Zingibain

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

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

References

  1. ↑ Choi, K.H. and 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. doi:10.1046/j.1432-1327.2000.01152.x. PMID 10691991.
  2. ↑ Ohtsuki, K., Taguchi, K., Sato, K. and Kawabata, M. (1995). "Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing". Biochim. Biophys. Acta 1243: 181–184. doi:10.1016/0304-4165(94)00145-n. PMID 7873561.
  3. ↑ Choi, K.H., Laursen, R.A. and 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. doi:10.1021/bi990651b. PMID 10512617.
  4. ↑ X. W. Huang, L. J. Chen, Y. B. Luo, H. Y. Guo, and 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, and 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, and 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

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