Purification and characterization of a tuliposide-converting enzyme from bulbs of tulipa gesneriana

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Abstract

An enzyme that catalyzes the stoichiometric conversion of 6-tuliposide into tulipalin was purified and characterized from bulbs of Tulipa gesneriana. The enzyme appeared to be a dimer, the relative molecular mass (Mr) of each subunit being 34,900; it had maximum activity and stability at neutral pH and moderate temperature. The enzyme preferentially acted on such glucose esters as 6-tuliposides, and to a lesser extent on /7-nitrophenylacetate.

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Kato, Y., Shoji, K., Ubukata, M., Shigetomi, K., Sato, Y., Nakajima, N., & Ogita, S. (2009). Purification and characterization of a tuliposide-converting enzyme from bulbs of tulipa gesneriana. Bioscience, Biotechnology and Biochemistry, 73(8), 1895–1897. https://doi.org/10.1271/bbb.90226

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