✦ LIBER ✦

Biochemical characteristics of trypsin inhibitor from wheat grain, Beta variety

✍ Scribed by Mossor, G. ;Skupin, J.

Publisher: John Wiley and Sons
Year: 1990
Tongue: English
Weight: 395 KB
Volume: 34
Category: Article
ISSN: 0027-769X
DOI: 10.1002/food.19900340506

No coin nor oath required. For personal study only.

✦ Synopsis

A homogenous trypsin inhibitor from wheat grain has been characterized. It is a protein of molecular weight 9105 Da and isoelectric point PI = 9.5. It belongs to arginine type inhibitors. The isolated inhibitor does neither inhibit native proteinases from wheat grain nor a-chymotrypsin, papein and pepsin. However, it inhibits some proteinases from microorganisms and moulds. It is susceptible to the action of hydrogen peroxide. The inhibitory protein consists of all amino acid residues with the largest amount of glutamic acid, proline and arginine, and the lowest of histidine and tyrosine, respectively.

📜 SIMILAR VOLUMES

Isolation and identification of trypsin

Isolation and identification of trypsin inhibitors from wheat grain, Beta variety

✍ Mossor, G. ;Skupin, J. 📂 Article 📅 1990 🏛 John Wiley and Sons 🌐 English ⚖ 417 KB

The aim of this study was the identification of trypsin inhibitors in wheat grain, Beta variety. These inhibitors in spite of other functional properties belong to the antinutrient substances. According to the elaborated procedure first, the extract showing inhibitory activity was salted out at 30-8

Some biochemical properties of trypsin i

Some biochemical properties of trypsin inhibitor type antinutrients derived from extracts of wheat grain, Beta variety

✍ Mossor, G. ;Skupin, J. 📂 Article 📅 1985 🏛 John Wiley and Sons 🌐 English ⚖ 486 KB

## Some biochemical properties of trypsin inhibitor type antinutrients derived from extracts of wheat grain, Beta variety. G. M o s s o ~ and J. Skupin Trypsin inhibitors were isolated and partially purified from wheat grain, Beta variety. The procedure for determination ofthe inhibitory activity