Identification of the trypsin-reactive site of the Bowman-Birk soybean inhibitor

Seidl, Dinah S.; Liener, Irvin E.

doi:10.1016/0005-2795(71)90063-8

Cited by 27 publications

(5 citation statements)

References 28 publications

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“…The trypsin inhibitory activity of SBTI/WBTI decreased sharply with increasing amounts of maleic anhydride added. These results suggested the involvement of the Lys residues in the interaction between SBTI/WBTI and trypsin, in agreement with previous reports (Seidl and Liener 1971;Shivaraj and Pattabiraman 1998). Taken together, the amino acid composition, binding with trypsin and chymotrypsin, and the involvement of Lys residues in the active site for trypsin inhibition activity confirmed that SBTI and WBTI from cultivated and wild-type soybean can be classed as Bowman-Birk TI.…”

Section: Resultssupporting

confidence: 93%

“…The results are given in Table 1. The amino acid compositions of SBTI/ WBTI, trypsin/chymotrypsin-SBTI/WBTI, and trypsin-SBTI/WBTI-chymotrypsin agreed with the theoretical values of the BBI from other Leguminosae and their complexes (Wilcox 1970;Seidl and Liener 1971;Sessa and Nelsen 1991). These results suggest that SBTI/WBTI could also form a 1:1 molar complex with either trypsin or chymotrypsin and a 1:1:1 molar complex with both enzymes, confirming that the SBTI/WBTI belong to the BBI.…”

Section: Resultssupporting

confidence: 82%

“…In addition, A. flavus conidia also showed significant growth inhibition when they were treated with a lower concentration of exogenous α-amylase (5.0 μg/ml) plus 1.8 μM SBTI/WBTI (the mycelium diameter of A. flavus was about 3.1/2.6 mm). In contrast, the mycelium diameter of A. flavus with SBTI/ WBTI (1.8 μM) plus higher exogenous α-amylase (40 μg/ Seidl and Liener (1971) and Sessa and Nelsen (1991) b Values obtained by amino acid analysis as described in the text c Theoretical values taken from Seidl and Liener (1971) d Theoretical values taken from Seidl and Liener (1971) and Wilcox (1970) Fig. Alpha-amylase is an important hydrolyzing enzyme for breaking down starch to produce reducing sugar, the amount of which can be used to determine the activity levels of secreted α-amylase.…”

Section: Sbti and Wbti Inhibit α-Amylase Activity And Aflatoxin B 1 Pmentioning

confidence: 85%

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Inhibition of endogenous α-amylase and protease of Aspergillus flavus by trypsin inhibitor from cultivated and wild-type soybean

Zhang

Wang

et al. 2010

Ann Microbiol

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The anti-Aspergillus flavus activity of trypsin inhibitor (TI) from cultivated and wild-type soybean (SBTI and WBTI) was investigated in order to confirm its ability to reduce the activity of endogenous α-amylase, protease enzymes and production of aflatoxin B 1 secreted by A. flavus. In the current study, it was demonstrated that purified SBTI/WBTI belonged to the family of Bowman-Birk TI, based on evidence from amino acid composition, the presence of two independent binding sites for trypsin and chymotrypsin, and a lysine residue as the active site for trypsin inhibition. Studying the inhibition of A. flavus showed that the effect of SBTI/SBTI on A. flavus α-amylase activity and aflatoxin B 1 production depended on TI concentration. However, no inhibitory effect was observed when sufficient exogenous α-amylase (EC 3.2.1.1, from Bacillus subtilis) was added. The resistance to A. flavus infection was partially due to the ability of SBTI/WBTI to inhibit α-amylase activity, thereby limiting the availability of hydrolyzed reducing sugar for fungal growth and further suppressing aflatoxin B 1 biosynthesis. In addition, the relationship between SBTI/WBTI levels and fungal protease expression revealed that A. flavus released a certain quantity of endogenous proteases into the culture medium, and the decreased activity of protease and production of aflatoxin B 1 suggested that the inhibition activity might also be mediated by SBTI/WBTI as A. flavus protease inhibitor activity.

