Substrate Profiling of Cysteine Protease from Zingiber officinale

ABSTRACT

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.

KEYWORDS:

• Zingiber officinale
• ginger rhizome
• cysteine protease
• GP
• amino acid sequence
• cleavage specificity

Conflict of interest

The authors declare that we have no conflicts of interest. This article does not contain any studies with human participants or animals performed by any of the authors.