T2327
Trypsin inhibitor
lyophilized powder, ≥95% (Kunitz inhibitor, SDS-PAGE)
Synonym(s):
Kunitz Inhibitor
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product name
Trypsin Inhibitor from Glycine max (soybean), BioUltra, lyophilized powder, ≥95% (Kunitz inhibitor, SDS-PAGE)
biological source
Glycine max (soybean)
product line
BioUltra
Assay
≥95% (Kunitz inhibitor, SDS-PAGE)
form
lyophilized powder
storage temp.
2-8°C
Related Categories
General description
Trypsin Inhibitor from Glycine max (soybean) also known as Kunitz trypsin inhibitor is a 21 kDa protein with a single trypsin binding reactive site.
Application
Trypsin Inhibitor from Glycine max (soybean) has been used:
- as a standard protein to measure the amount of endogenous trypsin inhibitor present in midgut lysate (M1) of Riptortus pedestris
- as a standard to compare the trypsin inhibitory activity of the purified protein
- to monitor the trypsin inhibitory activity by fractionating in MonoS cation exchange chromatography
- as an trypsin inhibitor
Biochem/physiol Actions
Soybean trypsin inhibitor inhibits trypsin and to a lesser extent chymotrypsin and plasmin. It forms a 1:1 stoichiometric complex with trypsin. Upon formation of this complex, trypsin may cleave a single arginine-isoleucine bond in the inhibitor. Dissociation of this complex may yield the modified form or the native inhibitor. At the optimal pH for trypsin binding (pH 8.0), the association constant is ≥ 10x108.
Trypsin Inhibitor from Glycine max (soybean) binds with the active site of trypsin enzyme, in a competitive inhibition manner.
Unit Definition
One trypsin unit will produce a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C; reaction volume 3.2 ml, 1 cm light path.
Preparation Note
Further purification of T9128 yielding an electrophoretically pure Kunitz inhibitor with increased activity.
Trypsin inhibitor is soluble in water and phosphate buffers at concentrations of 10 mg/ml or higher. Solutions at higher concentrations may be hazy and have a yellow to amber color.
Analysis Note
One mg will inhibit ≥1.0 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein.
Other Notes
View more information on Trypsin Inhibitor.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Xingfei Li et al.
Journal of agricultural and food chemistry, 66(17), 4439-4448 (2018-03-23)
We first observed that protein/polysaccharide interaction exhibited noninteracting behavior which makes Bowman-Birk chymotrypsin inhibitor (BBI) always free of complexation, being separated from another protein with similar isoelectric points, Kunitz trypsin inhibitor (KTI). Turbidity titrations showed that the electrostatic attractions were
Functional analysis of the Kunitz trypsin inhibitor family in poplar reveals biochemical diversity and multiplicity in defense against herbivores
Major IT and Constabel CP
Plant Physiology, 146(3), 888-903 (2008)
A continuous fluorometric assay for trypsin based on melittin and the noncovalent-binding-induced pyrene excimer
Xu N, et al.
Chemistry Letters (Jpn), 42(12), 1528-1530 (2013)
A midgut lysate of the Riptortus pedestris has antibacterial activity against LPS O-antigen-deficient Burkholderia mutants
Am Jang H, et al.
Developmental and Comparative Immunology, 67, 97-106 (2017)
Quantitative determination of active Bowman-Birk isoinhibitors, IBB1 and IBBD2, in commercial soymilks
Arques MC, et al.
Food Chemistry, 155, 24-30 (2014)
Chromatograms
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