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Heidar-ali Tajmir-riahi - One of the best experts on this subject based on the ideXlab platform.
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Aggregation of Trypsin and Trypsin Inhibitor by Al cation.
Journal of Photochemistry and Photobiology B-biology, 2017Co-Authors: P. Chanphai, Laurent Kreplak, Heidar-ali Tajmir-riahiAbstract:Abstract Al cation may trigger protein structural changes such as aggregation and fibrillation, causing neurodegenerative diseases. We report the effect of Al cation on the solution structures of Trypsin (try) and Trypsin Inhibitor (tryi), using thermodynamic analysis, UV–Visible, Fourier transform infrared (FTIR) spectroscopic methods and atomic force microscopy (AFM). Thermodynamic parameters showed Al-protein bindings occur via H-bonding and van der Waals contacts for Trypsin and Trypsin Inhibitor. AFM showed that Al cations are able to force Trypsin into larger or more robust aggregates than Trypsin Inhibitor, with Trypsin 5 ± 1 SE ( n = 52) proteins per aggregate and for Trypsin Inhibitor 8.3 ± 0.7 SE ( n = 118). Thioflavin T test showed no major protein fibrillation in the presence of Al cation. Al complexation induced more alterations of Trypsin Inhibitor conformation than Trypsin.
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Aggregation of Trypsin and Trypsin Inhibitor by Al cation.
Journal of Photochemistry and Photobiology B-biology, 2017Co-Authors: P. Chanphai, Laurent Kreplak, Heidar-ali Tajmir-riahiAbstract:Abstract Al cation may trigger protein structural changes such as aggregation and fibrillation, causing neurodegenerative diseases. We report the effect of Al cation on the solution structures of Trypsin (try) and Trypsin Inhibitor (tryi), using thermodynamic analysis, UV–Visible, Fourier transform infrared (FTIR) spectroscopic methods and atomic force microscopy (AFM). Thermodynamic parameters showed Al-protein bindings occur via H-bonding and van der Waals contacts for Trypsin and Trypsin Inhibitor. AFM showed that Al cations are able to force Trypsin into larger or more robust aggregates than Trypsin Inhibitor, with Trypsin 5 ± 1 SE ( n = 52) proteins per aggregate and for Trypsin Inhibitor 8.3 ± 0.7 SE ( n = 118). Thioflavin T test showed no major protein fibrillation in the presence of Al cation. Al complexation induced more alterations of Trypsin Inhibitor conformation than Trypsin.
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Conjugation of biogenic and synthetic polyamines with Trypsin and Trypsin Inhibitor
RSC Advances, 2016Co-Authors: P. Chanphai, Thekkumkat Thomas, Heidar-ali Tajmir-riahiAbstract:Polyamine–protein conjugates can be used as delivery tools to transport antitumor polyamine analogues. We report the conjugation of Trypsin and Trypsin Inhibitor with biogenic polyamines spermine (spm), spermidine (spmd) and synthetic polyamines 3,7,11,15-tetrazaheptadecane·4HCl (BE-333) in aqueous solution. Multiple spectroscopic methods, thermodynamic parameters and molecular modeling were used to analyse polyamine bindings to Trypsin and Trypsin Inhibitor. Thermodynamic parameters ΔS, ΔH and ΔG showed that polyamines bind protein through H-bonding and van der Waals contacts with Trypsin forming more stable conjugates than with the Trypsin Inhibitor and synthetic polyamines show stronger affinity than biogenic polyamines. Modeling showed that the polyamine–protein interaction is spontaneous and several H-bonding networks stabilize polyamine–protein conjugation.
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Chitosan nanoparticles conjugate with Trypsin and Trypsin Inhibitor.
Carbohydrate Polymers, 2016Co-Authors: P. Chanphai, Heidar-ali Tajmir-riahiAbstract:Chitosan-protein conjugates are widely used in therapeutic drug delivery. We report the bindings of chitosan nanoparticles with Trypsin (try) and Trypsin Inhibitor (tryi), using thermodynamic analysis and multiple spectroscopic methods. Thermodynamic parameters ΔS, ΔH and ΔG showed chitosan-protein bindings occur mainly via H-bonding and van der Waals contacts with Trypsin Inhibitor forming more stable conjugate than Trypsin. As chitosan size increased more stable polymer-protein conjugate was formed. Chitosan complexation induces more perturbations of Trypsin Inhibitor structure than Trypsin with reduction of protein alpha-helix and major increase of random structure. The negative value of ΔG indicates spontaneous protein-chitosan complexation at room temperature. Chitosan nanoparticles can be used to transport Trypsin and Trypsin Inhibitor.
