Biotec

REVIEW: ISOLATION AND PURIFICATION OF MILK
WHEY GLYCOMACROPEPTIDE

LINDAMIR TOMCZAK TULLIO*
ELISA NOEMBERG LAZZARI KARKLE**
LYS MARY BILESKI CÂNDIDO***

The objective of this work was to review the isolation and purification methods of glycomacropeptide
(GMP). This peptide is formed during enzymatic coagulation of milk, using chymosin. Aspects such as structure, composition, biological activities and functional and technological properties of GMP are also covered. It was concluded that t he various methods mentioned in this paper for GMP isolation and purification use isolated or combined processes, which can be classified in three categories: selective precipitation induced by adjustment of the physical properties of the solution; membrane filtration based mainly on different membrane sizes and load, and selective adsorption.
Regarding the biological activities of GMP, this peptide can be understood as a promising compound, although additional research is necessary in order to define quantities, efficacy and to allow functionality claims. There is, however, little information regarding GMP’s addition i n food, interaction with other components and chemical stability under different processing conditions.

KEY-WORDS: MILK WHEY; GLYCOMACROPEPTIDE; BIOLOGICAL ACTIVITY.

*

Chemist, Master in Food Technology, Universidade Federal do Paraná (UFPR), Curitiba, PR (e-mail: [e-mail]). ** Nutritionist, Master in Food Science, Universidade Estadual de Londrina, Substitute Professor, UFPR,
Curitiba, PR.
*** Industrial Pharmacist, Doctor in Food Engineering, Universidade Estadual de Campinas, Senior
Professor, UFPR, Curitiba PR.

B.CEPPA, Curitiba, n. 1, n. 1, jan./jun. 2007
B.CEPPA, Curitiba, v. 25, v. 25, p. 121-132, jan./jun. 2007

121

1 INTRODUCTION
Milk whey can be obtained in laboratory or industry mainly by three processes: (a) enzymatic coagulation, resulting in casein coagulates, which are used for cheese and