Identification of Rice β-Glucosidase with High Hydrolytic Activity towards Salicylic Acid β-D-Glucoside

Himeno, Nami; Saburi, Wataru; Wakuta, Shinji; Takeda, Ryosuke; Matsuura, Hideyuki; Nabeta, Kensuke; Sansenya, Sompong; Ketudat Cairns, James R.; Mori, Haruhide; Imai, Ryozo; Matsui, Hirokazu

Identification of Rice β-Glucosidase with High Hydrolytic Activity towards Salicylic Acid β-D-Glucoside

Himeno, Nami; Saburi, Wataru; Wakuta, Shinji et al.

Bioscience, Biotechnology, and Biochemistry, 2013, 77(5), 934-939

Permalink : https://hdl.handle.net/2115/67543

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アクセス権	open access
URI	https://hdl.handle.net/2115/67543
タイトル	Identification of Rice β-Glucosidase with High Hydrolytic Activity towards Salicylic Acid β-D-Glucoside
著者	Himeno, Nami ; Saburi, Wataru ; Wakuta, Shinji ; Takeda, Ryosuke ; Matsuura, Hideyuki ; Nabeta, Kensuke ; Sansenya, Sompong ; Ketudat Cairns, James R. ; Mori, Haruhide ; Imai, Ryozo ; Matsui, Hirokazu
著者名 Himeno, Nami
e-Rad_Researcher 00598089 著者名 Saburi, Wataru
著者名 Wakuta, Shinji
著者名 Takeda, Ryosuke
e-Rad_Researcher 20344492 著者名 Matsuura, Hideyuki
著者名 Nabeta, Kensuke
著者名 Sansenya, Sompong
著者名 Ketudat Cairns, James R.
e-Rad_Researcher 80241363 著者名 Mori, Haruhide
著者名 Imai, Ryozo
e-Rad_Researcher 90109504 著者名 Matsui, Hirokazu
言語	英語
キーワード	β-glucosidase
	rice
	tuberonic acid
	salicylic acid
	substrate specificity
発行日	2013-05
出版者	Taylor & Francis
収録物名	Bioscience, Biotechnology, and Biochemistry
巻(号)	77(5)
ページ	934-939
抄録	β-Glucosidases (EC 3.2.1.21) split β-glucosidic linkages at the non-reducing end of glucosides and oligosaccharides to release β-D-glucose. One of the important functions of plant β-glucosidase is deglucosylation of inactive glucosides of phytohormones to regulate levels of active hormones. Tuberonic acid is a jasmonate-related compound that shows tuber-inducing activity in the potato. We have identified two enzymes, OsTAGG1 and OsTAGG2, that have hydrolytic activity towards tuberonic acid β-D-glucoside in rice (Oryza sativa L.). The expression of OsTAGG2 is upregulated by wounding and by methyl jasmonate, suggesting that this isozyme is involved in responses to biotic stresses and wounding, but the physiological substrate of OsTAGG2 remains ambiguous. In this study, we produced recombinant OsTAGG2 in Pichia pastoris (rOsTAGG2P), and investigated its substrate specificity in detail. From 1 L of culture medium, 2.1 mg of purified recombinant enzyme was obtained by ammonium sulfate precipitation and Ni-chelating column chromatography. The specific activity of rOsTAGG2P (182 U/mg) was close to that of the native enzyme (171 U/mg), unlike recombinant OsTAGG2 produced in Escherichia coli, which had approximately 3-fold lower specific activity than the native enzyme. The optimum pH and temperature for rOsTAGG2P were pH 3.4 and 60 °C. After pH and heat treatments, the enzyme retained its original activity in a pH range of 3.4-9.8 and below 55 °C. Native OsTAGG2 and rOsTAGG2P showed 4.5-4.7-fold higher activities towards salicylic acid β-D-glucoside, an inactive storage-form of salicylic acid, than towards tuberonic acid β-D-glucoside (TAG), although OsTAGG2 was originally isolated from rice based on TAG-hydrolytic activity.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience, biotechnology, and biochemistry on 2013 May, available online: http://wwww.tandfonline.com/10.1271/bbb.120889
PISSN	0916-8451
EISSN	1347-6947
NCID	AA10824164
関連情報	PMID 23649259
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1271/bbb.120889