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Trypsin and Trypsin Inhibitor bind PAMAM nanoparticles: Effect of hydrophobicity on protein–polymer conjugation
Journal of Colloid and Interface Science, 2015Co-Authors: P. Chanphai, Heidar-ali Tajmir-riahiAbstract:Abstract Protein–polymer conjugates are widely used in therapeutic drug delivery. We report the bindings of Trypsin (Try) and Trypsin Inhibitor (Tryi) with polyamidoamine (PAMAM-G4) dendrimer at physiological conditions, using thermodynamic analysis, UV–Visible and Fourier transform infrared (FTIR) spectroscopic methods. Thermodynamic parameters ΔS, ΔH and ΔG showed protein–PAMAM bindings occur via H-bonding and van der Waals contacts with Trypsin Inhibitor forming more stable conjugate than Trypsin. PAMAM complexation induces more perturbations of Trypsin Inhibitor structure than Trypsin with reduction of protein alpha-helix and major changes of beta-structures. The negative value of ΔG indicates spontaneous protein–polymer conjugation at room temperature.
Sappasith Klomklao - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of Trypsin Inhibitor from yellowfin tuna thunnus albacores roe
Journal of Food Biochemistry, 2016Co-Authors: Sappasith Klomklao, Hideki Kishimura, Kazufumi Osako, Soottawat Benjakul, Benjamin K SimpsonAbstract:Trypsin Inhibitor was purified to homogeneity from the roe of yellowfin tuna (Thunnus albacores) by heat treatment at 60C for 10 min, followed by column chromatographies on Sephacryl S-200, Sephadex G-50 and DEAE-cellulose. The Trypsin Inhibitor was purified 11.29-fold with a yield of 46.02%. Yellowfin tuna Trypsin Inhibitor migrated as a single band using native polyacrylamide gel electrophoresis. Purified Trypsin Inhibitor had an apparent molecular weight of 70 kDa when analyzed using sodium dodecyl sulfate–polyacrylamide gel electrophoresis and size exclusion chromatography. No Inhibitory activity was obtained under reducing condition of β-mercaptoethanol. Maximal activity was recorded at pH 7.0 and 50C. The purified Inhibitor was stable in the temperature range of 20–60C for 10 min and in the pH range of 5–8. NaCl concentration up to 3% did not significantly affect the Inhibitory activity of purified Trypsin Inhibitor. However, the activity decreased when Trypsin Inhibitor was incubated with metal ions (Cu+, Na+, Mg2+ and Ca2+) at ambient temperature for 30 min. Practical Applications Trypsin Inhibitor from yellowfin tuna (Thunnus albacores) roe, the by-products of tuna processing, can be purified. The yellowfin tuna Trypsin Inhibitor is a salt-stable peptide and could be useful for food applications, especially surimi.
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optimum extraction and recovery of Trypsin Inhibitor from yellowfin tuna thunnus albacores roe and its biochemical properties
International Journal of Food Science and Technology, 2014Co-Authors: Sappasith Klomklao, Soottawat Benjakul, Hideki KishimuraAbstract:Summary Effect of lipid removal, extraction medium and extraction time on the isolation and recovery of Trypsin Inhibitor from yellowfin tuna (Thunnus albacores) roe was investigated. Trypsin Inhibitor extracted from defatted tuna roe showed the higher specific Inhibitory activity than extracted from origin tuna roe. Optimal extraction medium was attained by shaking the defatted yellowfin tuna roe powder in 10 mm Na phosphate buffer (pH 7.0) containing 0.5 m NaCl (P < 0.05). The extraction time affected the Inhibitor recovery significantly (P < 0.05). The extraction time of 30 min was optimum for recovery of Trypsin Inhibitor from yellowfin tuna roe. The biochemical properties of Trypsin Inhibitor from yellowfin tuna roes were also determined. The Inhibitor was stable to heat treatment up to 60C and over a broad pH range (5-8). Increasing the concentration of salt (up to 3%, w/v) did not significantly decrease the Trypsin Inhibitory activity. However, the activity decreased when Trypsin Inhibitor was incubated with metal ions at ambient temperature for 30 min.
