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Potential Significance of Proteases
Published in Hafiz Ansar Rasul Suleria, Megh R. Goyal, Masood Sadiq Butt, Phytochemicals from Medicinal Plants, 2019
Marwa Waheed, Muhammad Bilal Hussain, Sadia Hassan, Mohammad Ali Shariati, Oluwafemi Adeleke Ojo
Plant derived enzymes are most popular choice and among these, protease are the major constituent of these enzymes.65 Proteases, like cardosins from Cynara sp., ficin from Ficus sp., and papain from C. papaya are sometimes constituents of sap, roots, seeds, latex, and fruits, but largely of their flowers or leave. Proteases from plant sources take part in numerous biological processes, such as hydrolysis of chloroplast proteins that are damaged by light, flower senescence, and storage protein mobilization. These enzymes are generally acid resistant and instigate their action in the abdomen.
Ancient Egyptian Pharmacology
Published in Ibrahim M. Eltorai, A Spotlight on the History of Ancient Egyptian Medicine, 2019
Figs were a valued article of food and medicine amongst the ancient Egyptians and subsequently the Hebrews and the Greeks. In the Qur’an (Rodwell, 2004) it is mentioned in relation to Sinai. The Hebrews called it tinab; in Arabic it is teen. It was one of the principal fruits of Palestine even before the entrance of the Hebrews. The fruits were made into a cake for the treatment of boils. The fig tree was associated with the wine as an emblem of peace or prosperity. Failure of the crop and destruction of the tree were regarded as misfortune and punishment from God. The trilobed leaf remained in symbolic worship since the earliest date. Let us read a quotation from Cultus Arborum: “Near Cairo at a fountain wherein the Virgin Mary washed her infant’s clothes, a lamp was, three centuries ago, kept burning in her honor in the hollow of an old fig tree, which has served them as a place of shelter” according to the Intinerario de Antonio Tenreiro (Lloyd, 1929). The fresh latex of Ficus (fig tree) species is antihelminthic. Its active principal is ficin, a crystallizable protective enzyme, which digests Ascaris in vitro. Ficin is highly effective in preventing the coagulation of blood and of milk, by digesting prothrombase and caseinogen (Cançado, 1944).
Molecular Recognition and Chemical Modification of Biopolymers — Two Main Components of Affinity Modification
Published in Dmitri G. Knorre, Valentin V. Vlassov, Affinity Modification of Biopolymers, 1989
Dmitri G. Knorre, Valentin V. Vlassov
Easy identification of essential residues is usually achieved when only a limited number (one to two) of specific residues is attacked by the reagent and modification results in complete inactivation of the biopolymer. Thus, very specific modification of a single SH group in the proteinases papain and ficin inactivates the enzymes demonstrating the essential role of this group for catalysis.81 Usually the results of chemical modification-inactivation studies are not clear-cut. Inactivation is achieved at rather heavy biopolymer derivatization; further analysis of modified residues is difficult and interpretation is uncertain. A typical example of studying the functional role of enzyme side chains is the investigation of the role of positively charged residues of Escherichia coli phenylalanyl-tRNA-synthetase in the aminoacylation of tRNAphe82,83 (see Section II.A).
Patent evaluation of US2019338018 (A1) 2019-11-07 (antibody fragments for the treatment of biofilm-related disorders)
Published in Expert Opinion on Therapeutic Patents, 2020
Ivana Cacciatore, Lisa Marinelli
Antibody fragmentation is usually performed using reducing agents and proteases that digest or cleave selective portions of the immunoglobulin protein structure. In this patent, inventors used ficin, a thiol protease, in the presence of cysteine at the concentration of 25 mM, to obtain monovalent fragments of 50,000 Daltons from murine monoclonal antibodies [24]. Fab fragments were also purified and analyzed by SDS-PAGE. On the other hand, rabbit Fab fragments were prepared from IgG-enriched polyclonal rabbit by 4-hour digestion with papain protease in the presence of cysteine and purified via Protein A spin column.
