Protease inhibitors from broad bean isolation and purification

Warsy, Arjumand S.; Norton, G.; Stein, M.

doi:10.1016/s0031-9422(00)86924-1

Cited by 39 publications

(15 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, there are reports of plant protease inhibitors inhibiting other classes of proteases. The trypsin/ chymotrypsin inhibitor from broad beans inhibits the sulphydryl enzyme papain [56]. Serine protease inhibitors such as barley subtilisin inhibitor [57] and wheat germ protease K inhibitor [58] are found to be active against α -amylases.…”

Section: Discussionmentioning

confidence: 99%

Evaluating the role of a trypsin inhibitor from soap nut (Sapindus trifoliatus L. Var. Emarginatus) seeds against larval gut proteases, its purification and characterization

et al. 2015

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Evaluating the role of a trypsin inhibitor from soap nut (Sapindus trifoliatus L. Var. Emarginatus) seeds against larval gut proteases, its purification and characterization

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Several workers7, 10 have reported the presence of proteinaceous, heat labile, protease inhibitors in whole field beans. The results of these studies confirm the findings reported previously even for varieties and genotypes of both widely differing protein contents and diverse geographical origins.…”

Section: Discussionmentioning

confidence: 99%

The inhibition of digestive enzymes by extracts of field bean (vicia faba)

Griffiths

1979

J Sci Food Agric

View full text Add to dashboard Cite

Protease inhibitor activity was determined for a wide range of differing field bean (Viciu fabn) varieties and genotypes. Although a two-fold variation was observed under the assay conditions used, the highest values were approximately five times less active in inhibiting trypsin than either soya or navy beans. N o correlation was found between protein content and protease inhibitor activity. Water extracts from the testa from coloured-flower varieties inhibited the activity of a-amylase, lipase and trypsin. The addition of polyvinylpyrrolidone reactivated these enzymes t o varying degrees. No inhibitory activity was found in similar extracts from white-flowered varieties. It was concluded that the enzyme inhibition exhibited by extracts of the seed coat of coloured varieties was due to the presence of tannins.

show abstract

“…minor L.) and many other legumes contain inhibitors of mammalian trypsin and chymotrypsin (Warsy et al 1974). Borchers et at.…”

mentioning

confidence: 99%

Trypsin Inhibitor Activity in Faba Beans (Vicia Faba Var. Minor), Changes During Germination and Distribution

Bhatty¹

1977

Can. J. Plant Sci.

View full text Add to dashboard Cite

Faba beans (Vicia faba var. minor L.) contained about the same level of trypsin inhibitor activity (TIA) as lentils and peas, ⅓ to [Formula: see text] that of vetch, chick pea and bean and about [Formula: see text] to [Formula: see text] that of flatpea and soybean. The TIA of faba bean increased two-fold during germination on the 3rd to 4th days after which it declined. The TIA was present mostly in the cotyledon fraction of faba bean.

show abstract

Protease inhibitors from broad bean isolation and purification

Cited by 39 publications

References 15 publications

Evaluating the role of a trypsin inhibitor from soap nut (Sapindus trifoliatus L. Var. Emarginatus) seeds against larval gut proteases, its purification and characterization

Evaluating the role of a trypsin inhibitor from soap nut (Sapindus trifoliatus L. Var. Emarginatus) seeds against larval gut proteases, its purification and characterization

The inhibition of digestive enzymes by extracts of field bean (vicia faba)

Trypsin Inhibitor Activity in Faba Beans (Vicia Faba Var. Minor), Changes During Germination and Distribution

Contact Info

Product

Resources

About