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extraction purification and properties of Trypsin Inhibitor from thai mung bean vigna radiata l r wilczek
Food Chemistry, 2011Co-Authors: Sappasith Klomklao, Hideki Kishimura, Soottawat Benjakul, Manat ChaijanAbstract:A Trypsin Inhibitor from mung bean (Vigna radiata (L.) R. Wilczek) seeds grown in Thailand was extracted and characterised. The optimal extraction medium was attained by shaking the defatted mung been seed powder in distilled water (P < 0.05). The extraction time affected the Inhibitor recovery significantly (P < 0.05). The extraction time of 2 h was optimum for the recovery of the Trypsin Inhibitor from mung bean seeds. The Trypsin Inhibitor from mung bean seeds was purified by heat-treatment at 90 C for 10 min, followed by ammonium sulphate precipitation with 30–65% saturation and gel filtration on Sephadex G-50. It was purified to 13.51-fold with a yield of 30.25%. Molecular weight distribution and Inhibitory activity staining showed that the purified Trypsin Inhibitor had a molecular weight of 14 kDa. However, the purified Inhibitor had no activity under reducing condition (bME). The purified Inhibitor was heat stable up to 50 min at 90 C. The Inhibitory activity was retained over a wide pH range. NaCl, at 0–3% concentration, did not influence the Inhibitory activity of the purified Trypsin Inhibitor from mung bean seeds.
Hideki Kishimura - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of Trypsin Inhibitor from yellowfin tuna thunnus albacores roe
Journal of Food Biochemistry, 2016Co-Authors: Sappasith Klomklao, Hideki Kishimura, Kazufumi Osako, Soottawat Benjakul, Benjamin K SimpsonAbstract:Trypsin Inhibitor was purified to homogeneity from the roe of yellowfin tuna (Thunnus albacores) by heat treatment at 60C for 10 min, followed by column chromatographies on Sephacryl S-200, Sephadex G-50 and DEAE-cellulose. The Trypsin Inhibitor was purified 11.29-fold with a yield of 46.02%. Yellowfin tuna Trypsin Inhibitor migrated as a single band using native polyacrylamide gel electrophoresis. Purified Trypsin Inhibitor had an apparent molecular weight of 70 kDa when analyzed using sodium dodecyl sulfate–polyacrylamide gel electrophoresis and size exclusion chromatography. No Inhibitory activity was obtained under reducing condition of β-mercaptoethanol. Maximal activity was recorded at pH 7.0 and 50C. The purified Inhibitor was stable in the temperature range of 20–60C for 10 min and in the pH range of 5–8. NaCl concentration up to 3% did not significantly affect the Inhibitory activity of purified Trypsin Inhibitor. However, the activity decreased when Trypsin Inhibitor was incubated with metal ions (Cu+, Na+, Mg2+ and Ca2+) at ambient temperature for 30 min. Practical Applications Trypsin Inhibitor from yellowfin tuna (Thunnus albacores) roe, the by-products of tuna processing, can be purified. The yellowfin tuna Trypsin Inhibitor is a salt-stable peptide and could be useful for food applications, especially surimi.
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optimum extraction and recovery of Trypsin Inhibitor from yellowfin tuna thunnus albacores roe and its biochemical properties
International Journal of Food Science and Technology, 2014Co-Authors: Sappasith Klomklao, Soottawat Benjakul, Hideki KishimuraAbstract:Summary Effect of lipid removal, extraction medium and extraction time on the isolation and recovery of Trypsin Inhibitor from yellowfin tuna (Thunnus albacores) roe was investigated. Trypsin Inhibitor extracted from defatted tuna roe showed the higher specific Inhibitory activity than extracted from origin tuna roe. Optimal extraction medium was attained by shaking the defatted yellowfin tuna roe powder in 10 mm Na phosphate buffer (pH 7.0) containing 0.5 m NaCl (P < 0.05). The extraction time affected the Inhibitor recovery significantly (P < 0.05). The extraction time of 30 min was optimum for recovery of Trypsin Inhibitor from yellowfin tuna roe. The biochemical properties of Trypsin Inhibitor from yellowfin tuna roes were also determined. The Inhibitor was stable to heat treatment up to 60C and over a broad pH range (5-8). Increasing the concentration of salt (up to 3%, w/v) did not significantly decrease the Trypsin Inhibitory activity. However, the activity decreased when Trypsin Inhibitor was incubated with metal ions at ambient temperature for 30 min.
