Isolation and characterization of ice structuring proteins from cold-acclimated winter wheat grass extract for recrystallization inhibition in frozen foods

V. Kontogiorgos, A. Regand, R. Y. Yada, H. D. Goff

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Antifreeze proteins have shown a great potential in improving the quality of frozen foods, and the isolation of proteins from natural sources that are readily available is deemed to be important. The raw leaf apoplastic extract from cold-acclimated winter wheat grass (Triticum aestivum) containing recrystallization inhibition (RI) proteins was screened for proteolytic and lipolytic activity, and a heat-stable RI protein was isolated. The enzymes detected could be easily removed by heat treatment without any loss in the RI activity. The RI protein was isolated after heat treatment of the raw extract, alcohol precipitation and separation on a size exclusion Chromatographic column. Circular dichroism indicated that the RI protein was mainly β-sheet and random coil, and these structures were preserved up to 75C. After trypsin digestion, mass fingerprinting and sequencing of the digests revealed that the protein belongs to the thaumatin-like protein group.

LanguageEnglish
Pages139-160
Number of pages22
JournalJournal of Food Biochemistry
Volume31
Issue number2
Early online date9 Mar 2007
DOIs
Publication statusPublished - 1 Apr 2007
Externally publishedYes

Fingerprint

Frozen Foods
frozen foods
Ice
Poaceae
Triticum
winter wheat
ice
grasses
extracts
Proteins
proteins
Hot Temperature
Antifreeze Proteins
heat treatment
circular dichroism spectroscopy
Circular Dichroism
Trypsin
trypsin
Digestion
Triticum aestivum

Cite this

@article{805f5426e3d04ddda0dadc06982cf5f3,
title = "Isolation and characterization of ice structuring proteins from cold-acclimated winter wheat grass extract for recrystallization inhibition in frozen foods",
abstract = "Antifreeze proteins have shown a great potential in improving the quality of frozen foods, and the isolation of proteins from natural sources that are readily available is deemed to be important. The raw leaf apoplastic extract from cold-acclimated winter wheat grass (Triticum aestivum) containing recrystallization inhibition (RI) proteins was screened for proteolytic and lipolytic activity, and a heat-stable RI protein was isolated. The enzymes detected could be easily removed by heat treatment without any loss in the RI activity. The RI protein was isolated after heat treatment of the raw extract, alcohol precipitation and separation on a size exclusion Chromatographic column. Circular dichroism indicated that the RI protein was mainly β-sheet and random coil, and these structures were preserved up to 75C. After trypsin digestion, mass fingerprinting and sequencing of the digests revealed that the protein belongs to the thaumatin-like protein group.",
author = "V. Kontogiorgos and A. Regand and Yada, {R. Y.} and Goff, {H. D.}",
year = "2007",
month = "4",
day = "1",
doi = "10.1111/j.1745-4514.2007.00112.x",
language = "English",
volume = "31",
pages = "139--160",
journal = "Journal of Food Biochemistry",
issn = "0145-8884",
publisher = "Wiley-Blackwell",
number = "2",

}

Isolation and characterization of ice structuring proteins from cold-acclimated winter wheat grass extract for recrystallization inhibition in frozen foods. / Kontogiorgos, V.; Regand, A.; Yada, R. Y.; Goff, H. D.

In: Journal of Food Biochemistry, Vol. 31, No. 2, 01.04.2007, p. 139-160.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Isolation and characterization of ice structuring proteins from cold-acclimated winter wheat grass extract for recrystallization inhibition in frozen foods

AU - Kontogiorgos, V.

AU - Regand, A.

AU - Yada, R. Y.

AU - Goff, H. D.

PY - 2007/4/1

Y1 - 2007/4/1

N2 - Antifreeze proteins have shown a great potential in improving the quality of frozen foods, and the isolation of proteins from natural sources that are readily available is deemed to be important. The raw leaf apoplastic extract from cold-acclimated winter wheat grass (Triticum aestivum) containing recrystallization inhibition (RI) proteins was screened for proteolytic and lipolytic activity, and a heat-stable RI protein was isolated. The enzymes detected could be easily removed by heat treatment without any loss in the RI activity. The RI protein was isolated after heat treatment of the raw extract, alcohol precipitation and separation on a size exclusion Chromatographic column. Circular dichroism indicated that the RI protein was mainly β-sheet and random coil, and these structures were preserved up to 75C. After trypsin digestion, mass fingerprinting and sequencing of the digests revealed that the protein belongs to the thaumatin-like protein group.

AB - Antifreeze proteins have shown a great potential in improving the quality of frozen foods, and the isolation of proteins from natural sources that are readily available is deemed to be important. The raw leaf apoplastic extract from cold-acclimated winter wheat grass (Triticum aestivum) containing recrystallization inhibition (RI) proteins was screened for proteolytic and lipolytic activity, and a heat-stable RI protein was isolated. The enzymes detected could be easily removed by heat treatment without any loss in the RI activity. The RI protein was isolated after heat treatment of the raw extract, alcohol precipitation and separation on a size exclusion Chromatographic column. Circular dichroism indicated that the RI protein was mainly β-sheet and random coil, and these structures were preserved up to 75C. After trypsin digestion, mass fingerprinting and sequencing of the digests revealed that the protein belongs to the thaumatin-like protein group.

UR - http://www.scopus.com/inward/record.url?scp=33847736199&partnerID=8YFLogxK

U2 - 10.1111/j.1745-4514.2007.00112.x

DO - 10.1111/j.1745-4514.2007.00112.x

M3 - Article

VL - 31

SP - 139

EP - 160

JO - Journal of Food Biochemistry

T2 - Journal of Food Biochemistry

JF - Journal of Food Biochemistry

SN - 0145-8884

IS - 2

ER -