Digestibility and proteinase inhibitory action of a kidney bean globulin

Seidl, Dinah S.; Jaffe, Mercedes; Jaffé, W. G.

doi:10.1021/jf60166a004

Cited by 40 publications

(9 citation statements)

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“…aureus and Ph. mzGltgo [IZ,131 and three varieties of 7 s reserve proteins in Dolichos lablab [II]. In these cases we studied the sum of respective proteins.…”

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confidence: 99%

The action of trypsin and chymotrypsin on the reserve proteins of some leguminous seeds

Vaintraub¹,

Bassüner²,

Shutov³

1976

Nahrung

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The action of trypsin on the reserve proteins of the leguminous seeds belonging to Vicieae and Phaseoleae tribes was investicated. The hydrolysis of11S and 7S proteins of Vicieae proceeds relatively fast and some of the proteins are hydrolyzed practically completely. The hydrolysis of most of the investigated reserve proteins of the Phaseoleae tribe proceeds much slower, while that of 7S proteins of four Phaseolus species of American origin stops after the cleavage of only 10-20% of peptide bonds capable of reacting. Analogous results were obtained studying the action of chymotrypsin on a more restricted number of proteins. Both trypsin and chymotrypsin hydrolyze the same parts of Ph. vulgaris 7S protein, splitting off peptides which can be separated on a Sephadex G-50 column. The nonhydrolyzable high molecular weight core has a slightly smaller sedimentation coefficient and a higher elelctrophoretic mobility than the native protein and is able to dimerize at high ionic strength. Urea does not alter the hydrolyzability of the core butt the latter is partially hydrolyzed after the action of urea or guanidine hydrocholoride in the presence of mercaptoethanol.

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“…aureus and Ph. mzGltgo [IZ,131 and three varieties of 7 s reserve proteins in Dolichos lablab [II]. In these cases we studied the sum of respective proteins.…”

mentioning

confidence: 99%

The action of trypsin and chymotrypsin on the reserve proteins of some leguminous seeds

Vaintraub¹,

Bassüner²,

Shutov³

1976

Nahrung

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“…Since trypsin is an anti‐nutritional factor, it should be reduced to minimum. Trypsin bound with the proteolytic enzyme and does not let them act on the proteins to break down in peptides and causes indigestion (Seidl, Jaffé, & Jaffe, 1969). UT played a significant role in inactivating the trypsin inhibitors, as it may cause denaturation of the trypsin inhibitors.…”

Section: Resultsmentioning

confidence: 99%

Comparative performance analysis of enzyme inactivation of soy milk by using RSM and ANN

Kumar

Rao

Rana

et al. 2020

J Food Process Engineering

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The presence of antinutritional factors as trypsin inhibitors (TIA) and lipoxygenase (LOX) in soy milk produces indigestion and off‐flavor due to oxidation of linoleic acid to hyperoxide. The objective of the study was to determine the prediction capacity of response surface methodology (RSM) and artificial neural network (ANN) for enzyme inactivation of soy milk. The microwave and thermo‐sonication method were used to prepare and treat the sample. Statistical parameters like NRMSE and %MAE were used to compare and evaluate the final result. NRMSE value had shown five times better results in the case of ANN (0.015) compared to RSM (0.082). Similarly, the % MAE value was also fivefold better in the case of ANN. In the case of RSM, Chi‐square values for TIA and LOX were 317.32 and 146.73, respectively. Whereas for ANN, the value was 4.68 and 2.69, respectively. So, it can be concluded that the prediction capacity of ANN is better than RSM. Practical Applications This modeling has a tremendous potential contributing to prediction of enzymes inactivation without real‐time experiments with great accuracy. Moreover, a number of industries are producing soy milk nowadays, and it could be helpful in elimination of beany flavor with desirable inactivation of lipoxygenase and enhancing the digestibility by removing trypsin inhibitors with appropriate environmental conditions. In addition, it can also pave the way for a number of food processing technology in which enzymatic inactivation is prominent and the prediction of percentage inactivation is crucial. This technique could be applied to predict the yield of any process after maintaining a certain treatment and process condition. Process engineering of any industry and biochemical processes are very sensitive to small changes in parameters and their effects could be predicted by using the modern approach of artificial neural network with more preciseness without running the actual experiments.

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“…The distribution of the trypsin inhibitory activity was rather complex (Table 3). There might be as many as three types of trypsin inhibitors present in these seeds (Pusztai, 1972;Seidl, Jaffe and Jaffe, 1969). Their subcellular location could not therefore be determined unequivocally from activity determinations alone.…”

Section: Discussionmentioning

confidence: 98%

COMPARTMENTALIZATION IN THE COTYLEDONARY CELLS OF PHASEOLUS VULGARIS L. SEEDS: A DIFFERENTIAL SEDIMENTATION STUDY

Pusztai¹,

Croy

Grant³

et al. 1977

New Phytologist

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SUMMARYThe appearance and the yield of sedimentable organelles from the cotyledons of Phaseolus vulgaris L. were measured with respect to the influence of the method of homogenization, the choice of dry or imbibed seeds, and the composition and the concentration of the homogenization medium. Sucrose, (0.2-0.8 M), the addition of Mg^"" (2 X 10~^M) or EDTA (3 X 10~^M) or the replacement of sucrose with mannitol made little difference to the average size distribution or the amount recovered of the 21 000 ^^v ^ 10 min pelleted organelles, the main protein body-containing fraction of the homogenate. Slicing the imbibed seeds with a razor blade or by a mechanical rotary cutter combined with a short extraction was the gentlest and the most efficient method for the production of organelles. Cell homogenates were fractionated on the basis of size by differential sedimentation into several subcellular fractions. These included a residue, starch particles (300 ^ X 10 min), a main protein body fraction (21 000 ^^v X 10 min), 38 000 ^av^ 60 min pellets, 78 000 ^av X 240 min pellets and a final supernatant. The activity in these fractions of several catabolic enzymes was measured. Most of the activity of the acidic nucleases, amylases, the BAPA-ase and a substantial part of the acidic phosphatase and the cathepsin A-type enzyme(s) were found in the supernatant, while no specific DNA-ase was found in these seeds. Protein bodies contained some of the trypsin inhibitors and most (if not all) of the lectins and Glycoprotein II. Most of the endopeptidase (azoproteinase) activity of the cotyledons appeared to be tightly bound to the cell walls or to other insoluble structural elements. Protein bodies and other intracellular organelles had very little autolytic activity and, thus, the main storage proteins of the seed were not degraded during the first 4 days of germination.

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Digestibility and proteinase inhibitory action of a kidney bean globulin

Abstract: A globulin fraction, isolated from black beans (.Phaseolus vulgaris), was resistant to hydrolysis by pepsin, trypsin, chymotrypsin, papain, ficin, hurain, and subtilisin. After denaturation of the globulin

Cited by 40 publications

References 10 publications

The action of trypsin and chymotrypsin on the reserve proteins of some leguminous seeds

The action of trypsin and chymotrypsin on the reserve proteins of some leguminous seeds

Comparative performance analysis of enzyme inactivation of soy milk by using RSM and ANN

COMPARTMENTALIZATION IN THE COTYLEDONARY CELLS OF PHASEOLUS VULGARIS L. SEEDS: A DIFFERENTIAL SEDIMENTATION STUDY

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