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extraction purification and properties of Trypsin Inhibitor from thai mung bean vigna radiata l r wilczek
Food Chemistry, 2011Co-Authors: Sappasith Klomklao, Hideki Kishimura, Soottawat Benjakul, Manat ChaijanAbstract:A Trypsin Inhibitor from mung bean (Vigna radiata (L.) R. Wilczek) seeds grown in Thailand was extracted and characterised. The optimal extraction medium was attained by shaking the defatted mung been seed powder in distilled water (P < 0.05). The extraction time affected the Inhibitor recovery significantly (P < 0.05). The extraction time of 2 h was optimum for the recovery of the Trypsin Inhibitor from mung bean seeds. The Trypsin Inhibitor from mung bean seeds was purified by heat-treatment at 90 C for 10 min, followed by ammonium sulphate precipitation with 30–65% saturation and gel filtration on Sephadex G-50. It was purified to 13.51-fold with a yield of 30.25%. Molecular weight distribution and Inhibitory activity staining showed that the purified Trypsin Inhibitor had a molecular weight of 14 kDa. However, the purified Inhibitor had no activity under reducing condition (bME). The purified Inhibitor was heat stable up to 50 min at 90 C. The Inhibitory activity was retained over a wide pH range. NaCl, at 0–3% concentration, did not influence the Inhibitory activity of the purified Trypsin Inhibitor from mung bean seeds.
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Isolation and characteristics of Trypsin Inhibitor from the hepatopancreas of a squid (Todarodes pacificus).
Comparative biochemistry and physiology. Part B Biochemistry & molecular biology, 2001Co-Authors: Hideki Kishimura, Hiroki Saeki, Kenji HayashiAbstract:Trypsin Inhibitor was purified from the hepatopancreas of squid (Todarodes pacificus). The final Inhibitor preparation was nearly homogeneous by SDS-PAGE with an estimated molecular weight of approximately 6300. The squid Trypsin Inhibitor was acid- and heat-stable, and active against Trypsins from the pyloric ceca of starfish (Asterias amurensis) and saury (Cololabis saira) and porcine pancreatic Trypsin. Amino acid composition of the squid Trypsin Inhibitor was compared with other invertebrate Trypsin Inhibitors. The squid Trypsin Inhibitor inhibited the autolysis of walleye pollock (Theragra chalcogramma) myofibrillar proteins.
Vineet Kumar - One of the best experts on this subject based on the ideXlab platform.
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Comparative Assessment of Trypsin Inhibitor vis-à-vis Kunitz Trypsin Inhibitor and Bowman-Birk Inhibitor Activities in Soybean
Food Analytical Methods, 2018Co-Authors: Vineet Kumar, Anita Rani, Mohd Shuaib, Priyanka MittalAbstract:Trypsin Inhibitor activity (TIA) in soybean is attributed to two polypeptides, namely, Kunitz Trypsin Inhibitor (KTI) and Bowman-Birk Inhibitor (BBI). Standard spectrophotometric protocol widely followed for estimation of TIA is cumbersome and does not distinguish KTI from BBI. In the present investigation, extraction conditions for KTI were optimized and different forms of this polypeptide were resolved in 180 soybean genotypes of Indian and exotic origin through native PAGE. This led to the identification of three KTI alleles, namely, Ti ^ a , Ti ^ b , and Ti ^ c , with Ti ^ a occurring in most of the Indian genotypes. Trypsin-KTI complex assay exhibited binding of Ti ^ a polypeptide with 2.51 fold concentration of Trypsin. Subsequently, seeds of selected genotypes were subjected to estimation of KTI and BBI activity through densitometry and enzyme-linked immunosorbent assay (ELISA), respectively; and total TIA through standard spectrophotometric protocol. Summation of KTI and BBI was significantly ( P
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comparative assessment of Trypsin Inhibitor vis a vis kunitz Trypsin Inhibitor and bowman birk Inhibitor activities in soybean
