Antimicrobial activity studies on a trypsin–chymotrypsin protease inhibitor obtained from potato

Kim, Jin‐Young; Park, Seong-Cheol; Kim, Mi-Hyun; Lim, Hyung‐Tae; Park, Yoonkyung; Hahm, Kyung‐Soo

doi:10.1016/j.bbrc.2005.03.057

Cited by 138 publications

(79 citation statements)

References 24 publications

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“…The BBI are small cysteine-rich proteins in size (8-20kDa), with seven disulfide linkages, high cysteine content, and two independent reactive sites for trypsin and chymotrypsin, soluble between pH 1.5 and 12 and in dry state or in 0.02% aqueous solution is stable at 100 °C or at 105 °C for 10 min, respectively (Losso, 2008). These classes of proteins has been studied due to its application in the treatment of different pathologies as cancer (Zhang et al, 2011), antifungal activity (Kim et al, 2005), inflammation and coagulation (Machado et al, 2013) or as bioinsecticides (Rai et al, 2010), demonstrating its importance as new therapeutic agents for the pharmaceutical industry. Despite there are abundantly studies of PIs in leguminous plants, little is known in cereals, such as amaranth (Tamir et al, 1996); buckwheat (Park et al, 1997) and buckwheat Seeds (Tsybina et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds

Pesoti

Oliveira

et al. 2015

Food Sci. Technol

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A novel trypsin inhibitor of protease (CqTI) was purified from Chenopodium quinoa seeds. The optimal extracting solvent was 0.1M NaCl pH 6.8 (p < 0.05). The extraction time of 5h and 90 °C was optimum for the recovery of the trypsin inhibitor from C. quinoa seeds. The purification occurred in gel-filtration and reverse phase chromatography. CqTI presented active against commercial bovine trypsin and chymotrypsin and had a specific activity of 5,033.00 (TIU/mg), which was purified to 333.5-fold. The extent of purification was determined by SDS-PAGE. CqTI had an apparent molecular weight of approximately 12KDa and two bands in reduced conditions as determined by Tricine-SDS-PAGE. MALDI-TOF showed two peaks in 4,246.5 and 7,908.18m/z. CqTI presented high levels of essential amino acids. N-terminal amino acid sequence of this protein did not show similarity to any known protease inhibitor. Its activity was stable over a pH range (2-12), temperatures range (20-100 °C) and reducing agents.Keywords: purification; characterization; inhibitor of trypsin; Chenopodium quinoa; seeds. Practical Application:The purification and characterization of this novel trypsin inhibitor allow its study for a diversity of applications such as antibacterial, anticancer, anti-inflammatory and biotechnology and its further use as drugs for human diseases.

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Section: Introductionmentioning

confidence: 99%

Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds

Pesoti

Oliveira

et al. 2015

Food Sci. Technol

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“…The implication of trypsin and chymotrypsin inhibitors on fungal and bacterial growth inhibition has been previously reported [25][26][27][28]. Among the family 16 inhibitors, the 14 kDa protein from maize seed was able to inhibit spore germination and mycelial growth of nine different plant pathogen fungi [29].…”

Section: Introductionmentioning

confidence: 99%

Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms

Carrillo¹,

Herrero²,

Cambra³

et al. 2011

Plant Physiology and Biochemistry

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Keywords:Cysteine protease inhibitor Serine protease inhibitor Barley Plant pathogen Transgenic plant Protease inhibitors from plants have been involved in defence mechanisms against pests and pathogens. Phytocystatins and trypsin/a-amylase inhibitors are two of the best characterized protease inhibitor families in plants. In barley, thirteen cystatins (HvCPI-1 to 13) and the BTI-CMe trypsin inhibitor have been previously studied. Their capacity to inhibit pest digestive proteases, and the negative in vivo effect caused by plants expressing these inhibitors on pests support the defence function of these proteins. Barley cystatins are also able to inhibit in vitro fungal growth. However, the antifungal effect of these inhibitors in vivo had not been previously tested. Moreover, their in vitro and in vivo effect on plant pathogenous bacteria is still unknown. In order to obtain new insights on this feature, in vitro assays were made against different bacterial and fungal pathogens of plants using the trypsin inhibitor BTI-CMe and the thirteen barley cystatins. Most barley cystatins and the BTI-CMe inhibitor were able to inhibit mycelial growth but no bacterial growth. Transgenic Arabidopsis plants independently expressing the BTI-CMe inhibitor and the cystatin HvCPI-6 were tested against the same bacterial and fungal pathogens. Neither the HvCPI-6 expressing transgenic plants nor the BTI-CMe ones were more resistant to plant pathogen fungi and bacteria than control Arabidopsis plants. The differences observed between the in vitro and in planta assays against phytopathogenic fungi are discussed.

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“…Protease inhibitors (PIs) play essential roles in biological systems regulating proteolytic processes and participate in defense mechanisms against attack by a large number of insects (Carlini and Grossi-de-Sá, 2002), fungi (Kim et al, 2005) and other pathogenic microorganisms (Breiteneder and Radauer, 2004).…”

Section: Introductionmentioning

confidence: 99%

Physico-chemical and antifungal properties of protease inhibitors from Acacia plumosa

et al. 2009

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Antimicrobial activity studies on a trypsin–chymotrypsin protease inhibitor obtained from potato

Cited by 138 publications

References 24 publications

Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds

Extraction, purification and characterization of inhibitor of trypsin from Chenopodium quinoa seeds

Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms

Physico-chemical and antifungal properties of protease inhibitors from Acacia plumosa

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