Skip to Content
Merck
All Photos(3)

Documents

T2327

Sigma-Aldrich

Trypsin Inhibitor from Glycine max (soybean)

BioUltra, lyophilized powder, ≥95% (Kunitz inhibitor, SDS-PAGE)

Synonym(s):

Kunitz Inhibitor

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.77

biological source

Glycine max (soybean)

Quality Level

product line

BioUltra

Assay

≥95% (Kunitz inhibitor, SDS-PAGE)

form

lyophilized powder

storage temp.

2-8°C

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.

Pictograms

Health hazard

Signal Word

Danger

Hazard 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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
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)
Quantitative determination of active Bowman-Birk isoinhibitors, IBB1 and IBBD2, in commercial soymilks
Arques MC, et al.
Food Chemistry, 155, 24-30 (2014)

Protocols

Enzymatic Assay of Trypsin Inhibitor

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service