The isolation and characterization of a trypsin inhibitor from Kintoki bean (Phaseolus vulgaris).

Miyoshi, Masamitsu; Hamaguchi, Yoichi; Matsumoto, Keiko; Mizuno, Izumi

doi:10.3177/jnsv.24.195

Cited by 10 publications

(16 citation statements)

References 6 publications

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“…All three bean samples had at least an 80% reduction in TI activity ( Table 1). The slightly higher TI level in the acidic beans could be predicted, since Miyoshi et al (1978) and Marquez and Lajolo (1981) found that TI is most stable at low pHs and very unstable at high pHs.…”

Section: Results and Discussion Processing Whole Beansmentioning

confidence: 92%

“…A second reason for the low Cys levels could be the loss of the (&s-rich trypsin inhibitor, which leached into the soaking water. The TI from cultivars of Phaseolus vulgaris contain up to 14% Cys by weight, (Pusztai, 1966;Miyoshi et al, 1978).…”

Section: Amino Acid Analysismentioning

confidence: 99%

“…There appears to be a significant relationship between pH and trypsin inhibitor (TI) inactivation. Miyoshi et al (1978) and Marquez and Lajolo (1981) have demonstrated that about 75% of the TI remains active in varieties of Phaseolus vulgaris beans after heating for 1 to 4 hr at 100°C under acidic conditions. Under alkaline conditions the TI was easily destroyed.…”

Section: Introductionmentioning

confidence: 98%

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Nutritional Quality of Great Northern Bean Proteins Processed at Varying pH

Eicher

Saiterlee

1988

Journal of Food Science

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Heating whole dry beans at pH well above or below their average protein isoelectric point of 6.3, results in significant increases in protein digestibility, as measured by the rat NPR assay. Yet the nutritional quality of these pH-adjusted beans was lower than that for conventionally cooked dry beans due to the loss of cysteine/cystine (Cys) from the beans during the long pH adjustment step as well as the increased sensitivity of Cys to heat at alkaline pHs. In contrast pH adjusted bean flour slurries, after rapidly drying (40 set) on a double drum drier, yielded products having a high protein digestibility (>80%), low trypsin inhibitor content (< 1Omg TI/g protein) and showing little or no loss of Cys.

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Section: Results and Discussion Processing Whole Beansmentioning

confidence: 92%

Section: Amino Acid Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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Nutritional Quality of Great Northern Bean Proteins Processed at Varying pH

Eicher

Saiterlee

1988

Journal of Food Science

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“…White cloud bean trypsin inhibitors demonstrate antiproliferative activity against tumor cells but do no inhibit mycelial growth or HIV-1 reverse transcriptase. Previously isolated P. vulgaris trypsin inhibitors have not been so tested [60][61][62][63][64]. They reportedly have a molecular mass of about 9 kDa [63,65] or 13 kDa [61], smaller than the value of 16 kDa obtained for white cloud bean trypsin inhibitors…”

Section: Journal Of Biomedicine and Biotechnologymentioning

confidence: 88%

Trypsin Isoinhibitors with Antiproliferative Activity toward Leukemia Cells fromPhaseolus vulgariscv “White Cloud Bean”

Jian

Wang

2010

Journal of Biomedicine and Biotechnology

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A purification protocol that comprised ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose, and gel filtration by FPLC on Superdex 75 was complied to isolate two trypsin inhibitors from Phaseolus vulgaris cv “White Cloud Bean”. Both trypsin inhibitors exhibited a molecular mass of 16 kDa and reduced the activity of trypsin with an IC50 value of about 0.6 μM. Dithiothreitol attenuated the trypsin inhibitory activity, signifying that an intact disulfide bond is indispensable to the activity. [Methyl-3H] thymidine incorporation by leukemia L1210 cells was inhibited with an IC50 value of 28.8 μM and 21.5 μM, respectively. They were lacking in activity toward lymphoma MBL2 cells and inhibitory effect on HIV-1 reverse transcriptase and fungal growth when tested up to 100 μM.

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“…Whereas after fermentation for 14 days the total TI in the seeds had decreased by 364.26mg, its increase in the brine was 147.40mg which is approximately 40% of the TI lost from the seeds. Ideally one would expect the amount of TI lost from the seeds to be more or less similar to levels found in the brine since TI, are known to be stable under acidic conditions (Miyoshi et al, 1978;Marquez & Lajolo, 1981). As this was not the case, it is evident that there are other factors responsible for TI losses in seeds besides leaching.…”

Section: Trypsin Inhibitor Thiamine Riboflavin Pmtein Treatment (Mg/gmentioning

confidence: 93%

Nutritional quality of green beans (var. Tuf) fermented with starter culture

Mnkeni

Gierschner

Maeda

1996

International Journal of Food Sciences and Nutrition

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Green beans (var. Tuf) were blanched at 90 degrees C for 20 min and then fermented in 3.08% salt solution with starter culture. Trypsin inhibitors, vitamins B1 and B2 and protein were determined before and during fermentation as well as after storage for 36 days. Trypsin inhibitors, vitamins B1 and B2 were reduced significantly (P < or = 0.05) during fermentation. A decrease in protein content was observed during the first 2 days of fermentation and thereafter the decrease was not significant (P > or = 0.05). Storage of pasteurised beans at 20 degrees for 36 days had no significant effect on the vitamins and protein.

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The isolation and characterization of a trypsin inhibitor from Kintoki bean (Phaseolus vulgaris).

Cited by 10 publications

References 6 publications

Nutritional Quality of Great Northern Bean Proteins Processed at Varying pH

Nutritional Quality of Great Northern Bean Proteins Processed at Varying pH

Trypsin Isoinhibitors with Antiproliferative Activity toward Leukemia Cells fromPhaseolus vulgariscv “White Cloud Bean”

Nutritional quality of green beans (var. Tuf) fermented with starter culture

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