Enzymatic debridement: past, present, and future
Published in Acta Chirurgica Belgica, 2022
Ignace De Decker, Liesl De Graeve, Henk Hoeksema, Stan Monstrey, Jozef Verbelen, Petra De Coninck, Els Vanlerberghe, Karel E. Y. Claes
The first attempts at non-surgical treatment with enzymes involved the use of plant-derived products like e.g. papain, derived from the fruits and leaves of the Carica papaya (melon tree). Although described for burn wounds by Glasser [25] and Guzman [65], papain did not show promising results in clinical trials and its popularity decreased [66]. Other enzymes originating from plants, such as ficin latex of the Ficus tree, met the same fate.
Factors determining phage stability/activity: challenges in practical phage application
Published in Expert Review of Anti-infective Therapy, 2019
Ewa Jończyk-Matysiak, Norbert Łodej, Dominika Kula, Barbara Owczarek, Filip Orwat, Ryszard Międzybrodzki, Joanna Neuberg, Natalia Bagińska, Beata Weber-Dąbrowska, Andrzej Górski
Oral phage therapy seems to be an easy as well as low immunogenic approach for phage delivery [179]. It seems that the impact of saliva on phages is not a point of concern, as was observed for some Salmonella phages which were stable during incubation in human saliva [180] and for T3 coliphage that survived (less than one log unit decrease in phage titer after 30 min) in sprayed saliva in high relative humidity conditions [181]. Unfortunately, this mode of phage administration exposes it to some potentially non-favorable factors in the gastrointestinal tract (GIT), e.g. low pH in the stomach, which likely forms a major barrier, as shown by Verthe et al. (2004), digestive enzymes (mainly proteases), and bile salts [182]. Anti-phage IgA antibodies secreted into the intestinal lumen during long-term phage application may also antagonize phage transit in the GIT [179]. The impact of the gastric juice barrier on this transit in vivo was presented by Międzybrodzki et al. (2017), who observed that a T4 phage as well as the therapeutic staphylococcal phage A5/80 presented similar sensitivity to low pH in vitro (complete loss of antibacterial activity after 60 min incubation in phosphate buffered saline of pH 4.0 at 37°C) [183]. They were almost completely inactivated in the stomach after their oral administration to rats. Therefore authors stated that the transit of those phages from the stomach to the lower parts of the GIT may be significantly improved by oral application of a gastric juice neutralizer (dihydroxyaluminum sodium carbonate suspension) that is traditionally used in phage treatment conducted at the Phage Therapy Unit in Wroclaw as well as intravenous doses of proton pump inhibitor (omeprazole) or a H2 receptor antagonist (ranitidine) prior to phage application. Interestingly, natural yogurt also showed relatively strong enhancement of phage transit. Strong sensitivity (complete inactivation after 10 min incubation at 2.5 pH) to 0.5 mg/mL of pepsin was observed in vitro for coliphage CA933P, a potential biocontrol agent of enterohemorrhagic E. coli [184]. Other digestive enzymes may also influence phage activity. According to Northrop (1964), who studied the effect of proteolytic enzymes on lambda, T2 and P1 coliphages, chymotrypsin slowly inactivated P1 and T2 phages at high concentrations, whereas trypsin inactivated only the P1 phage [185]. Ficin (a protease belonging to a group of the cysteine endopeptidases that also includes papain) slowly inactivated T2 phage. The lambda phage was not sensitive against any of these enzymes. There are a few studies showing the influence of bile salts on phage in vitro activity. Salmonella phage Felix O1 titer decreased by 1.7 log units after its 3-hour incubation in 2% bile solution at 37°C [138]. A previously mentioned E. coli phage cocktail (ΦJLA23, ΦKP26, ΦC119 and ΦE142) was much more resistant when exposed to bile in comparable conditions, exhibiting only a 0.8 log decrease in the phage titer [164].