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    Heat-Treatments Affect Protease Activities and Peptide Profiles of Ruminants' Milk
    (Frontiers Media S.A., 2021-03-10) Leite JAS; Montoya CA; Loveday SM; Maes E; Mullaney JA; McNabb WC; Roy NC; Abd El-Aty, AM
    Proteases present in milk are heat-sensitive, and their activities increase or decrease depending on the intensity of the thermal treatment applied. The thermal effects on the protease activity are well-known for bovine milk but poorly understood for ovine and caprine milk. This study aimed to determine the non-specific and specific protease activities in casein and whey fractions isolated from raw bovine, ovine, and caprine milk collected in early lactation, and to determine the effects of low-temperature, long-time (63°C for 30 min) and high-temperature, short-time (85°C for 5 min) treatments on protease activities within each milk fraction. The non-specific protease activities in raw and heat-treated milk samples were determined using the substrate azocasein. Plasmin (the main protease in milk) and plasminogen-derived activities were determined using the chromogenic substrate S-2251 (D-Val-Leu-Lys-pNA dihydrochloride). Peptides were characterized using high-resolution liquid chromatography coupled with tandem mass spectrometry. The activity of all native proteases, shown as non-specific proteases, was similar between raw bovine and caprine milk samples, but lower (P < 0.05) than raw ovine milk in the whey fraction. There was no difference (P > 0.05) between the non-specific protease activity of the casein fraction of raw bovine and caprine milk samples; both had higher activity than ovine milk. After 63°C/30 min, the non-specific protease activity decreased (44%; P > 0.05) for the bovine casein fraction only. In contrast, the protease activity of the milk heated at 85°C/5 min changed depending on the species and fraction. For instance, the activity decreased by 49% for ovine whey fraction, but it increased by 68% for ovine casein fraction. Plasmin and plasminogen were in general inactivated (P > 0.05) when all milk fractions were heated at 85°C/5 min. Most of the peptides present in heat-treated milk were derived from β-casein and αS1-casein, and they matched the hydrolysis profile of cathepsin D and plasmin. Identified peptides in ruminant milk samples had purported immunomodulatory and inhibitory functions. These findings indicate that the non-specific protease activity in whey and casein fractions differed between ruminant milk species, and specific thermal treatments could be used to retain better protease activity for all ruminant milk species.
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    Effect of Heat Treatment on Protein Self-Digestion in Ruminants' Milk
    (MDPI (Basel, Switzerland), 2023-09-21) Leite JAS; Montoya CA; Maes E; Hefer C; Cruz RAPA; Roy NC; McNabb WC; Liu Q; Liu H; Zhang J
    This study investigated whether heat treatments (raw, 63 °C for 30 min, and 85 °C for 5 min) affect protein hydrolysis by endogenous enzymes in the milk of ruminants (bovine, ovine, and caprine) using a self-digestion model. Self-digestion consisted of the incubation for six hours at 37 °C of the ruminants' milk. Free amino group concentration was measured by the o-phthaldialdehyde method, and peptide sequences were identified by chromatography-mass spectrometry. Results showed that heat treatments prior to self-digestion decreased the free NH2 by 59% in bovine milk heated at 85 °C/5 min, and by 44 and 53% in caprine milk heated at 63 °C/30 min and 85 °C/5 min, respectively. However, after self-digestion, only new free amino groups were observed for the raw and heated at 63 °C/30 min milk. β-Casein was the most cleaved protein in the raw and heated at 63 °C/30 min bovine milk. A similar trend was observed in raw ovine and caprine milk. Self-digestion increased 6.8-fold the potential antithrombin peptides in the bovine milk heated at 63 °C/30 min. Enhancing bioactive peptide abundance through self-digestion has potential applications in the industry for functional products. Overall, heat treatments affected the free amino groups according to the species and heat treatment applied, which was reflected in the varying degrees of cleaved peptide bonds and peptides released during self-digestion.
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    In Vitro Fermentation of Sheep and Cow Milk Using Infant Fecal Bacteria
    (MDPI (Basel, Switzerland), 2020-06-17) Ahlborn N; Young W; Mullaney J; Samuelsson LM
    While human milk is the optimal food for infants, formulas that contain ruminant milk can have an important role where breastfeeding is not possible. In this regard, cow milk is most commonly used. However, recent years have brought interest in other ruminant milk. While many similarities exist between ruminant milk, there are likely enough compositional differences to promote different effects in the infant. This may include effects on different bacteria in the large bowel, leading to different metabolites in the gut. In this study sheep and cow milk were digested using an in vitro infant digestive model, followed by fecal fermentation using cultures inoculated with fecal material from two infants of one month and five months of age. The effects of the cow and sheep milk on the fecal microbiota, short-chain fatty acids (SCFA), and other metabolites were investigated. Significant differences in microbial, SCFA, and metabolite composition were observed between fermentation of sheep and cow milk using fecal inoculum from a one-month-old infant, but comparatively minimal differences using fecal inoculum from a five-month-old infant. These results show that sheep milk and cow milk can have differential effects on the gut microbiota, while demonstrating the individuality of the gut microbiome.
