Recombinant human lactoferrin: a valuable protein for pharmaceutical products and functional foods

Biotechnol Adv. 2010 Nov-Dec;28(6):831-8. doi: 10.1016/j.biotechadv.2010.07.002. Epub 2010 Jul 17.

Abstract

Lactoferrin, the main iron-binding protein of milk, has biological activities that are essential for the newborn and are beneficial for adults. Given this beneficial effect, there is broad interest in exogenous sources of lactoferrin in human nutrition. Consequently, several transgenic approaches to produce lactoferrin have been achieved. However, the activity of heterologous lactoferrin cannot be assumed to identically mimic that of the homologous protein. Human lactoferrin obtained from yeast, transgenic cows, and rice has met the criteria of structural similarity, high yield, and ease of protein isolation. Human lactoferrin from Aspergillus awamori has been mainly directed to therapeutic uses with advanced phases of clinical trials currently in progress. In contrast, human lactoferrin produced in transgenic cows and rice brings the clear advantage of origins compatible with use in foods, although the approval for these applications is still in process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Genetically Modified
  • Functional Food*
  • Fungi / metabolism
  • Humans
  • Lactoferrin / chemistry
  • Lactoferrin / therapeutic use*
  • Plants / metabolism
  • Recombinant Proteins / therapeutic use*

Substances

  • Recombinant Proteins
  • Lactoferrin