Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases

Lee, Karen L.; Albee, Karen; Bernasconi, Richard; Edmunds, Tim

doi:10.1042/bj3270199

Cited by 60 publications

(44 citation statements)

References 13 publications

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“…In addition, numerous, different protein fractions were obtained by means of various biochemical methods [SDS-polyacrylamide gel electrophoresis (PAGE), isoelectric focusing (IEF), multicathodal-PAGE]. Among the basic proteinases, one fraction (F9, ananain) reveals the highest specific proteinase activity, is not glycosylated and has a molecular mass of 23,427 Da [6,8,9]. The enzymatic activities comprise a wide spectrum with pH optima between 5.5 and 8.0 [10].…”

Section: Biochemistry Of Bromelainmentioning

confidence: 99%

Bromelain: biochemistry, pharmacology and medical use

Maurer¹

2001

CMLS, Cell. Mol. Life Sci.

566

429

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Bromelain is a crude extract from the pineapple that contains, among other components, various closely related proteinases, demonstrating, in vitro and in vivo, antiedematous, antiinflammatory, antithrombotic and fibrinolytic activities. The active factors involved are biochemically characterized only in part. Due to its efficacy after oral administration, its safety and lack of undesired side effects, bromelain has earned growing acceptance and compliance among patients as a phytotherapeutical drug. A wide range of therapeutic benefits has been claimed for bromelain, such as reversible inhibition of platelet aggregation, angina pectoris, bronchitis, sinusitis, surgical traumas, thrombophlebitis, pyelonephritis and enhanced absorption of drugs, particularly of antibiotics. Biochemical experiments indicate that these pharmacological properties depend on the proteolytic activity only partly, suggesting the presence of nonprotein factors in bromelain. Recent results from preclinical and pharmacological studies recommend bromelain as an orally given drug for complementary tumor therapy: bromelain acts as an immunomodulator by raising the impaired immunocytotoxicity of monocytes against tumor cells from patients and by inducing the production of distinct cytokines such as tumor necrosis factor-a, interleukin (Il)-1beta, Il-6, and Il-8. In a recent clinical study with mammary tumor patients, these findings could be partially confirmed. Especially promising are reports on animal experiments claiming an antimetastatic efficacy and inhibition of metastasis-associated platelet aggregation as well as inhibition of growth and invasiveness of tumor cells. Apparently, the antiinvasive activity does not depend on the proteolytic activity. This is also true for bromelain effects on the modulation of immune functions, its potential to eliminate burn debris and to accelerate wound healing. Whether bromelain will gain wide acceptance as a drug that inhibits platelet aggregation, is antimetastatic and facilitates skin debridement, among other indications, will be determined by further clinical trials. The claim that bromelain cannot be effective after oral administration is definitely refuted at this time.

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Section: Biochemistry Of Bromelainmentioning

confidence: 99%

Bromelain: biochemistry, pharmacology and medical use

Maurer¹

2001

CMLS, Cell. Mol. Life Sci.

566

429

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“…It appeared to differ significantly in the number of lysine, arginine, and isoleucine compared to ananain and comosain (Napper et al 1994). Ananain possesses more hydrophobicity in the region near histidine-157 and sequence insert between 170 and 174 residues which cannot be found in stem bromelain (Lee et al 1997). Stem bromelain also contains four hexosamines, and 2.1 % carbohydrate, meaning it is a glycoprotein (Murachi 1964;Murachi et al 1964).…”

Section: Introductionmentioning

confidence: 99%

Bromelain: an overview of industrial application and purification strategies

Arshad

Amid

Yusof

et al. 2014

Appl Microbiol Biotechnol

169

134

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This review highlights the use of bromelain in various applications with up-to-date literature on the purification of bromelain from pineapple fruit and waste such as peel, core, crown, and leaves. Bromelain, a cysteine protease, has been exploited commercially in many applications in the food, beverage, tenderization, cosmetic, pharmaceutical, and textile industries. Researchers worldwide have been directing their interest to purification strategies by applying conventional and modern approaches, such as manipulating the pH, affinity, hydrophobicity, and temperature conditions in accord with the unique properties of bromelain. The amount of downstream processing will depend on its intended application in industries. The breakthrough of recombinant DNA technology has facilitated the large-scale production and purification of recombinant bromelain for novel applications in the future.

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“…One of the best known plant proteases, bromelain, is obtained from pineapple (Ananas comosus, Bromeliaceae), containing at least four peptidases (stem bromelain, fruit bromelain, ananain, and comosain) that have already been purified and characterized [7,8].…”

Section: Introductionmentioning

confidence: 99%

Cloning, Sequencing, and Identification Using Proteomic Tools of a Protease from Bromelia hieronymi Mez

Bruno

Trejo

Avilés

et al. 2011

Appl Biochem Biotechnol

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Fruits of Bromelia hieronymi, a tropical South American plant, possess a high content of peptidases with potential biotechnological uses. Total RNA was extracted from unripe fruits and peptidase cDNA was obtained by 3'RACE-PCR. The consensus sequence of the cysteine peptidase cDNA contained 875 bp, the 690 first ones codifying for a hypothetical polypeptide chain of the mature peptidase, named Bh-CP1 (molecular mass 24.773 kDa, pI 8.6, extinction molar coefficient 58,705 M(-1) cm(-1)). Bh-CP1 sequence shows a high percentage of identity with those of other cysteine plant proteases. The presence of highly preserved residues is observed, like those forming the catalytic site (Gln19, Cys25, His159, and Asn175, papain numbering), as well as other six Cys residues, involved in the formation of disulfide bounds. Molecular modeling results suggest the enzyme belongs to the α + β class of proteins, with two disulfide bridges (Cys23-Cys63 and Cys57-Cys96) in the α domain, while the β domain is stabilized by another disulfide bridge (Cys153-Cys203). Additionally, peptide mass fingerprints (PMFs) of the three peptidases previously isolated from B. hieronymi fruits (namely hieronymain I, II, and III) were performed and compared with the theoretical fingerprint of PMF of Bh-CP1, showing a partial matching between the in silico-translated protein and hieronymain II.

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Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases

Cited by 60 publications

References 13 publications

Bromelain: biochemistry, pharmacology and medical use

Bromelain: biochemistry, pharmacology and medical use

Bromelain: an overview of industrial application and purification strategies

Cloning, Sequencing, and Identification Using Proteomic Tools of a Protease from Bromelia hieronymi Mez

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