Effect of sonication on thermolysin hydrolysis of ovotransferrin

Bo Lei, Kaustav Majumder, Shengwen Shen, Jianping Wu

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The effect of sonication on proteolytic hydrolysis of ovotransferrin and bioactivities of the hydrolysates were investigated, and the large peptide fragments left in the hydrolysate were characterised. The results showed that sonication could increase the reactive sulphydryl groups in 5% ovotransferrin solution by 50%, although there were no improvements in the overall degree of hydrolysis. Furthermore, SDS-PAGE and reverse-phase HPLC profiles did not show difference of the treated samples. Angiotensin-converting enzyme (ACE) inhibitory activity, but not antioxidant activity, of the thermolysin hydrolysate was improved in a dose dependent manner at prolonged sonication time. Matrix assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF/MS) analysis revealed that thermolysin hydrolysate was composed of 926 peptides, of 99% having masses lower than 10. kDa and of 1% larger than 10. kDa derived from both N- and C-lobes of ovotransferrin.

Original languageEnglish (US)
Pages (from-to)808-815
Number of pages8
JournalFood Chemistry
Volume124
Issue number3
DOIs
StatePublished - Feb 1 2011

Fingerprint

Conalbumin
Thermolysin
Sonication
hydrolysates
Hydrolysis
hydrolysis
Peptide Fragments
Enzyme activity
Peptidyl-Dipeptidase A
peptides
Bioactivity
Ionization
Mass spectrometry
matrix-assisted laser desorption-ionization mass spectrometry
Polyacrylamide Gel Electrophoresis
Desorption
Mass Spectrometry
peptidyl-dipeptidase A
Lasers
Antioxidants

Keywords

  • Bioactive peptide
  • Degree of hydrolysis
  • MALDI-TOF/MS
  • Ovotransferrin
  • Sonication
  • Sulphydryl (SH) group
  • Thermolysin

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

Cite this

Effect of sonication on thermolysin hydrolysis of ovotransferrin. / Lei, Bo; Majumder, Kaustav; Shen, Shengwen; Wu, Jianping.

In: Food Chemistry, Vol. 124, No. 3, 01.02.2011, p. 808-815.

Research output: Contribution to journalArticle

Lei, Bo ; Majumder, Kaustav ; Shen, Shengwen ; Wu, Jianping. / Effect of sonication on thermolysin hydrolysis of ovotransferrin. In: Food Chemistry. 2011 ; Vol. 124, No. 3. pp. 808-815.
@article{b9a1b6030b8f481083114a2ace30a89c,
title = "Effect of sonication on thermolysin hydrolysis of ovotransferrin",
abstract = "The effect of sonication on proteolytic hydrolysis of ovotransferrin and bioactivities of the hydrolysates were investigated, and the large peptide fragments left in the hydrolysate were characterised. The results showed that sonication could increase the reactive sulphydryl groups in 5{\%} ovotransferrin solution by 50{\%}, although there were no improvements in the overall degree of hydrolysis. Furthermore, SDS-PAGE and reverse-phase HPLC profiles did not show difference of the treated samples. Angiotensin-converting enzyme (ACE) inhibitory activity, but not antioxidant activity, of the thermolysin hydrolysate was improved in a dose dependent manner at prolonged sonication time. Matrix assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF/MS) analysis revealed that thermolysin hydrolysate was composed of 926 peptides, of 99{\%} having masses lower than 10. kDa and of 1{\%} larger than 10. kDa derived from both N- and C-lobes of ovotransferrin.",
keywords = "Bioactive peptide, Degree of hydrolysis, MALDI-TOF/MS, Ovotransferrin, Sonication, Sulphydryl (SH) group, Thermolysin",
author = "Bo Lei and Kaustav Majumder and Shengwen Shen and Jianping Wu",
year = "2011",
month = "2",
day = "1",
doi = "10.1016/j.foodchem.2010.06.100",
language = "English (US)",
volume = "124",
pages = "808--815",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier Limited",
number = "3",

}

TY - JOUR

T1 - Effect of sonication on thermolysin hydrolysis of ovotransferrin

AU - Lei, Bo

AU - Majumder, Kaustav

AU - Shen, Shengwen

AU - Wu, Jianping

PY - 2011/2/1

Y1 - 2011/2/1

N2 - The effect of sonication on proteolytic hydrolysis of ovotransferrin and bioactivities of the hydrolysates were investigated, and the large peptide fragments left in the hydrolysate were characterised. The results showed that sonication could increase the reactive sulphydryl groups in 5% ovotransferrin solution by 50%, although there were no improvements in the overall degree of hydrolysis. Furthermore, SDS-PAGE and reverse-phase HPLC profiles did not show difference of the treated samples. Angiotensin-converting enzyme (ACE) inhibitory activity, but not antioxidant activity, of the thermolysin hydrolysate was improved in a dose dependent manner at prolonged sonication time. Matrix assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF/MS) analysis revealed that thermolysin hydrolysate was composed of 926 peptides, of 99% having masses lower than 10. kDa and of 1% larger than 10. kDa derived from both N- and C-lobes of ovotransferrin.

AB - The effect of sonication on proteolytic hydrolysis of ovotransferrin and bioactivities of the hydrolysates were investigated, and the large peptide fragments left in the hydrolysate were characterised. The results showed that sonication could increase the reactive sulphydryl groups in 5% ovotransferrin solution by 50%, although there were no improvements in the overall degree of hydrolysis. Furthermore, SDS-PAGE and reverse-phase HPLC profiles did not show difference of the treated samples. Angiotensin-converting enzyme (ACE) inhibitory activity, but not antioxidant activity, of the thermolysin hydrolysate was improved in a dose dependent manner at prolonged sonication time. Matrix assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF/MS) analysis revealed that thermolysin hydrolysate was composed of 926 peptides, of 99% having masses lower than 10. kDa and of 1% larger than 10. kDa derived from both N- and C-lobes of ovotransferrin.

KW - Bioactive peptide

KW - Degree of hydrolysis

KW - MALDI-TOF/MS

KW - Ovotransferrin

KW - Sonication

KW - Sulphydryl (SH) group

KW - Thermolysin

UR - http://www.scopus.com/inward/record.url?scp=77956615199&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77956615199&partnerID=8YFLogxK

U2 - 10.1016/j.foodchem.2010.06.100

DO - 10.1016/j.foodchem.2010.06.100

M3 - Article

AN - SCOPUS:77956615199

VL - 124

SP - 808

EP - 815

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

IS - 3

ER -