Zingibain

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Zingibain
Identifiers
EC number 3.4.22.67
CAS number 246044-91-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Zingibain, zingipain, or ginger protease (EC 3.4.22.67) is a cysteine protease enzyme found in ginger (Zingiber officinale) rhizomes.[1][2][3] It catalyses the preferential cleavage of peptides with a proline residue at the P2 position. It has two distinct forms, ginger protease I (GP-I) and ginger protease II (GP-II).[4]

Uses[edit]

Zingipain curdles milk, and has been suggested as a vegetable rennet for cheese production.[5] It is also used to make the Cantonese dish ginger milk curd.[6]

Like papain from papayas and bromelain from pineapples, it is used as a meat tenderizer.[7] However, extracted zingibain is unstable, with a half-life of about 2 days at 5°C, making it problematic for commercial applications.[8]

See also[edit]

References[edit]

  1. ^ Choi, K.H.; Laursen, R.A. (2000). "Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale". Eur. J. Biochem. 267: 1516–1526. PMID 10691991. doi:10.1046/j.1432-1327.2000.01152.x. 
  2. ^ Ohtsuki, K.; Taguchi, K.; Sato, K.; Kawabata, M. (1995). "Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing". Biochim. Biophys. Acta. 1243: 181–184. PMID 7873561. doi:10.1016/0304-4165(94)00145-n. 
  3. ^ Choi, K.H.; Laursen, R.A.; Allen, K.N. (1999). "The 2.1 Å structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale". Biochemistry. 38: 11624–11633. PMID 10512617. doi:10.1021/bi990651b. 
  4. ^ X. W. Huang; L. J. Chen; Y. B. Luo; H. Y. Guo; F. Z. Ren (2011). "Purification, characterization, and milk coagulating properties of ginger proteases". Journal of Dairy Science. 94: 2259–2269. doi:10.3168/jds.2010-4024. 
  5. ^ X.W. Huang; L.J. Chen; Y.B. Luo; H.Y. Guo; F.Z. Ren (May 2011). "Purification, characterization, and milk coagulating properties of ginger proteases". Journal of Dairy Science. 98 (5): 2259–2269. doi:10.3168/jds.2010-4024. 
  6. ^ http://blog.khymos.org/2014/02/24/ginger-milk-curd/
  7. ^ Minh Haa; Alaa El-Din A. Bekhit; Alan Carnea; David L. Hopkins (2012). "Characterisation of commercial papain, bromelain, actinidin and zingibain protease preparations and their activities toward meat proteins". Food Chemistry. 134 (1). doi:10.1016/j.foodchem.2012.02.071. 
  8. ^ Pitaya Adulyatham; Richard Owusu-Apenten (April 2005). "Stabilization and Partial Purification of a Protease from Ginger Rhizome (Zingiber offinale Roscoe)". Journal of Food Science. doi:10.1111/j.1365-2621.2005.tb07130.x. 

External links[edit]