Dataset Information

Loss of Eicosapentaenoic Acid (EPA) after Retort Sterilization of the EPA-BCAA Fortified Complete Nutrition Drink.

ABSTRACT: Retort sterilization is cost-effective for small-scale production of specialized nutrition products. However, the sensory properties and stability of active ingredients after sterilization remain undetermined. This study aimed to investigate the effect of retort on the existence of functional compounds and the sensory satisfaction of a fortified complete nutrition formula with branched-chain amino acids (BCAAs), and fish oil providing eicosapentaenoic acid (EPA). Changes in EPA and BCAA contents after retort were determined by using LC-MS/MS. Nutrient values, osmolality, rheology and sensory acceptance of the processed fortified and control formulas were compared. After retort, the fortified formula had an increase in all types of BCAAs but 30% loss of EPA (p = 0.001). The fortified formula had slightly higher protein and fiber contents, along with increased osmolality. It had higher viscosity and shear stress, but similar IDDSI level at 0. Among flavors tested, the fortified formula with Japanese rice flavor received the highest satisfaction scores with over 80% sensory acceptance. In conclusion, retort sterilization preserved BCAAs of the functional drink, but the addition of 30% fish oil was required to compensate for the EPA loss. The sterilized fortified formula with Japanese rice flavor was sensory acceptable.

SUBMITTER: Khoonin W

PROVIDER: S-EPMC9320311 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Loss of Eicosapentaenoic Acid (EPA) after Retort Sterilization of the EPA-BCAA Fortified Complete Nutrition Drink.

Khoonin Watcharapol W Shantavasinkul Prapimporn Chattranukulchai PC Santivarangkna Chalat C Trachootham Dunyaporn D

Foods (Basel, Switzerland) 20220708 14

Retort sterilization is cost-effective for small-scale production of specialized nutrition products. However, the sensory properties and stability of active ingredients after sterilization remain undetermined. This study aimed to investigate the effect of retort on the existence of functional compounds and the sensory satisfaction of a fortified complete nutrition formula with branched-chain amino acids (BCAAs), and fish oil providing eicosapentaenoic acid (EPA). Changes in EPA and BCAA contents ...[more]

PMID: 35885266

Similar Datasets

Project description:Background Donor human milk should be processed to guarantee microbiological safety prior to infant feeding, but this process can influence the structure and quantity of functional proteins. Objective The aim of this study was to determine the effect of thawing, homogenization, vat-pasteurization (Vat-PT), retort sterilization (RTR) and ultra-high-temperature (UHT) processing on the structure of bioactive proteins in donor milk. Methods Pooled donor milk was either not treated (Raw) or treated with an additional freeze-thaw cycle with and without homogenization, Vat-PT, RTR with and without homogenization, and UHT processing with and without homogenization. Overall protein retention was assessed via sodium-dodecyl sulfate (SDS-PAGE), and the immunoreactivity of 13 bioactive proteins were assessed via enzyme-linked immunosorbent assay (ELISA). Results Freeze-thawing, freeze-thawing plus homogenization and Vat-PT preserved all the immunoglobulins (sIgA/IgA, IgG, IgM) in donor milk, whereas RTR and UHT degraded almost all immunoglobulins. UHT did not alter osteopontin immunoreactivity, but Vat-PT and retort decreased it by ~50 and 70%, respectively. Freeze-thawing with homogenization, Vat-PT and UHT reduced lactoferrin's immunoreactivity by 35, 65, and 84%, respectively. Lysozyme survived unaltered throughout all processing conditions. In contrast, elastase immunoreactivity was decreased by all methods except freeze-thawing. Freeze-thawing, freeze-thawing plus homogenization and Vat-PT did not alter polymeric immunoglobulin receptor (PIGR) immunoreactivity, but RTR, RTR plus homogenization and UHT increased detection. All heat processing methods increased α-lactalbumin immunoreactivity. Vat-PT preserved all the growth factors (vascular/endothelial growth factor, and transforming growth factors β1 and β2), and UHT treatments preserved the majority of these factors. Conclusion Different bioactive proteins have different sensitivity to the treatments tested. Overall, Vat-PT preserved more of the bioactive proteins compared with UHT or RTR. Therefore, human milk processors should consider the impact of processing methods on key bioactive proteins in human milk.

Project description:BackgroundAmong extremophiles, halophiles are defined as microorganisms adapted to live and thrive in diverse extreme saline environments. These extremophilic microorganisms constitute the source of a number of hydrolases with great biotechnological applications. The interest to use extremozymes from halophiles in industrial applications is their resistance to organic solvents and extreme temperatures. Marinobacter lipolyticus SM19 is a moderately halophilic bacterium, isolated previously from a saline habitat in South Spain, showing lipolytic activity.Methods and findingsA lipolytic enzyme from the halophilic bacterium Marinobacter lipolyticus SM19 was isolated. This enzyme, designated LipBL, was expressed in Escherichia coli. LipBL is a protein of 404 amino acids with a molecular mass of 45.3 kDa and high identity to class C β-lactamases. LipBL was purified and biochemically characterized. The temperature for its maximal activity was 80°C and the pH optimum determined at 25°C was 7.0, showing optimal activity without sodium chloride, while maintaining 20% activity in a wide range of NaCl concentrations. This enzyme exhibited high activity against short-medium length acyl chain substrates, although it also hydrolyzes olive oil and fish oil. The fish oil hydrolysis using LipBL results in an enrichment of free eicosapentaenoic acid (EPA), but not docosahexaenoic acid (DHA), relative to its levels present in fish oil. For improving the stability and to be used in industrial processes LipBL was immobilized in different supports. The immobilized derivatives CNBr-activated Sepharose were highly selective towards the release of EPA versus DHA. The enzyme is also active towards different chiral and prochiral esters. Exposure of LipBL to buffer-solvent mixtures showed that the enzyme had remarkable activity and stability in all organic solvents tested.ConclusionsIn this study we isolated, purified, biochemically characterized and immobilized a lipolytic enzyme from a halophilic bacterium M. lipolyticus, which constitutes an enzyme with excellent properties to be used in the food industry, in the enrichment in omega-3 PUFAs.

Dataset Information

Loss of Eicosapentaenoic Acid (EPA) after Retort Sterilization of the EPA-BCAA Fortified Complete Nutrition Drink.

Publications

Loss of Eicosapentaenoic Acid (EPA) after Retort Sterilization of the EPA-BCAA Fortified Complete Nutrition Drink.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets