Zingibain
Zingibain | |||||||||
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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 | ||||||||
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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
- ↑ Choi KH, Laursen RA (March 2000). "Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale". European Journal of Biochemistry. 267 (5): 1516–26. doi:10.1046/j.1432-1327.2000.01152.x. PMID 10691991.
- ↑ Ohtsuki K, Taguchi K, Sato K, Kawabata M (February 1995). "Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing". Biochimica et Biophysica Acta. 1243 (2): 181–4. doi:10.1016/0304-4165(94)00145-n. PMID 7873561.
- ↑ Choi KH, Laursen RA, Allen KN (September 1999). "The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale". Biochemistry. 38 (36): 11624–33. doi:10.1021/bi990651b. PMID 10512617.
- ↑ Huang XW, Chen LJ, Luo YB, Guo HY, Ren FZ (May 2011). "Purification, characterization, and milk coagulating properties of ginger proteases". Journal of Dairy Science. 94 (5): 2259–69. doi:10.3168/jds.2010-4024.
- ↑ Huang XW, Chen LJ, Luo YB, Guo HY, Ren FZ (May 2011). "Purification, characterization, and milk coagulating properties of ginger proteases". Journal of Dairy Science. 94 (5): 2259–69. doi:10.3168/jds.2010-4024.
- ↑ http://blog.khymos.org/2014/02/24/ginger-milk-curd/
- ↑ 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.
- ↑ 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
- Zingipain at the US National Library of Medicine Medical Subject Headings (MeSH)
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