor glucose ester 6-tuliposide B (PosB) by endogenous Pos-converting enzyme (TCE). Despite the potential usefulness of antibacterial PaB in various industrial applications, lack of facile synthetic schemes hampers its practical use. Herein, we describe an environmentally benign and facile process for the preparation of PaB using tulip biomass materials based on one-step enzyme reaction catalyzed by TCE without the use of petroleum-derived solvents. By screening 115 tulip cultivars, we found three elite cultivars, which accumulated PosB almost exclusively in flower tissues. The flower extracts with aqueous ethanol were partially purified with activated charcoal and subjected to the enzyme reaction with reusable immobilized TCE prepared from bulb crude extracts. The reaction was completed in a few hours at room temperature, and PaB was purified with activated charcoal and ethanol in a batch-wise manner.

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