Expression, characterization, and biologic activity of recombinant human lactoferrin in rice

Yasushi A. Suzuki, Shannon L. Kelleher, Dorice Yalda, Liying Wu, Jianmin Huang, Ning Huang, Bo Lönnerdal

Research output: Contribution to journalArticle

76 Citations (Scopus)

Abstract

Background: Lactoferrin has been suggested to have many biologic activities, such as facilitating iron absorption and having antimicrobial and antiinflammatory effects. In humans, several of these activities are likely to only be facilitated by human lactoferrin because they depend on the binding of human lactoferrin to specific receptors. Rice may be a useful vehicle to introduce recombinant human lactoferrin to infant foods because it has low allergenicity and is likely to be safer than using microorganisms or transgenic animals. Methods: Recombinant human lactoferrin was expressed in the rice cell culture system, and its biologic activity was assessed by iron-binding and -releasing properties, antimicrobial activity, and binding and uptake to Caco-2 cells. The authors also compared the stability of recombinant and native human lactoferrins against heat, low pH, and in vitro digestion. Results: Biologic activity of rice-expressed recombinant human lactoferrin was similar to that of native human lactoferrin. Heat-treated proteins retained their functional activities except with severe treatment at 100°C for 8 seconds, which disturbed the iron-binding capacity of recombinant human lactoferrin. Both types of proteins retained their functional activities between pH 2 and 7.4. After in vitro digestion, 50% of both proteins were detectable by enzyme linked immunosorbent assay. The remaining native and recombinant lactoferrins retained antimicrobial and Caco-2 binding and uptake activities. Conclusions: The results indicate recombinant human lactoferrin has stability similar to native human lactoferrin when exposed to thermal treatment, pH treatment, and in vitro digestion, suggesting it may be active when added to infant formula.

Original languageEnglish (US)
Pages (from-to)190-199
Number of pages10
JournalJournal of Pediatric Gastroenterology and Nutrition
Volume36
Issue number2
DOIs
StatePublished - Feb 2003

Fingerprint

Lactoferrin
lactoferrin
Human Activities
bioactive properties
rice
in vitro digestion
Population Groups
Digestion
Iron
Hot Temperature
anti-infective properties
Oryza
Infant Food
iron
uptake mechanisms
heat
allergenicity
transgenic animals
Infant Formula
Genetically Modified Animals

Keywords

  • Antimicrobial activity
  • Caco-2 cells
  • Infant formula
  • Iron
  • Recombinant human lactoferrin
  • Transgenic rice

ASJC Scopus subject areas

  • Gastroenterology
  • Histology
  • Medicine (miscellaneous)
  • Food Science
  • Pediatrics, Perinatology, and Child Health

Cite this

Expression, characterization, and biologic activity of recombinant human lactoferrin in rice. / Suzuki, Yasushi A.; Kelleher, Shannon L.; Yalda, Dorice; Wu, Liying; Huang, Jianmin; Huang, Ning; Lönnerdal, Bo.

In: Journal of Pediatric Gastroenterology and Nutrition, Vol. 36, No. 2, 02.2003, p. 190-199.

Research output: Contribution to journalArticle

Suzuki, Yasushi A. ; Kelleher, Shannon L. ; Yalda, Dorice ; Wu, Liying ; Huang, Jianmin ; Huang, Ning ; Lönnerdal, Bo. / Expression, characterization, and biologic activity of recombinant human lactoferrin in rice. In: Journal of Pediatric Gastroenterology and Nutrition. 2003 ; Vol. 36, No. 2. pp. 190-199.
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AU - Suzuki, Yasushi A.

AU - Kelleher, Shannon L.

AU - Yalda, Dorice

AU - Wu, Liying

AU - Huang, Jianmin

AU - Huang, Ning

AU - Lönnerdal, Bo

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N2 - Background: Lactoferrin has been suggested to have many biologic activities, such as facilitating iron absorption and having antimicrobial and antiinflammatory effects. In humans, several of these activities are likely to only be facilitated by human lactoferrin because they depend on the binding of human lactoferrin to specific receptors. Rice may be a useful vehicle to introduce recombinant human lactoferrin to infant foods because it has low allergenicity and is likely to be safer than using microorganisms or transgenic animals. Methods: Recombinant human lactoferrin was expressed in the rice cell culture system, and its biologic activity was assessed by iron-binding and -releasing properties, antimicrobial activity, and binding and uptake to Caco-2 cells. The authors also compared the stability of recombinant and native human lactoferrins against heat, low pH, and in vitro digestion. Results: Biologic activity of rice-expressed recombinant human lactoferrin was similar to that of native human lactoferrin. Heat-treated proteins retained their functional activities except with severe treatment at 100°C for 8 seconds, which disturbed the iron-binding capacity of recombinant human lactoferrin. Both types of proteins retained their functional activities between pH 2 and 7.4. After in vitro digestion, 50% of both proteins were detectable by enzyme linked immunosorbent assay. The remaining native and recombinant lactoferrins retained antimicrobial and Caco-2 binding and uptake activities. Conclusions: The results indicate recombinant human lactoferrin has stability similar to native human lactoferrin when exposed to thermal treatment, pH treatment, and in vitro digestion, suggesting it may be active when added to infant formula.

AB - Background: Lactoferrin has been suggested to have many biologic activities, such as facilitating iron absorption and having antimicrobial and antiinflammatory effects. In humans, several of these activities are likely to only be facilitated by human lactoferrin because they depend on the binding of human lactoferrin to specific receptors. Rice may be a useful vehicle to introduce recombinant human lactoferrin to infant foods because it has low allergenicity and is likely to be safer than using microorganisms or transgenic animals. Methods: Recombinant human lactoferrin was expressed in the rice cell culture system, and its biologic activity was assessed by iron-binding and -releasing properties, antimicrobial activity, and binding and uptake to Caco-2 cells. The authors also compared the stability of recombinant and native human lactoferrins against heat, low pH, and in vitro digestion. Results: Biologic activity of rice-expressed recombinant human lactoferrin was similar to that of native human lactoferrin. Heat-treated proteins retained their functional activities except with severe treatment at 100°C for 8 seconds, which disturbed the iron-binding capacity of recombinant human lactoferrin. Both types of proteins retained their functional activities between pH 2 and 7.4. After in vitro digestion, 50% of both proteins were detectable by enzyme linked immunosorbent assay. The remaining native and recombinant lactoferrins retained antimicrobial and Caco-2 binding and uptake activities. Conclusions: The results indicate recombinant human lactoferrin has stability similar to native human lactoferrin when exposed to thermal treatment, pH treatment, and in vitro digestion, suggesting it may be active when added to infant formula.

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