Abstract
In this study, bovine lactoferrin (bLf), an iron-binding glycoprotein considered an important nutraceutical protein because of its several properties, was expressed in Pichia pastoris KM71-H under AOX1 promoter control, using pJ902 as the recombinant plasmid. Dot blotting analysis revealed the expression of recombinant bovine lactoferrin (rbLf) in Pichia pastoris. After Bach fermentation and purification by molecular exclusion, we obtained an expression yield of 3.5 g/L of rbLf. rbLf and predominantly pepsin-digested rbLf (rbLfcin) demonstrated antibacterial activity against Escherichia coli (E. coli) BL21DE3, Staphylococcus aureus (S. aureus) FRI137, and, in a smaller percentage, Pseudomonas aeruginosa (Ps. Aeruginosa) ATCC 27833. The successful expression and characterization of functional rbLf expressed in Pichia pastoris opens a prospect for the development of natural antimicrobial agents produced recombinantly.
Highlights
IntroductionMilk is a fluid produced by females of all mammal species whose main function is to be the first food of a newborn because it supplies all the nutritional requirements of the newborn to contribute to organ development and the maintenance of normal physiology [1,2]
Milk is a fluid produced by females of all mammal species whose main function is to be the first food of a newborn because it supplies all the nutritional requirements of the newborn to contribute to organ development and the maintenance of normal physiology [1,2].Lactoferrin (Lf) was first identified in milk in 1939 by Sorensen [3] and the first reports reference it as “red protein from milk” [4]
We demonstrated that, unlike non-fragmented lactoferrin, pepsin-digested recombinant bovine lactoferrin (rbLf) has a higher antibacterial potential against E. coli [15]
Summary
Milk is a fluid produced by females of all mammal species whose main function is to be the first food of a newborn because it supplies all the nutritional requirements of the newborn to contribute to organ development and the maintenance of normal physiology [1,2]. Lactoferrin (Lf) was first identified in milk in 1939 by Sorensen [3] and the first reports reference it as “red protein from milk” [4]. It is an 80-kDa iron-binding glycoprotein belonging to the transferrin family. It is found in high concentrations in colostrum and milk, and in lower amounts in mucosal secretions such as tears, saliva, semen, nasal and bronchial secretions, bile, and gastrointestinal fluids [5]. Dhoumeotloogtyhaemgornogwspinegcieps,raonbdleimts aonftimanictriobbioiatlicporteesnitsitaalnhcaes,bweeen tfeoscteuds inouvirvoreasnedairnchvitoron[2d0e].veloping technologDieuse tthoathaellogrwowfoinrgthperoobblteaminomf eannttiobfiortLicf rwesitishtaanpceo,wweerffuolcuasntoiumricrreosebairaclhefofnecdt,ewvehloicphincgan be usedtienchtnhoelofugiteusrtehast aallroewplfaocretmheeonbtttaoincmuernretnotf arLnftiwbitohtiacsp.oIwnetrhfuelparnetsimenictrsotbuiadlye,fwfecet,rwephoicrht fcoarntbhee first time uthseedexinprtehsesifountu, rpeuarsifiacaretipolnac,eamndenpt ototecnutirarel natnatinmtiibcirootibcisa.lIanctthiveitpyreosfernetcsotmudbyi,nwanet rbeopvoirnt efolractthoeferrin (rbLff)irinst Ptiimcheiathpeasetxoprirse.ssion, purification, and potential antimicrobial activity of recombinant bovine lactoferrin (rbLf) in Pichia pastoris
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