Food Analytical Methods, 2018Co-Authors: Vineet Kumar, Anita Rani, Mohd Shuaib, Priyanka MittalAbstract:Trypsin Inhibitor activity (TIA) in soybean is attributed to two polypeptides, namely, Kunitz Trypsin Inhibitor (KTI) and Bowman-Birk Inhibitor (BBI). Standard spectrophotometric protocol widely followed for estimation of TIA is cumbersome and does not distinguish KTI from BBI. In the present investigation, extraction conditions for KTI were optimized and different forms of this polypeptide were resolved in 180 soybean genotypes of Indian and exotic origin through native PAGE. This led to the identification of three KTI alleles, namely, Tia, Tib, and Tic, with Tia occurring in most of the Indian genotypes. Trypsin-KTI complex assay exhibited binding of Tia polypeptide with 2.51 fold concentration of Trypsin. Subsequently, seeds of selected genotypes were subjected to estimation of KTI and BBI activity through densitometry and enzyme-linked immunosorbent assay (ELISA), respectively; and total TIA through standard spectrophotometric protocol. Summation of KTI and BBI was significantly (P < 0.05) lower than that of TIA determined through the spectrophotometric method.
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deployment of gene specific marker in development of kunitz Trypsin Inhibitor free soybean genotypes
Indian Journal of Experimental Biology, 2013Co-Authors: Vineet Kumar, Anita Rani, Reena RawalAbstract:Genetic elimination of kunitz Trypsin Inhibitor in soybean seed would obviate the need for boiling required to inactivate the antinutritional factor and therefore economize the soy processing. PI542044, the source of null variant of kunitz Trypsin Inhibitor gene is being used in the development of kunitz Trypsin Inhibitor free soybean genotypes in India. Gene specific marker can expedite the genetic elimination of this undesirable trait from popular soybean genotypes. In the present study, w e tested the DNA amplification of soybean genotype PI542044 and kunitz Trypsin Inhibitor null lines derived from this genotype with a gene specific primer developed from the null variant of PI157740. The amplicons so obtained corresponded to the absence of kunitz Trypsin Inhibitor protein band on 10% polyacrylamide gel. The gene specific marker also amplified the null allele of template DNA of F1, BC1F1 and BC2F1 plants developed during marker assisted introgression of null allele of kunitz Trypsin Inhibitor into elite soybean cultivar JS97-52. The results presented show the utility of this gene specific marker developed from null allele of kunitz Trypsin Inhibitor for identification of kunitz Trypsin Inhibitor free genotypes developed from PI542044, the only source of null variant available in India.
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lipoxygenase isozymes and Trypsin Inhibitor activities in soybean as influenced by growing location
Food Chemistry, 2003Co-Authors: Vineet Kumar, Anita Rani, Chanda Tindwani, Mukti JainAbstract:Abstract Lipoxygenase isozymes, responsible for the off-flavour associated with soy-based foods, and Trypsin Inhibitor, that affects protein digestibility, are two undesirable biological components present in soybean. The information on influence of growing location on lipoxygenase isozymes and Trypsin Inhibitor is negligible. The dry seeds of seven Indian soybean varieties, grown at four locations widely differing in latitude and therefore climate, were evaluated for isozymes of lipoxygenase and Trypsin Inhibitor. Variation in different varieties, at different locations, for the activities of lipoxygenase-I and lipoxygenase-II+III ranged from 450 to 2042 and 118 to 600 units per gramme of soy flour, respectively, while, for Trypsin Inhibitor, it varied from 42 to 113 mg per gramme of soy flour. Averaged over seven genotypes, Palampur, the coolest location, showed maximum mean values for Lox-I as well as Lox-II+III, indicating the influence of minimum mean temperature prevalent from flowering to maturity on lipoxygenase activitity. Genotypic, locational and genotypic×locational variations were found to be significant for Lox-I as well as Lox-II+III activity. Genotypic variation and genotypic×locational interaction were found to be significant for Trypsin Inhibitor activity.
