Thermal denaturation of genetic variants of the kunitz soybean trypsin inhibitor

Sanderson, James E.; Freed, Robert; Ryan, Dale S.

doi:10.1016/0167-4838(82)90119-4

Cited by 12 publications

(4 citation statements)

References 15 publications

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“…The twophase inactivation feature for TIA could be explained by the difference in heat stability of Kunitz and Bowman-Birk inhibitors (Obara and Watanabe, 1971;Anderson, 1992). In addition, Sanderson et al, (1982) suggested that thermal denaturation of Kunitz inhibitor is not a simple two-state process and that a significant levels of at least one intermediate form must accumulate during denaturation.…”

Section: Effect Of Thermal Treatmentsmentioning

confidence: 99%

Inactivation of Trypsin Inhibitor Activity from Brazilian Varieties of Beans (Phaseolus vulgaris L.)

Jourdan

Noreña

Brandelli

2007

Food sci. technol. int.

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The trypsin inhibitor activity (TIA) of five varieties of beans ( Phaseolus vulgaris L.) namely, Carioca, Branco, Vermelho, Preto and Jalo, was investigated. No significant differences of TIA among varieties of raw beans were observed (P > 0.05). Pressure-cooking (121°C and 141 kPa) for 15 min resulted in complete inactivation of TIA. On cooking beans in water bath (90°C, 15 min), the TIA was inactivated between 80% and 95%, while total inactivation was achieved after 40 min suggesting the possibility of two-step inactivation kinetics. Microwave treatment was very effective for inactivation of this antinutritional factor (97% to 100% of inactivation) in the first 15 min of treatment. A 22 factorial design was developed to evaluate the effect of temperature and duration of thermal treatment for loss of TIA. As interdependence between temperature and time was evident, it is envisaged that both are important to process the beans to knock off TIA.

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Section: Effect Of Thermal Treatmentsmentioning

confidence: 99%

Inactivation of Trypsin Inhibitor Activity from Brazilian Varieties of Beans (Phaseolus vulgaris L.)

Jourdan

Noreña

Brandelli

2007

Food sci. technol. int.

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“…Wu and Scheraga (1962) observed tha&,T for KSTI ranged between 40C (pH 1) and 60C (pH 7). Sanderson et al (1982) found that KSTI unfolded with a T, of 64C in high ionic strength solvent (0.02 phosphate buffer pH 7, with 0.3M KC1). Donovan and Beardslee (1975) examined the heat unfolding of KSTI and the KSTI-trypsin complex using DSC.…”

Section: Heat Unfolding Of Kstimentioning

confidence: 99%

“…Unprocessed foods may contain a range of undesirable biologically active peptides or proteins (BAPP) including, allergenic proteins, opioid peptides, dimensional structures of crystalline KSTI and the KSTI-trypsin complex have been elucidated (Sweet et al 1974;Bode and Huber 1992). Some heat unfolding studies, though not using fluorescence measurements, have been also reported for KSTI (Wu and Scheraga 1962;Sanderson et al 1982).…”

Section: Introductionmentioning

confidence: 99%

The Heat Resistance and Conformational Plasticity of Kunitz Soybean Trypsin Inhibitor

Owusu‐Apenten

Mahadevan

1999

J Food Biochemistry

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The heat resistance of Kunitz soybean trypsin inhibitor (KSTI) and the conformational plasticity of the purified protein were examined in Tris‐HCI buffer (0.05M, pH 8). The rate of KSTI inactivation at moderate temperatures 70–100C was slow. The time for 90% inactivation (D‐value) of KSTI at 120–150C ranged between 81s–1047s. The activation enthalpy (ΔS) and entropy (ΔS#) change for ultrahigh temperature (UHT) inactivation of KSTI was 107 kj mot‐1 and ‐26 J mol‐1, respectively. Fluorescence monitoring of KSTI structure showed a conformational change at 30–70C with a mid‐point temperature (Tm) of 55.6C. The heat induced structural change was fully reversible. There was complete regain of the KSTI native structure after heating at 80C, as judged from intrinsic fluorescence measurements. The results are considered in relation to the Lumry‐Eyring 2‐stage scheme protein inactivation. The UHT resistance of KSTI may be ascribed to its conformation plasticity which allows efficient regain of its native structure after heat unfolding. Other possible causes of heat resistance in biologically active proteins and peptides (BAPP) are briefly discussed.

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“…The success indicator for heat processing is urease, a thermolabile enzyme. Decrease of its activity under the influence of heat in relation to untreated full fat soybean indicates successful processing (Sanderson et al, 1982;Miranda et al, 1999;Trugo et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Nutritional characteristics of soybean after thermal processing by toasting

Krička¹,

Jukić²,

Voća³

et al. 2003

Acta vet. (Beogr.)

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This paper deals with the characteristics of soybean processed by a new technical version of the toaster aimed to be used for small amounts. The research was conducted on a thin and a thick layer of soybean, and the results indicate that only a thin layer can be toasted satisfactorily due to large differences in urease activity ranging from 0.01 to 0.26 mgN/g/min and trypsin inhibitor activity (2.53 to 4.04 mg/g) in thick layers. Further more, it was determined that after toasting a thin layer of soybean at the temperatures of 125oC, 130oC and 135oC for 10- and 15-minute periods, the most favorable treatment for monogastric animals was 125oC/15min (2.12 mgTI/g trypsin inhibitor activity), and for polygastric (ruminant) animals 130oC/10 min (0.00 mgN/g/min urease)

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Thermal denaturation of genetic variants of the kunitz soybean trypsin inhibitor

Cited by 12 publications

References 15 publications

Inactivation of Trypsin Inhibitor Activity from Brazilian Varieties of Beans (Phaseolus vulgaris L.)

Inactivation of Trypsin Inhibitor Activity from Brazilian Varieties of Beans (Phaseolus vulgaris L.)

The Heat Resistance and Conformational Plasticity of Kunitz Soybean Trypsin Inhibitor

Nutritional characteristics of soybean after thermal processing by toasting

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