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Animal Source Foods
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
The main role attributed to insoluble caseins is mineral binding and their capacity as carriers, mainly for calcium and phosphorus (90–95). Total caseins can be divided in α-, β-, and κ-caseins. They transport calcium and phosphorus, forming a coagulum and improving their digestibility in the stomach. In addition, caseins give several bioactive peptides that have antioxidant, immunomodulatory, cyto-modulatory, antihypertensive, and antithrombotic actions in the cardiovascular, nervous, immune, and digestive systems (90–94). Milk protein is especially rich in amino acids that stimulates muscle synthesis, and some proteins and peptides in milk have positive health effects on blood pressure, inflammation, oxidation, and tissue development. The amino acid profile is quite different between the two fractions. Whey is especially rich in branched chain amino acids such as leucine, isoleucine, and valine as well as lysine; whereas casein has a higher proportion of histidine, methionine, and phenylalanine (90–94). The benefits of drinking whey have been known for centuries. An ancient proverb from the Italian city of Florence says: ‘If everyone was raised on whey, doctors would be bankrupt’ (93).
Lactic Acid Bacteria Application to Decrease Food Allergies
Published in Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani, Lactic Acid Bacteria, 2020
Vanessa Biscola, Marcela Albuquerque Cavalcanti de Albuquerque, Tatiana Pacheco Nunes, Antonio Diogo Silva Vieira, Bernadette Dora Gombossy de Melo Franco
In general bases, LAB proteolytic system is composed of extracellular-secreted (E) and surface-associated proteinases (cell envelope proteases, CEP), peptide transporters and intracellular peptidases. It consists of a series of chained reactions, starting with the action of CEPs, which break the proteins into dipeptides, tripeptides, and oligopeptides and are pointed by some authors as the most important enzymes of the system. Five different types of CEPs have already been characterized from different LAB, including PrtP from Lactococcus lactis and Lactobacillus paracasei, PrtH from Lactobacillus helveticus, PrtR from Lactobacillus rhamnosus, PrtS from Streptococcus thermophilus and PrtB from Lactobacillus bulgaricus. In lactococci and lactobacilli, CEPs are serine proteinases distinguished in PI and PII, according to their substrate specificity for αS1, β, and κ-caseins. PI-type primarily degrades β-casein, presenting a strong activity towards this protein fraction. These enzymes also degrade k-casein, but to a lesser extent and present no activity against αS1-casein. PIII-type hydrolyzes all casein fractions (α, β, and κ) equally. The peptides derived from CEP hydrolysis are carried into the cells by peptide transporters, in the second stage of the LAB proteolytic system. The type of transporter involved in this step depends on the size of the molecule been carried (Savijoki et al. 2006, Worsztynowicz et al. 2019).
Gestational Weight Gain and Postpartum Obesity
Published in Priyanka Bhatt, Maryam Sadat Miraghajani, Sarvadaman Pathak, Yashwant Pathak, Nutraceuticals for Prenatal, Maternal and Offspring’s Nutritional Health, 2019
Bovine milk is a liquid food which is nutrient dense with essential components such as calcium, vitamin D, vitamin B12, vitamin A, riboflavin, potassium, and phosphorus. [28] Milk is known to be a significant source of high-quality proteins that account for nutritional, functional, and physiological activities, and such proteins are αs1-caseins, β-caseins, κ-caseins, α-lactalbumin, and β-lactoglobulins. [28] These proteins are often found in weight gain supplements used by weight lifters and athletes as they help minimize muscle loss and increase muscle protein synthesis. Milk also contains all the nine essential amino acids in proportions corresponding to the recommended amino acid requirements. The presence of branched chain amino acids such as isoleucine, leucine, and valine are at higher levels than any other natural sources.
The Association between Consumption of Dairy-Originated Digestion Resistant and Bioactive Peptides and Breast Cancer Risk: A Case-Control Study
Published in Nutrition and Cancer, 2022
Masoumeh Jabbari, Meisam Barati, Mahdi Shabani, Elham Kazemian, Sajad Khalili-Moghadam, Fardin Javanmardi, Elaheh Hatami, Reihaneh Zeinalian, Sayed Hossein Davoodi, Bahram Rashidkhani, Shima Jafarzadeh, Elcin Huseyn, Amin Mousavi Khaneghah
The dietary intake of BPs was estimated based on dairy food items in the FFQ (26). Calculation of bioactive and digestion-resistant peptides intake was performed by multiplying dairy items intake (g) by the content of their bioactive and digestion-resistant peptides. The method of BP content estimation was developed and validated in our previous in silico study (28). In brief, simulated proteolysis of the dairy protein subunits was conducted using the "enzyme action" tool of the BIOPEP web server (29). First, in silico, proteolysis of proteins was conducted using pepsin, trypsin, and chymotrypsin A. Then, the peptide fragments resulting from proteolysis of αs1-casein, αs2-casein, β-casein, k-casein, β-lactoglobulin, and α-lactalbumin were submitted to the BIOPEP database to characterize active fragments. Finally, the sequences obtained from in silico digestion were separated according to (1) total peptides, (2) biological function (anti-diabetic, anti-hypertensive, antioxidant, and immunomodulatory), (3) number of residues (di, tri, tetra, penta, hexa, hepta, and more than heptapeptide), (4) hydrophilicity (low and high), and (5) bioactivity (low and high).
