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      Enzymological characterization of pineapple extract for potential application in oak tasar (Antheraea proylei J.) silk cocoon cooking and reeling

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          Abstract

          Proteinases have the potential to effect partial solubilization of the proteinaceous gum sericin involved in binding the silk strands together in cocoon, an essential step in the silk cocoon cooking and reeling. Therefore, pineapple extract rich in cysteine proteinases was enzymologically characterized for its potential application in oak tasar (Antheraea proylei J.) silk cocoon cooking and reeling. Optimum sodium carbonate concentration (9.8 mM) and optimum temperature (60ºC) for the proteinase activity were determined. Though relatively thermostable, an enhanced activity loss was observed when the extract was incubated in the temperature range 70-90ºC with sodium carbonate. Bulk of the activity (80-83%) remained after 1 hr of time-dependent inactivation at 60ºC. The tasar cocoon extract neither caused inhibition of the activity nor enhanced its time-dependent loss by incubation at 60ºC. However, it caused an enhanced time-dependent loss of the activity by incubation at 60ºC with sodium carbonate. Considering these enzymological characteristics, experimental cocoon-cooking media were constituted by taking the pineapple extract with or without sodium carbonate at room temperature or 60ºC. The results of the cocoon cooking and subsequent single silk filament reeling indicated for an applicability of pineapple extract as an effective agent for the oak tasar cocoon cooking and reeling.

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          Most cited references18

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          Bromelain: biochemistry, pharmacology and medical use.

          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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            Bromelain protects piglets from diarrhoea caused by oral challenge with K88 positive enterotoxigenic Escherichia coli.

            K88 positive enterotoxigenic Escherichia coli (K88+ ETEC) is an important cause of diarrhoea in young piglets. K88+ ETEC pathogenesis relies on attachment to specific glycoprotein receptors located on the intestinal mucosa. Proteolytic treatment of these receptors in vitro and in vivo prevents attachment of K88+ ETEC to piglet small intestines and may be of clinical use to prevent K88+ ETEC pathogenesis. To determine whether bromelain, a proteolytic extract obtained from pineapple stems, would protect piglets against K88+ ETEC diarrhoea and to confirm and extend earlier findings on the effects of bromelain on K88+ ETEC receptors in vivo. Bromelain (0, 12.5, or 125 mg) was orally administered to just weaned piglets for 10 days. One day following commencement of bromelain treatment, piglets were challenged with K88+ ETEC (5 x 10(10) K88ac:0149) for seven days. Intestinal contents from unchallenged piglets were obtained via an intestinal fistula, and tested for their ability to bind K88+ ETEC before and after bromelain treatment. Both doses of bromelain were successful in reducing the incidence of K88+ ETEC diarrhoea and protected piglets from life threatening disease. Bromelain treated pigs also had significantly increased weight gain compared with untreated pigs. Bromelain only temporarily inhibited K88+ ETEC receptor activity, with receptor activity being regenerated 30 hours following treatment, consistent with the regeneration of new enterocytes. Results show that bromelain can temporarily inactivate ETEC receptors in vivo and protect against ETEC induced diarrhoea. Bromelain may therefore be an effective prophylaxis against ETEC infection.
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              Methods in Enzymology

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                Author and article information

                Journal
                ejb
                Electronic Journal of Biotechnology
                Electron. J. Biotechnol.
                Pontificia Universidad Católica de Valparaíso (Valparaíso, , Chile )
                0717-3458
                December 2003
                : 6
                : 3
                : 198-207
                Affiliations
                [03] Canchipur orgnameManipur University orgdiv1Biochemistry Department India kdsanjenbam@ 123456yahoo.com
                [02] Canchipur orgnameManipur University orgdiv1Biochemistry Department India y_ranjana@ 123456yahoo.co.in
                [01] Canchipur orgnameManipur University orgdiv1Biochemistry Department India rslaishram@ 123456yahoo.com
                Article
                S0717-34582003000300005 S0717-3458(03)00600305
                10.4067/S0717-34582003000300005
                cd0a7990-e3f8-43be-8795-995a3bde239b

                This work is licensed under a Creative Commons Attribution 4.0 International License.

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                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 18, Pages: 10
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                SciELO Chile

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                RESEARCH ARTICLES

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