Partial purification and some properties of a trypsin inhibitor from rice bran.

Tashiro, Misao; Maki, Zensuke

doi:10.1271/bbb1961.42.1119

Cited by 21 publications

(9 citation statements)

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“…With a dilute solution of a crude extract of TI, however, the order was pH 7 > 2 >> 10 as shown in Fig 2. Tashiro and Maki (1978) used the same conditions of pH with a crude extract of rice TI, but they found an increased rate of inactivation at pH 7 compared with our results, hence their results gave stability pH 2 > 7 >> 10. The major effect is the large decrease in stability between pH 7 and 10. which was also found on heat inactivation of TI from soya bean milk during processing (Wallace et ul 1971).…”

Section: °Csupporting

confidence: 66%

“…Earlier chemical work on heat inactivation of TI was focused on solution studies using either purified or crude TI extracts (Horiguchi and Kitagishi 1971 ;Sugiura et a1 1973;Sumathi and Pattabiraman 1977;Tashiro and Maki 1978). It was found that heat inactivation in solution was promoted by the presence of albumin or high molecular weight proteins from bean extracts (Ellenrieder et a1 1980;Tsukamoto et a1 1983).…”

Section: Introductionmentioning

confidence: 99%

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Heat stability of trypsin inhibitors in tropical root crops and rice and its significance for nutrition

1992

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Abstract:The heat stability of trypsin inhibitors from rice (Oryza sativa L), sweet potato (Ipomoea batatas (L) Lam), taro (Colocasia esculenta var esculenta ( L ) Schott), giant taro (Alocasia macrorrhiza (L) G Don) and giant swamp taro (Cyrtosperma chamissonis (Schott) Merr) was studied. Rice trypsin inhibitor (TI) occurred only in the germ, so it is absent from white rice. Taro, giant taro and giant swamp taro (but not rice or sweet potato) showed an initial large increase (one-to tenfold) in the amount of TI present on heating at about 80°C. The heat release mechanism, which was accompanied by a change to a rubbery texture in the food, amounted to a breakdown of the cellular structure making TI available for extraction. Such heat release of TI would cause partially cooked food to be deleterious for human consumption. Brown rice, sweet potato, taro and giant swamp taro contained moderate amounts of TI, which was fully inactivated when the boiled or baked food was soft enough to eat. Giant taro, however, contained 10-100 times as much TI (which in this case also inhibited chymotrypsin) as the other foods, and a boiling time of at least 30 min was needed for its inactivation.

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Section: °Csupporting

confidence: 66%

Section: Introductionmentioning

confidence: 99%

Heat stability of trypsin inhibitors in tropical root crops and rice and its significance for nutrition

1992

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“…Whereas, with rice, HORIGUCHI and KITAGISHI (5) have reported that aqueous extract of the seed inhibits trypsin and that the inhibitor is localized on the embryo. We have also reported the partial purification of a trypsin inhibitor from rice bran (6).…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a trypsin inhibitor from rice bran.

Tashiro

Maki

1979

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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“…5b. As with the rice bran trypsin inhibitor, 15) JBTI was heat labile at basic pH, although it was stable at neutral pH. Mediumstability was shown at acidic pH.…”

Section: Molecular Weightmentioning

confidence: 98%

Properties of a trypsin inhibitor from Job's-tears (Coix lacryma-jobi L. var. Ma-yuen Stapf).

Ohtsubo

Yanagi

Yanase

1985

Agricultural and Biological Chemistry

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A heat stable trypsin inhibitor was found in the bran of soft-shelled job's-tears {Coix lacrymajobi L. var. Ma-yuenStapf) seeds. This inhibitor seemed to be a simple protein, and the molecular weight was about 12,000. Similar to other heat stable trypsin inhibitors, this inhibitor also contained manycysteine or cystine residues in the molecule. This inhibitor inhibited bovine trypsin at the molar ratio of 1 to 2, showing that it was double-headed. Its activity was stable against the change of pH at the range of3 to 1 1 and high temperature of 100°C under certain conditions. However, the degree of heat stability of the inhibitory activity depended highly upon the kind of the solution in which this inhibitor was dissolved.

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Partial purification and some properties of a trypsin inhibitor from rice bran.

Cited by 21 publications

References 1 publication

Heat stability of trypsin inhibitors in tropical root crops and rice and its significance for nutrition

Heat stability of trypsin inhibitors in tropical root crops and rice and its significance for nutrition

Purification and characterization of a trypsin inhibitor from rice bran.

Properties of a trypsin inhibitor from Job's-tears (Coix lacryma-jobi L. var. Ma-yuen Stapf).

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