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The pineapple is a tropical plant with an edible fruit; it is the most economically significant plant in the family Bromeliaceae.
In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.
Bromelain is an enzyme extract derived from the stems of pineapples, although it exists in all parts of the fresh pineapple. The extract has a history of folk medicine use. As an ingredient, it is used in cosmetics, as a topical medication, and as a meat tenderizer.
Papain, also known as papaya proteinase I, is a cysteine protease enzyme present in papaya and mountain papaya. It is the namesake member of the papain-like protease family.
Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad.
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
Ficain also known as ficin, debricin, or higueroxyl delabarre is a proteolytic enzyme extracted from the latex sap from the stems, leaves, and unripe fruit of the American wild fig tree Ficus insipida.
Actinidain is a type of cysteine protease enzyme found in fruits including kiwifruit, pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases.
Cathepsin E is an enzyme that in humans is encoded by the CTSE gene. The enzyme is also known as slow-moving proteinase, erythrocyte membrane aspartic proteinase, SMP, EMAP, non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme.
FA2 or variant, may refer to:
Nepenthesin is an aspartic protease of plant origin that has so far been identified in the pitcher secretions of Nepenthes and in the leaves of Drosera peltata. It is similar to pepsin, but differs in that it also cleaves on either side of Asp residues and at Lys┼Arg. While more pH and temperature stable than porcine pepsin A, it is considerably less stable in urea or guanidine hydrochloride. It is the only known protein with such a stability profile.
Cucumisin is an enzyme. This enzyme catalyzes hydrolysis of a wide range of proteins. It has been identified as an allergen in humans.
Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Ananain is an enzyme. This enzyme catalyses the following chemical reaction
Zingibain, zingipain, or ginger protease is a cysteine protease enzyme found in ginger rhizomes. 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).
Penicillopepsin is an enzyme. This enzyme catalyses the following chemical reaction
Endothiapepsin is an enzyme. This enzyme catalyses the following chemical reaction
Phytepsin is an enzyme. This enzyme catalyses the following chemical reaction
Serralysin is an enzyme. This enzyme catalyses the following chemical reaction
Bromelain, a concentrate of proteolytic enzymes from the pineapple plant, is used in medicine. It is approved in the European Union for the debridement of severe burn wounds under the brand name Nexobrid. It was developed by MediWound.
References
- ↑ Sasaki M, Kato T, Iida S (September 1973). "Antigenic determinant common to four kinds of thiol proteases of plant origin". Journal of Biochemistry. 74 (3): 635–7. PMID 4127920.
- ↑ Yamada F, Takahashi N, Murachi T (June 1976). "Purification and characterization of a proteinase from pineapple fruit, fruit bromelain FA2". Journal of Biochemistry. 79 (6): 1223–34. PMID 956152.
- ↑ Ota S, Muta E, Katahira Y, Okamoto Y (July 1985). "Reinvestigation of fractionation and some properties of the proteolytically active components of stem and fruit bromelains". Journal of Biochemistry. 98 (1): 219–28. PMID 4044551.
- ↑ Rowan AD, Buttle DJ, Barrett AJ (March 1990). "The cysteine proteinases of the pineapple plant". The Biochemical Journal. 266 (3): 869–75. PMC 1131219 . PMID 2327970.
