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zingiber oligophyllum/protease

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Protease mediated proteolysis has been widely implicated in virulence of necrotrophic fungal pathogens. This is counteracted in plants by evolving new and effective antimicrobial peptides (AMP) that constitute important components of innate immune system. Peptide extraction from rhizome of Zingiber
BACKGROUND Due to increase in the number of patients with impaired immunity, incidence of dermatophytoses has increased considerably. Antidermatophytic agents with anti-inflammatory and protease-inhibiting activities will help in restricting inflammatory response associated with

ZCPG, a cysteine protease from Zingiber montanum rhizome exhibits enhanced anti-inflammatory and acetylcholinesterase inhibition potential

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A 48 kDa Zingiber montanum cysteine protease glycoprotein (ZCPG) purified previously was studied for anti-inflammatory and acetylcholinesterase inhibitory activity. The lipoxygenase inhibition by ZCPG was linear, with an IC50 value of 2.25 μM. MTT, LDH, and cell cycle analysis in THP-1 derived

Fluorescence quenching, structural and unfolding studies of a purified cysteine protease, ZCPG from Zingiber montanum rhizome.

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A first attempt was made to study the fluorescence quenching, structure and unfolding nature of the purified Zingiber montanum (J.Koenig) Link ex A.Dietr. cysteine protease glycoprotein (ZCPG). ATR-IR spectra showed the presences of amide groups along with carbohydrate stretch indicating the

Purification, biochemical characterization and antioxidant property of ZCPG, a cysteine protease from Zingiber montanum rhizome.

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Zingiber montanum cysteine protease glycoprotein (ZCPG) was purified to homogeneity by DEAE- cellulose and Sephadex G50 resulting in sixteen fold purification and total activity of 39.4U/mg. ZCPG presented a prominent single peak in HPLC chromatogram with an estimated molecular weight of 48kDa on
The objective of this study was to investigate the activity of a protein identified as cysteine protease, purified from Zingiber ottensii Valeton rhizomes, in terms of antiproliferation against fungi, bacteria, and human malignant cell lines. By means of buffer extraction followed by (NH(4))(2)SO(4)

The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale.

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A cysteine protease from ginger rhizome (GP-II) cleaves peptides and proteins with proline at the P(2) position. The unusual specificity for proline makes GP-II an attractive tool for protein sequencing and identification of stably folded domains in proteins. The enzyme is a 221 amino acid

Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale.

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The ginger proteases (GP-I and GP-II), isolated from the ginger rhizome Zingiber officinale, have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P2 position. The complete amino-acid sequence of GP-II, a glycoprotein containing 221 amino acids, and

Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome).

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This study was conducted to develop a method for improving tenderness and overall qualities of tough buffalo meat using plant proteolytic enzymes from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome). Their tenderizing efficacy was compared with the most popular enzyme

Partial characterization of an enzymatic extract from Bentong ginger (Zingiber officinale var. Bentong).

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Extraction of protease from a local ginger rhizome (Zingiber officinale var. Bentong) was carried out. The effect of extraction pH (6.4, 6.8, 7.0, 7.2, 7.6, 8.0, 8.4, and 8.8) and stabilizers (0.2% ascorbic acid, 0.2% ascorbic acid and 5 mM EDTA, or 10 mM cysteine and 5 mM EDTA) on protease activity

Data in support of three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes.

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This paper describes data related to a research article titled "Three Phase Partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes" (Gagaoua et al., 2015) [1]. Zingibain (EC 3.4.22.67), is a coagulant cysteine protease and a meat tenderizer agent that have been
Ginger, Zingiber officinale, which was fed at 0, 0.05, 0.1, 0.5 and 1.0 g per 100 g of feed for 14 days to rainbow trout, Oncorhynchus mykiss (Walbaum), led to control of experimental infection with Aeromonas hydrophila. At 0.5 g ginger per 100 g of feed, there was a reduction in mortalities to 0%

Enzyme-assisted extraction of bioactive compounds from ginger (Zingiber officinale Roscoe).

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Ginger (Zingiber officinale R.) is a popular spice used in various foods and beverages. 6-Gingerol is the major bioactive constituent responsible for the antiinflammatory, antitumour and antioxidant activities of ginger. The effect of application of α-amylase, viscozyme, cellulase, protease and

The hidden mechanism beyond ginger (Zingiber officinale Rosc.) potent in vivo and in vitro anti-inflammatory activity.

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BACKGROUND Ginger (Zingiber officinale Roscoe) is a well known anti-inflammatory drug in the Egyptian, Indian and Chinese folk medicines, yet its mechanism of action is unclear. OBJECTIVE To explore its mechanism of action and to correlate it to its biophytochemicals. METHODS Various extracts viz.
The present study was designed to investigate the dietary effects of ginger extract (Zingiber officinale) on common carp (Cyprinus carpio). Three hundred and sixty fish weighing 10.9 ± 0.17g were randomly divided into four experimental treatments in triplicates. Four experimental diets were designed
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