Protease Inhibitors in Cereals

Boisen, S.

doi:10.1080/00015128309435377

Cited by 47 publications

(16 citation statements)

References 83 publications

(76 reference statements)

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“…Evidence in support of this viewpoint was provided by observations of the high content of inhibitors in seeds and other storage organs of plants and of their dynamics in the course of seed maturation and germination [289][290][291]. Similar to other storage proteins, inhibitors are located in vacuoles and protein bodies [292][293][294]. In certain cases, proteinases were identified which initiated the decomposition of the inhibitors in germinating seeds [295,296].…”

Section: Physiological Functionsmentioning

confidence: 84%

Proteinase inhibitors and their function in plants: A review

Mosolov

Valueva

2005

Appl Biochem Microbiol

111

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Section: Physiological Functionsmentioning

confidence: 84%

Proteinase inhibitors and their function in plants: A review

Mosolov

Valueva

2005

Appl Biochem Microbiol

111

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“…Cereal grains contain multiple proteins that inhibit the activities of microbial proteinases [9,10] and it seems likely that they make some of these inhibitors to slow or prevent the disruption of the grain proteins during fungal attacks. We are purifying, identifying and characterizing the proteinases that are synthesized by Fusarium fungi when they are grown on grain protein-containing media.…”

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confidence: 99%

Purification and properties of an alkaline proteinase of Fusarium culmorum

Pekkarinen

Jones

Niku‐Paavola

2002

European Journal of Biochemistry

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The disease Fusarium head blight (scab) causes severe problems for farmers and for the industries that use cereals. It is likely that the fungi that cause scab (Fusarium spp.) use various enzymes when they invade grains. We are studying enzymes that the fungi may use to hydrolyze grain proteins. To do this, Fusarium culmorum was grown in a gluten-containing medium from which an alkaline serine proteinase with a molecular mass of 28.7 kDa was puri®ed by sizeexclusion and cation exchange chromatographies. The enzyme was maximally active at pH 8.3±9.6 and 50°C, but was unstable under these conditions. It hydrolyzed the synthetic substrates N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide and, to a lesser extent, N-succinyl-Ala-Ala-Pro-Leu p-nitroanilide. It was inhibited by phenylmethanesulfonyl¯u oride and chymostatin, but not by soybean trypsin or Bowman±Birk inhibitors. Parts of the amino-acid sequence were up to 82% homologous with those of several fungal subtilisins. One of the active site amino acids was detected and it occupied the same relative position as in the other subtilisins. Therefore, on the basis of these characteristics, the proteinase is subtilisin-like. Puri®cation of the enzyme was complicated by the fact that, when puri®ed, it apparently underwent autolysis. The presence of extraneous protein stabilized the activity.

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“…Several studies have shown that the content of proteinase inhibitors in oat, a cereal of the Aveneae tribe, is much lower than in the cereals of the Triticeae tribe (Mikola and Kirsi 1972, Boisen 1983) and, to our knowledge, no proteinase inhibitor has been isolated from oat grain and characterized. In an early study (Mikola and Kirsi 1972) wheat, rye and barley grains were all found to contain two types of trypsin inhibitors, an endosperm type (approximately 14 kDa) and an embryo type (approximately 16 kDa), which were characterized in detail in later studies (reviewed in Shewry 1999).…”

Section: Introductionmentioning

confidence: 89%

Serpins of oat (Avena sativa) grain with distinct reactive centres and inhibitory specificity

Hejgaard

Hauge

2002

Physiologia Plantarum

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Most proteinase inhibitors from plant seeds are assumed to contribute to broad-spectrum protection against pests and pathogens. In oat (Avena sativa L.) grain the main serine proteinase inhibitors were found to be serpins, which utilize a unique mechanism of irreversible inhibition. Four distinct inhibitors of the serpin superfamily were detected by native PAGE as major seed albumins and purified by thiophilic adsorption and anion exchange chromatography. The four serpins OSZa-d are the first proteinase inhibitors characterized from this cereal. An amino acid sequence close to the blocked N-terminus, a reactive centre loop sequence, and the second order association rate constant (ka') for irreversible complex formation with pancreas serine proteinases at 24 degrees C were determined for each inhibitor. OSZa and OSZb, both with the reactive centre scissile bond P1-P1' Thr downward arrow Ser, were efficient inhibitors of pancreas elastase (ka' > 105M-1 s-1). Only OSZb was also an inhibitor of chymotrypsin at the same site (ka' = 0.9 x 105M-1 s-1). OSZc was a fast inhibitor of trypsin at P1-P1' Arg downward arrow Ser (ka' = 4 x 106M-1 s-1); however, the OSZc-trypsin complex was short-lived with a first order dissociation rate constant kd = 1.4 x 10-4 s-1. OSZc was also an inhibitor of chymotrypsin (ka' > 106M-1 s-1), presumably at the overlapping site P2-P1 Ala downward arrow Arg, but > 90% of the serpin was cleaved as substrate. OSZd was cleaved by chymotrypsin at the putative reactive centre bond P1-P1' Tyr downward arrow Ser, and no inhibition was detected. Together the oat grain serpins have a broader inhibitory specificity against digestive serine proteinases than represented by the major serpins of wheat, rye or barley grain. Presumably the serpins compensate for the low content of reversible inhibitors of serine proteinases in oats in protection of the grain against pests or pathogens.

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Protease Inhibitors in Cereals

Cited by 47 publications

References 83 publications

Proteinase inhibitors and their function in plants: A review

Proteinase inhibitors and their function in plants: A review

Purification and properties of an alkaline proteinase of Fusarium culmorum

Serpins of oat (Avena sativa) grain with distinct reactive centres and inhibitory specificity

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