Bioactive peptides of whey: obtaining, activity, mechanism of action, and further applications.

Bioactive peptides derived from diverse food proteins have been part of diverse investigations. Whey is a rich source of proteins and components related to biological activity. It is known that proteins have effects that promote health benefits. Peptides derived from whey proteins are currently widely studied. These bioactive peptides are amino acid sequences that are encrypted within the first structure of proteins, which required hydrolysis for their release. The hydrolysis could be through in vitro or in vivo enzymatic digestion and using microorganisms in fermented systems. The biological activities associated with bio-peptides include immunomodulatory properties, antibacterial, antihypertensive, antioxidant and opioid, etc. These functions are related to general conditions of health or reduced risk of certain chronic illnesses. To determine the suitability of these peptides/ingredients for applications in food technology, clinical studies are required to evaluate their bioavailability, health claims, and safety of them. This review aimed to describe the biological importance of whey proteins according to the incidence in human health, their role as bioactive peptides source, describing methods, and obtaining technics. In addition, the paper exposes biochemical mechanisms during the activity exerted by biopeptides of whey, and their application trends.

Proteolytic System of Streptococcus thermophilus.

The growth of lactic acid bacteria (LAB) generates a high number of metabolites related to aromas and flavors in fermented dairy foods. These microbial proteases are involved in protein hydrolysis that produces necessary peptides for their growth and releases different molecules of interest, like bioactive peptides, during their activity. Each genus in particular has its own proteolytic system to hydrolyze the necessary proteins to meet its requirements. This review aims to highlight the differences between the proteolytic systems of Streptococcus thermophilus and other lactic acid bacteria (Lactococcus and Lactobacillus) since they are microorganisms that are frequently used in combination with other LAB in the elaboration of fermented dairy products. Based on genetic studies and in vitro and in vivo tests, the proteolytic system of Streptococcus thermophilus has been divided into three parts: 1) a serine proteinase linked to the cellular wall that is activated in the absence of glutamine and methionine; 2) the transport of peptides and oligopeptides, which are integrated in both the Dpp system and the Ami system, respectively; according to this, it is worth mentioning that the Ami system is able to transport peptides with up to 23 amino acids while the Opp system of Lactococcus or Lactobacillus transports chains with less than 13 amino acids; and finally, 3) peptide hydrolysis by intracellular peptidases, including a group of three exclusive of S. thermophilus capable of releasing either aromatic amino acids or peptides with aromatic amino acids.

Population pharmacokinetics of levetiracetam in neonates with seizures.

WHAT IS KNOWN AND OBJECTIVE: This study developed a population pharmacokinetic (PK) model of levetiracetam (LEV) for treating neonatal seizures (NS) and determined the influence of clinically relevant covariates to explain the interindividual variability and residual error. METHODS: Twenty newborns admitted to the Neonatal Intensive Care Unit at the Hospital Central "Dr. Ignacio Morones Prieto" were included. LEV doses were administered by intermittent infusion. Blood samples were drawn 3 times post-infusion. Levetiracetam was quantified by a chromatographic technique. NONMEM software was used to determine the population PK model of LEV in neonates and the influence of clinical covariates on drug disposition. RESULTS AND DISCUSSION: The LEV PK in neonates is described by a one-compartment open model with first-order elimination. The influence of creatinine clearance (CRCL) and body weight (BW) on clearance (CL[L/h] = 0.47*CRCL), as well as the volume of the distribution (Vd[L] = 0.65*BW) of LEV, were confirmed, considering interindividual variabilities of 36% and 22%, respectively, and a residual error of 13%. WHAT IS NEW AND CONCLUSION: Based on the PK of LEV in neonates and the influence of the final PK model, a priori dosing guidelines are proposed considering CRCL, BW and LEV plasma concentrations between 6 and 20 mg/L for NS treatment.

Enhancement of lactase activity in milk by reactive sulfhydryl groups induced by heat treatment.

The effects of heat treatments of milk and whey prior to lactose hydrolysis with Kluyveromyces lactis beta-galactosidase were studied. It was observed that heat treatment of milk significantly increases lactase activity, with a maximum activity increase found when milk was heated at 55 degrees C. In whey from 55 up to 75 degrees C, beta-galactosidase activity decreased slightly. Nevertheless, heating whey at 85 degrees C for 30 min raised the rate of hydrolysis significantly. Electrophoretic patterns and UV spectra proved that the activity change correlated with milk protein denaturation, particularly that of beta-lactoglobulin. Heating whey permeate did not increase the enzyme activity as heating whole whey; but heating whey prior to ultrafiltration also resulted in enzyme activation. Measurement of free sulfhydryl (SH) groups in both whey and heated whey permeate showed that the liberation of free SH is highly correlated to the change of the activity. Furthermore, this activation can be reversed by oxidizing the reactive sulfhydryl groups, proving that the observed effect may be related to the release of free SH to the medium, rather than to the denaturation of a thermolabile protein inhibitor.

[Uses of microbial beta-galactosidases to reduce lactose content in milk and dairy products]. / Usos de beta-galactosidasas microbianas para reducir el contenido de lactosa en leche y productos lácteos.

The commercial sources of microbial beta-galactosidases (lactases) include the yeasts species Kluyveromyces marxianus, Kluyveromyces lactis and Candida kefyr which are used to hydrolyse lactose in milk due to their optimum pH. On the other hand, lactases obtained from the moulds Aspergillus niger and Aspergillus oryzae have an acid optimum pH and therefore are used to hydrolyse lactose in whey to obtain whey syrups to be used as raw materials in the food industry. The lactose intolerance problem has led to many studies concerning lactose hydrolysis by means of these microbial enzymes to obtain milk suitable for people with lactose maldigestion and special diets for ill persons, elderly population and intolerant babies due to secondary deficiency of lactose. Most industries obtain hydrolyzed lactose milk with free enzyme; however, there are some developments of immobilized lactase catalysts which are being used mainly in whey.