Protein inhibitors of hydrolases in plant foodstuffs

Belitz, Hans‐Dieter; Weder, Jürgen K. P.

doi:10.1080/87559129009540866

Cited by 60 publications

(45 citation statements)

References 271 publications

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“…No inhibitory activity was detected for porcine and human chymotrypsin, but the crude extract was able to weakly inhibit bovine quimotrypsin. A large number of grain legumes have been shown to inhibit trypsin and chymotrypsin from several animal sources (3,7,8).…”

Section: Discussionmentioning

confidence: 99%

“…The isoelectric focusing studies performed with the negative staining to inhibitor was used to detect the number and kind of inhibitor present in the crude extract (3,18). After negative staining for inhibitor, only one protein band was detected in the gel with a strong inhibitory activity for trypsin.…”

Section: Discussionmentioning

confidence: 99%

“…Inhibitors belonging to the Kunitz family present, in general, one polypeptide chain with 170-181 amino acids residues, molecular mass of » 20-22 kDa, one or two disul de bridges, and one reactive site localized close to the N-terminal region (1,3).…”

Section: Introductionmentioning

confidence: 99%

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Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

Pando

Ciero²,

Novello

et al. 1999

IUBMB Life

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SummaryA new trypsin inhibitor (CPTI) has been isolated from Crotalaria paulina seeds. Puri cation of the inhibitor was carried out by gel ltration, ion-exchange chromatography, and subsequent reversed-phase HPLC. The presence of a single polypeptide chain, with a molecular mass of 20 kDa and isoelectric point 4.0, was detected. The trypsin inhibitor had a K i value of 4.5 £ 10 ¡ 8 M and was capable of acting on human, bovine, and porcine trypsin and weakly on bovine chymotrypsin. Amino acid analysis showed that CPTI has a high content of aspartate, glutamate, leucine, serine, and glycine, having 177 amino acid residues in its composition. These data suggest that the protein belongs to the Kunitz-type trypsin inhibitors. IUBMB Life, 48: 519-523, 1999

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

Pando

Ciero²,

Novello

et al. 1999

IUBMB Life

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“…Protease inhibitors found in pulses act on either or both of the serine proteases chymotrypsin and trypsin and are important from the nutritional point of view [7,76]. They are found in relatively high quantities in pulses compared to other plant foods and can be broadly classiied as either Bowman-Birk or Kuniz type, based on their molecular masses and cystine contents [75].…”

Section: Protease Inhibitors Lectins and Phytatesmentioning

confidence: 99%

“…They are found in relatively high quantities in pulses compared to other plant foods and can be broadly classiied as either Bowman-Birk or Kuniz type, based on their molecular masses and cystine contents [75]. Inhibitors of the Kuniz type have two disulide bridges with a molecular mass of approximately 20 kDa and act speciically against trypsin, while the Bowman-Birk type contains seven disulide bridges, with a molecular mass between 8 and 10 kDa, and inhibits chymotrypsin and trypsin simultaneously at independent binding sites [7,76]. Although protease inhibitors can block chymotrypsin and trypsin activities, thus reducing protein digestibility, the Boman-Brik family of protease inhibitors has been reported to show antiinlammatory and anticarcinogenic efects in human colon cancer cells [77][78][79][80][81].…”

Section: Protease Inhibitors Lectins and Phytatesmentioning

confidence: 99%

Fermented Pulse-Based Food Products in Developing Nations as Functional Foods and Ingredients

Adebo¹,

Njobeh²,

AdeyinkaAdebiyi³

et al. 2017

Functional Food - Improve Health Through Adequate Food

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Pulses play a signiicant and diverse role in the agricultural systems and diets of underprivileged populations worldwide. They are ideal produce for reducing poverty, improving human health and nutrition, and enhancing resilience of the ecosystem. Fermentation is a processing technique that has been used for decades to transform food produce with improved health, functional, and nutraceutical beneits. In tandem with the United Nations' (UN's) sustainable development goal Number 3, fermented food products from pulses with health beneits align with this initiative to end hunger, achieve food security, and improve nutrition. In solidarity with the celebration of International Year of Pulses 2016 (IYP2016) and considering the relative neglect of pulses as compared with other food groups, this chapter would be vital in positioning pulses and fermented products from them as readily available functional foods. With increased interest in fermentation, fermented pulse-based foods have been identiied as excellent sources of bioactive and functional foods. Thus, fermented pulse-based products present a viable alternative, relatively available, afordable, and cheap source of foods with properties beyond that of basic nutrition.

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Protease inhibitors and lectins in soya beans and effects of aqueous heat-treatment

Armour¹,

Perera²,

Buchan³

et al. 1998

J. Sci. Food Agric.

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Protease inhibitor and lectin concentrations and N and lipid levels were evaluated in 27 soya bean samples. All contained trypsin and chymotrypsin inhibiting activity and lectin. Shinano midori, Shinano wasediro, Shinano‐oomame and Tsuronoku had high protein contents and average lipid levels, and their lectin and trypsin and chymotrypsin inhibitory activities were not unduly high. These lines, in particular, merit further nutritional evaluation. Food intake, feed conversion efficiency and growth by rats was reduced when soya bean was included in their diet, but the extent to which these parameters were affected did not appear to depend only on the protease inhibitor or lectin content. In contrast, pancreatic and small intestinal growth did seem to reflect the levels of these factors in the diet. Chymotrypsin inhibitor activity in soya bean was more readily abolished by heat‐treatment than was trypsin inhibitory activity. Lectin activity was also relatively heat‐resistant. However, all of these activities could be abolished by aqueous heat‐treatment of fully imbibed seeds at 100°C for 10 min. The effects of a soya diet on pancreas and small intestine weights were also abolished by this pre‐treatment, and food intake and nutrient utilisation by rats was greatly improved. © 1998 Society of Chemical Industry

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Protein inhibitors of hydrolases in plant foodstuffs

Cited by 60 publications

References 271 publications

Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

Fermented Pulse-Based Food Products in Developing Nations as Functional Foods and Ingredients

Protease inhibitors and lectins in soya beans and effects of aqueous heat-treatment

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