PURIFICATION AND PARTIAL CHARACTERIZATION OF TWO ?-AMYLASE INHIBITORS FROM BLACK BEAN (Phaseolus vulgaris)

Frels, Jane Marie; Rupnow, John H.

doi:10.1111/j.1745-4514.1984.tb00329.x

Cited by 35 publications

(30 citation statements)

References 38 publications

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“…Inhibitors have been purified from black, white and red kidney beans and pinto beans (Marshall and Lauda, 1975;Powers and Whitaker, 1977a,b;Frels and Rupnow, 1984;Wilcox and Whitaker, 1984b;Lajolo and Finardi Filho, 1985;Kotaru et al, 1987;Ho and Whitaker, 1993a,b;X. Yin and J.R. Whitaker, 1994, unpublished data).…”

Section: Common Bean (Phaseolus Vulgaris) A-amylase Inhibitorsmentioning

confidence: 99%

“…The carbohydrate content of several of the inhibitors (Table 5.6) ranges from 7.5% for black bean 1-1 (Frels and Rupnow, 1984) to 14.5% for black bean var. Rico 23 .…”

Section: Carbohydrate Contentmentioning

confidence: 99%

“…Two different cultivars of red kidney beans had 8.6% (Powers and Whitaker, 1977a) and 13.0% (Wilcox and Whitaker, 1984b) carbohydrate. Isoinhibitors from the same black bean contained from 7.5-9.0% carbohydrate (Frels and Rupnow, 1984). A 6 M urea-PAGE of the black bean inhibitors 1-1 and 1-2 (X. Yin and J.R. Whitaker, 1994, unpublished data), black bean var.…”

Section: Carbohydrate Contentmentioning

confidence: 99%

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Naturally occurring α-amylase inhibitors: Structure/function relationships

Ho¹,

Yin²,

Filho³

et al. 1994

Protein Structure-Function Relationships in Foods

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Perhaps because a-amylase is ubiquitous in all living systems, several natural inhibitors against this enzyme are found in biological materials. These inhibitors include the microbial nitrogen-containing carbohydrates with an oligobioamine unit, the microbial polypeptides such as Paim and Haim, and the larger protein inhibitors, found in cereals, legumes and some other higher plants. The protein inhibitors were discovered as early as 1933; however, much of the research has been performed since the mid 1970s, with important medical, nutritional and insect-control implications. The structures of several of the microbial N-containing carbohydrates and microbial polypeptides are known, and aminoacid sequences are also known for some of the higher plant protein inhibitors. Enzyme specificity studies with several a-amylases have been carried out, some detailed kinetic studies are available and a few chemical modification studies have been performed. Nevertheless, very little is known about why and how the compounds inhibit a-amylases, primarily those from animals and insects. R. Y. Yada et al. (eds.), Protein Structure-Function Relationships in Foods

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Section: Common Bean (Phaseolus Vulgaris) A-amylase Inhibitorsmentioning

confidence: 99%

“…The carbohydrate content of several of the inhibitors (Table 5.6) ranges from 7.5% for black bean 1-1 (Frels and Rupnow, 1984) to 14.5% for black bean var. Rico 23 .…”

Section: Carbohydrate Contentmentioning

confidence: 99%

Section: Carbohydrate Contentmentioning

confidence: 99%

See 1 more Smart Citation

Naturally occurring α-amylase inhibitors: Structure/function relationships

Ho¹,

Yin²,

Filho³

et al. 1994

Protein Structure-Function Relationships in Foods

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“…The inhibitor blocks the function of mammalian salivary and'pancreatic amylases but not plant, fungal, or bacterial a-amylases. aAIs from red kidney bean and black kidney bean inhibit the aamylase of Tenebrio molitor (Powers and Whitaker, 197713;Frels and Rupnow, 1984). Furthermore, aAI from kidney bean inhibits a-amylase from three species of bruchids that are seed storage pests (Ishimoto and Kitamura, 1989).…”

Section: Division Of Energy Biosciencesmentioning

confidence: 99%

Activation of Bean (Phaseolus vulgaris) [alpha]-Amylase Inhibitor Requires Proteolytic Processing of the Proprotein

1993

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Seeds of the common bean (Pbaseolus vulgaris) contain a plant defense protein that inhibits the a-amylases of mammals and insects. This a-amylase inhibitor (aAl) is synthesized as a proprotein on the endoplasmic reticulum and is proteolytically processed after arrival in the protein storage vacuoles to polypeptides of relative molecular weight (M,) 15,000 to 18,000. We report two types of evidence that proteolytic processing is linked to activation of the inhibitory activity. First, by surveying seed extracts of wild accessions of P. vulgaris and other species in the genus Pbaseolus, we found that antibodies to uAl recognize large (M. 30,000-35,000) polypeptides as well as typical aAl processing products (M, 15,000-18,000). aAl activity was found in all extracts that had the typical aAl processed polypeptides, but was absent from seed extracts that lacked such polypeptides. Second, we made a mutant aAl in which asparagine-77 is changed to aspartic acid-77. This mutation slows down the proteolytic processing of pro-aAl when the gene is expressed in tobacco. When pro-aAl was separated from mature aAl by gel filtration, pro-aAl was found not to have a-amylase inhibitory activity. We interpret these results to mean that formation of the active inhibitor is causally related to proteolytic processing of the proprotein. We suggest that the polypeptide cleavage removes a conformational constraint on the precursor to produce the biochemically active molecule.Many secretory proteins in plant, mammalian, and funga1 cells are synthesized as preproproteins that undergo cotranslational removal of the signal peptide, as well as posttranslational proteolytic maturation processing (Neurath, 1986). Such maturation processing, which may occur as a singlestep or a multistep process, converts an inactive proprotein into an active mature protein through the release of a confonnational constraint within the proprotein. Examples are the release of peptide hormones and growth factors in mammalian and yeast cells, the activation of enzyme zymogens, especially proteases, the complement system, and blood coagulation. Processing is often accompanied by the loss of one or more polypeptide domains that are present in the proprotein but absent from the mature protein. Limited proteolysis requires that enzyme and substrate be present in the same compartment and that the processing enzyme be specific for the cleavage and selective for the substrate.

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“…I) IX-Amylase inhibitors have been purified from white kidney beans,z) red kidney beans/A) and black bean. 5 ) However, IX-amylase inhibitor in pinto kidney beans has not been studied. In this paper, the purification and some properties of an IX-amylase inhibitor from cranberry bean (American pinto bean) were described.…”

mentioning

confidence: 99%