Soottawat Benjakul - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of Trypsin Inhibitor from yellowfin tuna thunnus albacores roe
Journal of Food Biochemistry, 2016Co-Authors: Sappasith Klomklao, Hideki Kishimura, Kazufumi Osako, Soottawat Benjakul, Benjamin K SimpsonAbstract:Trypsin Inhibitor was purified to homogeneity from the roe of yellowfin tuna (Thunnus albacores) by heat treatment at 60C for 10 min, followed by column chromatographies on Sephacryl S-200, Sephadex G-50 and DEAE-cellulose. The Trypsin Inhibitor was purified 11.29-fold with a yield of 46.02%. Yellowfin tuna Trypsin Inhibitor migrated as a single band using native polyacrylamide gel electrophoresis. Purified Trypsin Inhibitor had an apparent molecular weight of 70 kDa when analyzed using sodium dodecyl sulfate–polyacrylamide gel electrophoresis and size exclusion chromatography. No Inhibitory activity was obtained under reducing condition of β-mercaptoethanol. Maximal activity was recorded at pH 7.0 and 50C. The purified Inhibitor was stable in the temperature range of 20–60C for 10 min and in the pH range of 5–8. NaCl concentration up to 3% did not significantly affect the Inhibitory activity of purified Trypsin Inhibitor. However, the activity decreased when Trypsin Inhibitor was incubated with metal ions (Cu+, Na+, Mg2+ and Ca2+) at ambient temperature for 30 min. Practical Applications Trypsin Inhibitor from yellowfin tuna (Thunnus albacores) roe, the by-products of tuna processing, can be purified. The yellowfin tuna Trypsin Inhibitor is a salt-stable peptide and could be useful for food applications, especially surimi.
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optimum extraction and recovery of Trypsin Inhibitor from yellowfin tuna thunnus albacores roe and its biochemical properties
International Journal of Food Science and Technology, 2014Co-Authors: Sappasith Klomklao, Soottawat Benjakul, Hideki KishimuraAbstract:Summary Effect of lipid removal, extraction medium and extraction time on the isolation and recovery of Trypsin Inhibitor from yellowfin tuna (Thunnus albacores) roe was investigated. Trypsin Inhibitor extracted from defatted tuna roe showed the higher specific Inhibitory activity than extracted from origin tuna roe. Optimal extraction medium was attained by shaking the defatted yellowfin tuna roe powder in 10 mm Na phosphate buffer (pH 7.0) containing 0.5 m NaCl (P < 0.05). The extraction time affected the Inhibitor recovery significantly (P < 0.05). The extraction time of 30 min was optimum for recovery of Trypsin Inhibitor from yellowfin tuna roe. The biochemical properties of Trypsin Inhibitor from yellowfin tuna roes were also determined. The Inhibitor was stable to heat treatment up to 60C and over a broad pH range (5-8). Increasing the concentration of salt (up to 3%, w/v) did not significantly decrease the Trypsin Inhibitory activity. However, the activity decreased when Trypsin Inhibitor was incubated with metal ions at ambient temperature for 30 min.
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extraction purification and properties of Trypsin Inhibitor from thai mung bean vigna radiata l r wilczek
Food Chemistry, 2011Co-Authors: Sappasith Klomklao, Hideki Kishimura, Soottawat Benjakul, Manat ChaijanAbstract:A Trypsin Inhibitor from mung bean (Vigna radiata (L.) R. Wilczek) seeds grown in Thailand was extracted and characterised. The optimal extraction medium was attained by shaking the defatted mung been seed powder in distilled water (P < 0.05). The extraction time affected the Inhibitor recovery significantly (P < 0.05). The extraction time of 2 h was optimum for the recovery of the Trypsin Inhibitor from mung bean seeds. The Trypsin Inhibitor from mung bean seeds was purified by heat-treatment at 90 C for 10 min, followed by ammonium sulphate precipitation with 30–65% saturation and gel filtration on Sephadex G-50. It was purified to 13.51-fold with a yield of 30.25%. Molecular weight distribution and Inhibitory activity staining showed that the purified Trypsin Inhibitor had a molecular weight of 14 kDa. However, the purified Inhibitor had no activity under reducing condition (bME). The purified Inhibitor was heat stable up to 50 min at 90 C. The Inhibitory activity was retained over a wide pH range. NaCl, at 0–3% concentration, did not influence the Inhibitory activity of the purified Trypsin Inhibitor from mung bean seeds.
