Cysteine Proteases

Grzonka, Zbigniew; Kasprzykowski, Franciszek; Wiczk, Wiesław

doi:10.1007/1-4020-5377-0_11

Cited by 40 publications

(31 citation statements)

References 82 publications

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“…While the optimum pH range for FBM is 3-8 and optimum temperature ranges from 37-70 ºC (Lopes et al 2009;Jutamongkon and Charoenrein 2010;Silvestre et al 2012). Likewise, the molecular weight range for SBM is 26-37kDa (Grzonka et al 2007;Kumar et al 2011) and for FBM molecular weight range is 24.5-32kDa (Grzonka et al 2007;Lopes et al 2009;Gautam et al 2010). When bromelain is kept at -20 ºC its stability remains intact for a defined time period (Rowan et al 1990).…”

Section: Propertiesmentioning

confidence: 99%

“…When bromelain is kept at -20 ºC its stability remains intact for a defined time period (Rowan et al 1990). Amongst other, cysteine is the most efficient compound for the activation of bromelain (Grzonka et al 2007). SBM is in fact a combination of several thiol endopeptidases (Pavan et al 2012) and also contains compounds like peroxidases, acid phosphatase, several protease inhibitors glucosidases, cellulases, glycoproteins, carbohydrates and organically intact Ca 2+ (Maurer 2001;Smith-Marshall and Golden 2012).…”

Section: Propertiesmentioning

confidence: 99%

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Bromelain: Methods of Extraction, Purification and Therapeutic Applications

Manzoor

Nawaz

Mukhtar

et al. 2016

Braz. arch. biol. technol.

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Section: Propertiesmentioning

confidence: 99%

Section: Propertiesmentioning

confidence: 99%

Bromelain: Methods of Extraction, Purification and Therapeutic Applications

Manzoor

Nawaz

Mukhtar

et al. 2016

Braz. arch. biol. technol.

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“…Even though, both stem bromelain and fruit bromelain are single-chain glycosylated enzymes, stem bromelain has low proteolytic ability and specificity for peptide bonds compared to fruit bromelain. Similarly, the molecular weight ranges for stem bromelain and fruit bromelain are 26–37 kDa and 24.5–32 kDa respectively (Grzonka et al, 2007; Gautam et al, 2010; Kumar et al, 2011). …”

Section: Roles Of Plant Protease Inhibitors In Health and Disease Conmentioning

confidence: 99%

Plant Protease Inhibitors in Therapeutics-Focus on Cancer Therapy

2016

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Plants are known to have many secondary metabolites and phytochemical compounds which are highly explored at biochemical and molecular genetics level and exploited enormously in the human health care sector. However, there are other less explored small molecular weight proteins, which inhibit proteases/proteinases. Plants are good sources of protease inhibitors (PIs) which protect them against diseases, insects, pests, and herbivores. In the past, proteinaceous PIs were considered primarily as protein-degrading enzymes. Nevertheless, this view has significantly changed and PIs are now treated as very important signaling molecules in many biological activities such as inflammation, apoptosis, blood clotting and hormone processing. In recent years, PIs have been examined extensively as therapeutic agents, primarily to deal with various human cancers. Interestingly, many plant-based PIs are also found to be effective against cardiovascular diseases, osteoporosis, inflammatory diseases and neurological disorders. Several plant PIs are under further evaluation in in vitro clinical trials. Among all types of PIs, Bowman-Birk inhibitors (BBI) have been studied extensively in the treatment of many diseases, especially in the field of cancer prevention. So far, crops such as beans, potatoes, barley, squash, millet, wheat, buckwheat, groundnut, chickpea, pigeonpea, corn, and pineapple have been identified as good sources of PIs. The PI content of such foods has a significant influence on human health disorders, particularly in the regions where people mostly depend on these kind of foods. These natural PIs vary in concentration, protease specificity, heat stability, and sometimes several PIs may be present in the same species or tissue. However, it is important to carry out individual studies to identify the potential effects of each PI on human health. PIs in plants make them incredible sources to determine novel PIs with specific pharmacological and therapeutic effects due to their peculiarity and superabundance.

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“…However, Tyr fluorescence is either very weak or masked by the greater signal from Trp [37]. Ficin contains six Trp and fifteen Tyr residues [19]. The emission maximum at 338 nm in the fluorescence spectrum of CF agrees well with that of class 'B' proteins which contain Trp residues [38].…”

Section: Fluorescence Characteristicsmentioning

confidence: 70%

“…3.4.22.3), an endopeptidase of the sulfhydryl protease class, has been widely used for industrial meat tenderization, alcohol production, photographic industries etc. [19]. It belongs to the papain superfamily because of its many properties and primary structural similarity to papain [20].…”

Section: Introductionmentioning

confidence: 99%