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    The effect of milk processing on protein digestion and amino acid absorption in the gastrointestinal tract of pigs as a model human : a thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Nutritional Sciences at Massey University, Manawatū, New Zealand
    (Massey University, 2024-06-19) Ahlborn, Natalie Gisela Marlis
    Globally, milk is processed using heat and homogenisation to improve food safety and extend shelf life. These common processing techniques can alter the native structures present in milk, including protein structures. However, the impact of these processing-induced changes on the digestion of milk protein and subsequent absorption of amino acids in the human body is not yet fully understood. The overall objective of this research was to understand how heat treatment and homogenisation affect milk protein coagulation and digestion in the stomach, and to investigate how changes to gastric coagulation (curd formation) influence amino acid (AA) absorption in the small intestine and AA concentrations in blood circulation. Due to the limited accessibility of the human gastrointestinal tract, pigs were used as a model of the human. An initial study using raw bovine (cow), caprine (goat), and ovine (sheep) milk established the role of gastric curd formation in small intestinal AA absorption in piglets at a single postprandial time point. Specifically, differences in the retention of AA in the gastric curd were responsible for differences in the small intestinal AA absorption across milk of different species. A separate study using bovine milk as a milk model was then conducted to determine the effect of heat treatment and homogenisation on the kinetics of milk protein digestion and small intestinal AA absorption. The selected processing treatments were pasteurisation, ultra-high temperature treatment (UHT), and homogenisation. Raw milk was included as a comparator. In the stomach, heat treatment and homogenisation altered the strength and structure of the curd formed during gastric digestion, which in turn affected both milk protein hydrolysis and the rate of AA entering the small intestine. Differences in the release of digested protein and AA into the small intestine were reflected in the kinetics of AA absorption of the processed milk types. For example, UHT milk had both a faster rate of AA entering the small intestine and a faster rate of AA absorption. Processing also altered the appearance of some AA in blood circulation; however, these differences were not directly reflective of the differences observed in their small intestinal absorption kinetics. In conclusion, this PhD research demonstrated that the rate of small intestinal AA absorption was modulated by gastric curd formation, indicating that milk processing could be used as a strategy to modulate protein digestion and AA absorption in the gastrointestinal tract.
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    Differences in small intestinal apparent amino acid digestibility of raw bovine, caprine, and ovine milk are explained by gastric amino acid retention in piglets as an infant model
    (Frontiers Media S.A., 2023-09-04) Ahlborn NG; Montoya CA; Roy D; Roy NC; Stroebinger N; Ye A; Samuelsson LM; Moughan PJ; McNabb WC; Gallier S
    BACKGROUND: The rate of stomach emptying of milk from different ruminant species differs, suggesting that the small intestinal digestibility of nutrients could also differ across these milk types. OBJECTIVE: To determine the small intestinal amino acid (AA) digestibility of raw bovine, caprine, and ovine milk in the piglet as an animal model for the infant. METHODS: Seven-day-old piglets (n = 12) consumed either bovine, caprine, or ovine milk diets for 15 days (n = 4 piglets/milk). On day 15, fasted piglets received a single meal of fresh raw milk normalized for protein content and containing the indigestible marker titanium dioxide. Entire gastrointestinal tract contents were collected at 210 min postprandially. Apparent AA digestibility (disappearance) in different regions of the small intestine was determined. RESULTS: On average, 35% of the dietary AAs were apparently taken up in the small intestine during the first 210 min post-feeding, with 67% of the AA digestibility occurring in the first quarter (p ≤ 0.05) and 33% in the subsequent two quarters. Overall, except for isoleucine, valine, phenylalanine, and tyrosine, the small intestinal apparent digestibility of all AAs at 210 min postprandially in piglets fed ovine milk was, on average, 29% higher (p ≤ 0.05) than for those fed bovine milk. Except for lysine, there was no difference in the apparent digestibility (p > 0.05) of any AAs between piglets fed caprine milk or ovine milk. The apparent digestibility of alanine was higher (p ≤ 0.05) in piglets fed caprine milk than those fed bovine milk. When apparent digestibility was corrected for gastric AA retention, only small differences in the small intestinal apparent digestibility of AAs were observed across milk types. CONCLUSION: Bovine, caprine and ovine milk had different apparent small intestinal AA digestibility at 210 min postprandially. When corrected for gastric AA retention, the differences in apparent digestibility across species largely disappeared. The apparent AA digestibility differed across small intestinal locations.