Purification and biochemical characterization of a 22-kDa stable cysteine- like protease from the excretory-secretory product of the liver fluke Fasciola hepatica by using conventional techniques

Hemici, Ahmed; Benerbaiha, Roumaila Sabrina; Bendjeddou, Dalila

doi:10.1016/j.jchromb.2017.10.049

Cited by 4 publications

(2 citation statements)

References 54 publications

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“…In addition, it was found that the level of peptidase activity in the whole body of hydrobionts (total samples of zooplankton, amphipoda, chironomid larvae, oligochaeta and dreissena) and the associated microbiota largely depends on pH (Kuz'mina et al, 2017). Cysteine-like protease of the hepatic fluke Fasciola hepatica exhibited the highest proteolytic activity on casein at pH 5.5 and temperature of 35-40 °C (Hemici et al, 2017). Information on the temperature characteristics of peptidases functioning in the whole body of potential prey of juvenile fish and adult benthophages living in freshwater bodies (Kuz'mina, 1999;Skvortsova et al, 2016) is rare.…”

Section: Introductionmentioning

confidence: 99%

Temperature characteristics of peptidase in chironomid larvae, potential fish prey, at various pH values

Кузьмина

Chornaya²,

Skvortsova

et al. 2018

Biosys. divers.

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The temperature dependence of casein- and hemoglobinlytic peptidases functioning in the whole organism of chironomid larvae Chironomus plumosus, food objects of adult benthophages and juvenile fish of various ecological groups, was studied within the temperature range of 0–70 ºС at different рН values (3.0, 5.0 and 7.4). The method of mixed samples was used to determine the activity and characteristics of enzymes. Homogenates of previously crushed and carefully mixed dozens of larvae were used as enzymatically active preparations. Activity of peptidases was assayed by the increase in tyrosine concentration using the Folin-Ciocalteu reagent. It is shown that the activity of peptidases that function in the tissues of chironomid larvae depends to a considerable extent on temperature and рН, but the pH has a smaller effect on the activity and the temperature dependence of casein- and hemoglobin-lytic peptidases than temperature. The temperature optimum of the studied peptidases of chironomid larvae corresponds to 40 ºС. The Q10 values in the zone of vital temperatures are slightly changed. They are, as a rule, increased in the zone of 30–40 ºС, and are sharply decreased in the zone of high temperatures. The values of activation energy of the process of hydrolysis of casein and hemoglobin in the zone of low and high temperatures are different. The Еact values of the process of hydrolysis of casein and hemoglobin at a temperature not exceeding 20 ºС are usually below those in the zone of higher temperatures (except for hemoglobin-lytic peptidases at pH 5.0). The data obtained indicate a significant effect of pH not only on the activity, but also on the temperature characteristics of peptidases that function in the body of chironomid larvae. Differences in the characteristics of casein- and hemoglobin-lytic peptidases in chironomid larvae at different temperatures and pH can influence the digestion in benthophages and fry of all fish species.

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Section: Introductionmentioning

confidence: 99%

Temperature characteristics of peptidase in chironomid larvae, potential fish prey, at various pH values

Кузьмина

Chornaya²,

Skvortsova

et al. 2018

Biosys. divers.

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“…After the final ultrafiltration step, the purification fold was increased up to 13.1 and the overall activity yield reached a rate of 18.8%. 46 A novel transglutaminase (MsTGase) from Mythimna separata larvae was found to display biochemical property and enzymatic catalytic activities and hence investigated. For this reason is was separated and purified; MsTGase was obtained chromatographically by the precipitation of Sephadex G-100 gel and DEAE-C-52 ion-exchange column with 48-fold purification and a reproducible yield of approximately 12%.…”

Section: © Author(s)mentioning

confidence: 99%

Diethylaminoethyl cellulose (DEAE-C) between chromatography and synthetic applications

Aljaf¹,

Amin²,

Hussain³

et al. 2020

Arkivoc

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The aim of this review is to point out the attention of the reader to the use of DEAE-C in organic reactions, possibly not only devoted to the preparation of heterocycles but potentially extending to other classes of organic compounds. Being DEAE-C an ammonium salt commonly used in chromatographic applications, it can be considered as a potential mild acid catalyst or a proton donor and these features can in theory catalyze standard acid-catalyzed organic reactions. In addition, the resin nature of DEAE-C could suggest the way to perform organic reactions in the solid state.

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Characterization, whole-genome sequence analysis, and protease production of a new thermophilic Bacillus licheniformis strain isolated from Debagh hot spring, Algeria

Boukeroui,

González-Siso,

DeCastro

et al. 2024

Int Microbiol

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Purification and biochemical characterization of a 22-kDa stable cysteine- like protease from the excretory-secretory product of the liver fluke Fasciola hepatica by using conventional techniques

Cited by 4 publications

References 54 publications

Temperature characteristics of peptidase in chironomid larvae, potential fish prey, at various pH values

Temperature characteristics of peptidase in chironomid larvae, potential fish prey, at various pH values

Diethylaminoethyl cellulose (DEAE-C) between chromatography and synthetic applications

Characterization, whole-genome sequence analysis, and protease production of a new thermophilic Bacillus licheniformis strain isolated from Debagh hot spring, Algeria

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