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Section: Resultssupporting

confidence: 93%

Section: Resultssupporting

confidence: 82%

Section: Sbti and Wbti Inhibit α-Amylase Activity And Aflatoxin B 1 Pmentioning

confidence: 85%

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Inhibition of endogenous α-amylase and protease of Aspergillus flavus by trypsin inhibitor from cultivated and wild-type soybean

Zhang

Wang

et al. 2010

Ann Microbiol

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“…When the data on the active sites of LBI against trypsin (this paper) and chymotrypsin (Krahn and Stevens, 1970) are extrapolated5 6to the known sequence of LBI, component IV (Tan and Stevens, 1971a,b), it becomes evident that, as previously suggested (Tan and Stevens, 1971b;, these two sites are located in two homologous regions of the sequence: Ile-Pro-Ala-Gln-CMCys 4 Since the time this manuscript was first submitted for publication, the complete amino acid sequence of the Bowman-Birk inhibitor has been published (Odani et al, 1971) and its trypsin reactive site has also been identified (Seidl and Liener, 1971). Both of these papers point out the striking similarities in sequence between Bowman-Birk inhibitor and LBI, particularly with reference to their proposed antitrypsin and antichymotrypsin sites.…”

Section: Discussionmentioning

confidence: 67%

Antitrypsin site of lima bean protease inhibitor

Krahn¹,

Stevens²

1972

Biochemistry

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“…The concentration, and extent of modification, of derivatized BBI was determined by amino acid analysis. Modification of BBI by CT and TPCK-T employed methods previously described (Seidl and Liener, 1971). For purposes of calculation, a molecular weight of 8000 was assumed for BBI (Kakade et al, 1 970).…”

Section: Methodsmentioning

confidence: 99%

Equilibriums of Bowman-Birk inhibitor association with trypsin and α-chymotrypsin

Turner¹,

Liener²,

Lovrien³

1975

Biochemistry

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Association constants, enthalpies, and stoichiometries of Bowman-Birk soybean inhibitor for trypsin and alpha-chymotrypsin were measured in the pH range 4-8 at 25 degrees, 0.01 M Ca2+. The results are quoted in terms of moles of protease active sites, from active site titration. Enthalpies were obtained from calorimetry. The inhibitor was modified by carboxyl group modification, and by tryptic and chymotryptic attack. Association thermodynamics and stoichiometries of the modified inhibitors with both proteases were also determined. There is one independent site for each protease on the inhibitor protein. Modification decreases association to some extent, but does not appear to change stoichiometry or protease binding site independency. In the pH 4 region the association enthalpies are endothermic, of the order 6 kcal/mol for both trypsin and chymotrypsin. With increasing pH, the enthalpies decrease and become exothermic at pH 8 for chymotrypsin. Positive entropies, 50 cal mol-1 deg-1, occur at pH 4-5. They decrease as pH increases, but are always positive in sign. The observed to accompany the overall reaction, such as H+ transfer steps. The enthalpies and entropies probably compensate over the pH range 4-8, with a characteristic temperature of 390 plus or minus 30 degrees K. Estimates were made of the macromolecular Coulomb charge products in inhibitor-protease interaction. These range from about +5 to -60, over pH range 4-8, depending on the protease. Although intermolecular Coulombic forces cannot be easily delineated at the specific side chain level, they may operate at the macromolecule level.

show abstract

Identification of the trypsin-reactive site of the Bowman-Birk soybean inhibitor

Cited by 27 publications

References 28 publications

Inhibition of endogenous α-amylase and protease of Aspergillus flavus by trypsin inhibitor from cultivated and wild-type soybean

Inhibition of endogenous α-amylase and protease of Aspergillus flavus by trypsin inhibitor from cultivated and wild-type soybean

Antitrypsin site of lima bean protease inhibitor

Equilibriums of Bowman-Birk inhibitor association with trypsin and α-chymotrypsin

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