Proteases bromelain

L C Yamaguchl, K. Shibacam, Y. Suzuki. K. Yamazaki. Y. Komuchi. H. Onishi. and R Fujimura, Ajiti-inflammatory actions of proteases, bromelain, trypsin and their mixed preparations (original In Japanese). Nippon Yakurigaku Zesshi 75227 (1979). 

R. M. Silverstein and F. J. Klzdy. Characterization of the pineapple stem proteases (bromelains). Arch. Biochem. Biophys. 167 618 (1975). 

Bromeiain Cone.. See Protease Bromelain juice Bromelains. See Bromelain Bromelia. See P-Naphthyl ethyl ether Bromelin Bromelin ananase. See Bromelain Bromeosin. See D C Red No. 21 Solvent red 43... 

Another subclass of proteases attacks internal peptide bonds and Hberates large peptide fragments. Bromelain, a plant protease derived from the stem of the pineapple plant, can even produce detectable semm proteolysis after oral adrninistration (180). Oral therapy with bromelain significantly reduces bmising that stems from obstetrical manipulations (181). Bromelain—pancreatin combinations have been more effective in digestive insufficiency compared to either pancreatin or placebo (182,183). Bromelain may also enhance the activity of antibiotics, especially tetracycline, when adrninistered concurrently (184). 

Bromelain (anti-inflammatory Ananase from pineapple) [37189-34-7] Mr 33 000, [EC 3.4.33.4]. This protease has been purified via the acetone powder, G-75 Sephadex gel filtration and Bio-Rex 70 ion-exchange chromatography and has Aj 20.1 at 280nm. The protease from pineapple hydrolyses benzoyl glycine ethyl ester with a Km (app) of 210mM and kcat of 0.36 sec. [Murachi Methods Enzymol 19 273 1970 Balls et al. nd Eng Chem 33 950 1941.]... 

Pancreatin is a pancreatic extract usually obtained from the pancrease of slaughterhouse animals. It contains a mixture of enzymes, principally amylase, protease and lipase, and, thus, exhibits a broad digestive capability. It is administered orally mainly for the treatment of pancreatic insufficiency caused by cystic fibrosis or pancreatitis. As it is sensitive to stomach acid, it must be administered in high doses or, more usually, as enteric-coated granules or capsules that may be taken directly or sprinkled upon the food prior to its ingestion. Individual digestive activities, such as papain, pepsin or bromelains (proteases), or a-amylase are sometimes used in place of pancreatin. 

The protein obtained from the use of bromelain in the enzymatic corn wet milling process is different from that of the conventional corn wet milling process. Bromelain has a very wide spectrum of protease activities. Bromelain not only degrades the glutelin matrix that surrounds starch... 

FIG. 4 SDS gel electrophoresis of insoluble gluten samples from laboratory corn wet milling. Lane 1 Molecular mass standards (250, 150, 100, 75, 50, 37, 25, 15, and lOkDa). Lane 2 Enzymatic milling with commercial protease with added S02 and lactic acid. Lane 3 Enzymatic milling with commercial protease and no added S02. Lane 4 Conventional laboratory milling. Lane 5 Enzymatic milling using Bromelain and no added S02. 

Plant Proteases. These include the well known proteases papain, bromelain and ficin. Most plant enzymes are available as comparatively unpurified powder extracts, although papain is notable for being available in a stabilized and purified liquid form. Prospects for increased supply of plant enzymes, in response to greater use in traditional applications or for new processes, depend on several factors. Tlie influence of cultivation conditions, growth cycle and climate requirements make new supplies long term projects. 

The greatest variety of industrial enzymes are presently derived from microbial sources, with a lesser diversity coming from plant and animal sources 34), Enzymes derived from plant sources and which are used extensively in the food industry include papain, bromelain, ficin, and amylases. Animal enzymes of economic importance include trypsins, lipases, and gastric proteases. 

Treatment of albumen with trypsin, bromelain and fungal protease produced significantly greater volumes of foam compared to stored control albumen (49). However, all enzyme treatments had inferior foam stability when compared to controls. Both the rate and amount of foam collapse was greater in enzyme-treated samples. The fresh control produced the most stable foam. 

In enzymes, the most common nucleophilic groups that are functional in catalysis are the serine hydroxyl—which occurs in the serine proteases, cholinesterases, esterases, lipases, and alkaline phosphatases—and the cysteine thiol—which occurs in the thiol proteases (papain, ficin, and bromelain), in glyceraldehyde 3-phosphate dehydrogenase, etc. The imidazole of histidine usually functions as an acid-base catalyst and enhances the nucleophilicity of hydroxyl and thiol groups, but it sometimes acts as a nucleophile with the phos-phoryl group in phosphate transfer (Table 2.5). 

Bromelain—a plant protease with uses similar to those of papain. Bromelain is obtained from stumps left over from pineapple harvest. 

Cysteine (or thiol) proteases. The /3-thiol group is an even better nucleophile in comparison with the serine side chain thiol proteases operate under alkaline pH values as well examples include papain and bromelain. 

Cysteine proteases are a class of enzymes that have been widely studied over the years. The overall principles of substrate recognition, catalysis, and inhibition are now reasonably well documented. This enzyme class includes the plant proteases such as papain, actinidin, and bromelain, and several mammalian lysosomal cathe-psins. By far the majority of the literature reports dealing with cysteine proteases describe results obtained with the enzyme papain, because it is considered to be the archetype of this enzyme class. 

It is probable that proteases such as trypsin and bromelain, which are somewhat stable to self-proteolysis, would be absorbed to a greater extent than otho1 proteins of comparable size. Coadimiustraiion of soybean trypsin inhibitors or pancreatic duct ligation increases the absorption of intact protein [39]. 

G, Kamphuis, J. Drentii, and E. N. Baker. Thiol protease. Comparative studies based on the high-resolution structures of papain and actinidin, and an amino acid sequence information far cathenaim B and R and stem bromelain. J. MoL BioL /62 317 (19B5). 

Bromelain differs from (be other cysieinyl proteases papain and ficin in its 140-told difference of Itcat for the BAEK and BAA hydrolysis, suggesting a difference in the mechanism of catalysis for both substrates [37]. For BABE hydrolysis, deacylation is predominantly the rate-limiting step, while for BAA hydrolysis (he acylation is rate limiting [42]. However, Wharton et aL [43] explained the differences in kcot for BAEE and BAA hydrolysis a gauming (hat nonproductive binding plays a role in catalysis. 

R. M. Hdnicke and W. A. Gortner. Stem bromelain, a nrar protease preparation from pineapple plants. Econ. Hot. 11 225 (1957). 

R. M. Silveistdn and F. J. K zdy. Separation and characterization of sulfhydiyl proteases from stem bromelain. Fed Proc. Fed Am. Sac. Exp. BioL 29 929Ah ... 

S. Uda, M. Sasaki, and S. Ota. Immunological cross-reaction between thiol proteases of plant origin stem and fruit bromelains. J. Biochem. 73 377 (1973). 

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