The effects of dairy and dairy derivatives on the gut microbiota: a systematic literature review
Published in Gut Microbes, 2020
Hajara Aslam, Wolfgang Marx, Tetyana Rocks, Amy Loughman, Vinoomika Chandrasekaran, Anu Ruusunen, Samantha L. Dawson, Madeline West, Eva Mullarkey, Julie A. Pasco, Felice N. Jacka
Five studies39-43 included in this review demonstrated the potential of dairy products including milk and fermented dairy (i.e. yogurt and kefir) to increase the growth of so-called beneficial bacteria.40-43Lactobacillus and Bifidobacterium are two major bacterial genera that are considered to be ‘probiotics’ due to their demonstrated benefits to host health, such as improving metabolic disequilibrium, immune modulation and regulating inflammation.73 Components of dairy such as lactose and protein possess potential to stimulate the growth of these bacterial genera. Lactose is the key milk carbohydrate; it exists in a concentration of 53 g/L and is often referred to as ‘milk sugar’.74 Both in vitro and in vivo studies have demonstrated that lactose increased the growth of Bifidobacterium and Lactobacillus.67,75 Lactose also contains a prebiotic index of 5.75, which is similar to many other prebiotics.69,76 Prebiotics are a fermentable ingredient that instigates specific changes to both the composition and/or activity of the gastrointestinal microbes rendering health benefits. Milk proteins also hold potential to facilitate the growth of Bifidobacterium and Lactobacillus. Casein forms 80% of milk protein and is composed of four sub-units (α-caseinS1, α-caseinS2, β-casein, κ-casein). A κ-casein derived hydrolyzates demonstrated growth stimulatory effects on Bifidobacterium bifidum in a synthetic culture media.68 Whey protein forms 20% of milk proteins and include the water-soluble protein fraction: α-lactoalbumin, β-lactoglobulin, immunoglobulins (Ig), lactoferrin, serum albumin, lactoperoxidase and lysozymes. Short peptides produced by the proteolytic digestion of β-lactoglobulin showed growth proliferation effects on Bifidobacterium and Lactobacillus spp.77 Further, lactoferrin hydrolyzates increased the growth of Bifidobacterium adolescentis B-1 in a dose dependant manner.78
Bacterial outer membrane vesicles-cloaked modified zein nanoparticles for oral delivery of paclitaxel
Published in Pharmaceutical Development and Technology, 2023
Zeyu Wang, Yuqi Chu, Xu Tao, Jianchao Li, Lihong Wang, Yuli Sang, Xiuli Lu, Lijiang Chen
Recently, a broad range of new drug delivery systems has been developed, including liposomes, micelles, nanoemulsions, and nanogels (Arranja et al. 2017). Among these, amphiphilic protein biopolymers used to encapsulate and deliver bioactive compounds have attracted increasing attention. The availability of natural resources, inherent biocompatibility and biodegradability, and ease of binding to specific drugs and ligands are the key characteristics of natural proteins as potential efficient nanocarriers (Bhattacharya et al. 2021). More intriguingly, plant-derived proteins have emerged as strong contenders in a variety of pharmaceutical designs. Compared with animal-derived proteins, they are more dependable owing to being renewable and relatively affordable to prepare (Abdelsalam et al. 2021). Zein is an insoluble prolamin protein generated from corn (Parris and Dickey 2001) that is soluble in 60–85% ethanol, has two-thirds lipophilic and one-third hydrophilic amino acid residues (Argos et al. 1982; Zhong and Jin 2009), and is 50 times more hydrophobic than albumin or fibrinogen (Chen Y et al. 2014). Moreover, it is known that zein is columnar and self-assembles into particles and layers based on its molecular structure (Argos et al. 1982; Sousa et al. 2012). Thus, zein can easily self-assemble into nanoparticles that act as a solubility enhancer for poorly water-soluble nutrients and drugs (Zhao et al. 2020; Reboredo et al. 2021). However, zein nanoparticles are generally hydrophobic and easy to aggregate or precipitate. It is reported that modified nanoparticles with stabilizers such as sodium caseinate (CAS) (Luo, Teng, et al. 2013), pectin (Zhang et al. 2021), gum arabic (Spasojević et al. 2020), and carboxymethyl chitosan (Luo, Wang, et al. 2013) can effectively improve the stability of zein nanoparticles. Moreover, CAS stabilizes zein nanoparticles over a wide range of ionic strengths (Li H et al. 2018). CAS, a water-soluble salt of casein, consists of four main components (αs1-, αs2-, β-, and κ-casein) with high proportions of hydrophobic and hydrophilic amino acid residues. Casein-based formulations are widely used as emulsifiers, stabilizers (Urbánková et al. 2021), and drug delivery systems (Liu J et al. 2021) in the food and pharmaceutical industries due to the excellent surface activity and unique self-assembly properties of CAS as well as its low cost.