PRODUCT LITERATURE

Substrate Profiling of Cysteine Protease from Zingiber officinale

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Plants have different types of proteases and four types of cysteine protease have been isolated from ginger (GPI, II, 2, and 3). This study analyzed the structure and cleavage specificity of a newly isolated protease (GPii) from Zingiber officinale to evaluate the general properties of this protease. GPs were purified using anion exchange chromatography. Three GPs were purified and shown to be similar to the three reported types of GPs (GPII, 2, and 3). This is the first study in which one cultivar contains three types of GPs. GPii was sequenced, and revealed to carry two substitutions compared with GPII. The cleavage specificity of GPii was analyzed using protein substrates. GPii showed cleavage specificity for Ser, Gly, Lys, and Arg at first position; Ala, Pro, Ile, and Tyr at the second position; and Gly at the third position of the N-terminal side. Further, GPii could not cleave the insoluble substrate

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: .,

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Language

English

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NONE

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Subject(s)

HerbaVomitz

Specific Detail Info

FOOD BIOTECHNOLOGY 2018, VOL. 32, NO. 2, 148–161

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