Lactoferrin-based nanoparticles as a vehicle for iron in food applications – Development and release profile

Zhang

et al. 2018

CyTA - Journal of Food

This study aimed to investigate effects of amidated low methoxyl (ALM, 0.3%, w/v) pectin on physiochemical and structural properties of polymerized whey proteins (PWP, 10%, w/v) prepared by thermal aggregation at 85°C for 10-30 min. Particle size, zeta potential, isoelectric point (IEP), surface hydrophobicity, free sulphydryl group, rheological properties and the secondary structure of all samples were analysed. ALM pectin increased mean diameter and narrowed size distribution of PWP samples (p < 0.05) regardless of heating time. Addition of ALM pectin shifted the IEP of PWPpectin complex to lower pH, which decreased with heating time increased. ALM pectin decreased the surface hydrophobicity of PWP heated for 30 min pronouncedly. Whey protein (WP) complexed with ALM pectin showed decreased gelation time and rheological properties of improved elasticity. ALM pectin had no considerable effect on secondary structure of PWP. Data indicated that ALM pectin could alter physiochemical properties of heat-induced polymerized WPns. Efectos de la pectina amidada de bajo metoxilo en las propiedades fisicoquímicas y estructurales de las proteínas de suero polimerizadas RESUMEN El presente estudio se propuso investigar los efectos de la pectina amidada de bajo metoxilo (ALM, 0.3%, p/v) en las propiedades fisicoquímicas y estructurales de las proteínas de suero polimerizadas (PWP, 10%, w/v) y preparadas mediante el método de agregación térmica a 85°C durante 10-30 min. Asimismo, en el estudio se analizaron: el tamaño de las partículas, el potencial zeta, el punto isoeléctrico, la hidrofobicidad superficial, el grupo sulfhidrilo libre, las propiedades reológicas y la estructura secundaria de todas las muestras. Se constató que la pectina ALM aumentó el diámetro medio y estrechó la distribución de tamaños de las muestras de PWP (p < 0.05) independientemente de la duración del calentamiento. Por otra parte, la adición de pectina ALM llevó el punto isoeléctrico del complejo pectina PWP a un pH más bajo, lo cual fue disminuyendo a medida que aumentó el tiempo de calentamiento. La pectina ALM redujo drásticamente la hidrofobicidad superficial de la PWP calentada durante 30 min. La proteína de suero en complejo con la pectina ALM mostró tener un tiempo de gelificación más reducido y propiedades reológicas de mayor elasticidad. La pectina ALM no afectó sensiblemente la estructura secundaria de PWP. Los datos dan cuenta de que la pectina ALM puede alterar las propiedades fisicoquímicas de las proteínas de suero polimerizadas mediante su exposición al calor.

“…force during heating, which may reduce the contact frequency of WP molecules and then prevented the formation of large aggregates. Similar results were reported by Martins et al (2016).…”

Section: Resultssupporting

confidence: 92%

Effects of amidated low methoxyl pectin on physiochemical and structural properties of polymerized whey proteins

Zhang

et al. 2018

CyTA - Journal of Food

Trends in Food Science & Technology

“…19-48). Furthermore, encapsulating materials should have low viscosity, good Anionic; gelling and film-forming capacities (Li, Ni, Shao, & Mao, 2014) Pectin Anionic; gelation and emulsification properties; anti-oxidative effect (Noh et al, 2018) Proteins β-lactoglobulin Inexpensive; ability to form gels; antioxidant activity; resistant to gastric digestion (Madalena et al, 2016) Sodium Caseinate Emulsification and gelation properties (Montes de Oca-Ávalos, Candal, & Herrera, 2017) Lactoferrin Antibacterial; antiviral; immunomodulatory capacity; high iron binding capacity; high isoelectric point (Martins et al, 2016) Zein Ability to self-assemble; insolubility in aqueous conditions; resistance to gastric digestion (Zhang, Cui et al, 2016) Lipids Long chain triglycerides (LCT) (e.g. corn oil)…”

Section: Encapsulating Materialsmentioning

confidence: 99%

Advances in nutraceutical delivery systems: From formulation design for bioavailability enhancement to efficacy and safety evaluation

Gonçalves

Martins

Duarte

et al. 2018

Self Cite

175

Background: Aiming at the enhancement of food products' nutritional and health value, the incorporation of nutraceuticals has attracted increasing interest in the last years. However, they often exhibit low water solubility and stability, limiting their direct incorporation into food products. Also, they show very low bioavailability due to limited bioaccessibility, poor absorption and/or chemical transformation within the gastrointestinal tract. This renders their health benefits extremely difficult to be realized by the consumers. Scope and approach: In the present review the recent innovations regarding the formulation and design of biobased micro and nano-delivery systems to encapsulate nutraceuticals is discussed; it also gives an overview of the challenges associated to their development; and highlights some strategies to enhance nutraceuticals' bioavailability. An insight about delivery systems' potential toxicity (in particular at nano-scale) is also provided. Key findings and conclusions: Recent developments in the design of bio-based delivery systems offer the possibility of stabilizing and enhancing nutraceuticals' functionality within food products. In fact, different strategies can be used to enhance nutraceuticals' bioavailability: i) nano-delivery systems, besides showing a huge potential for the protection of valuable nutraceuticals during food processing/digestion, can be used to increase their bioavailability; ii) absorption enhancement technologies have been successfully used to increase nutraceuticals' membrane permeation; and iii) excipient foods have been shown to improve nutraceuticals' biological activity. However, the application of these enabling technologies to food is hindered by very pertinent issues that can be summarized in the effective preservation/maximization of the nutraceuticals' bioactivity and safety, once inside the human body.

Front. Sustain. Food Syst.

“…The nanoparticles showed an ironbinding efficiency value of ≈20% and showed to be stable to temperature (4-60 • C) and pH (pH 2-11) variations and during shelf-life (76 days at 4 • C). Results from iron release experiments showed a pH-dependent behavior (Martins et al, 2016).…”

Section: Nanoscale Structuresmentioning

confidence: 97%

Protein-Based Structures for Food Applications: From Macro to Nanoscale

Martins

Bourbon

Pinheiro

et al. 2018

Self Cite

Novel food structures' development through handling of macroscopic and microscopic properties of bio-based materials (e.g., size, shape, and texture) is receiving a lot of attention since it allows controlling or changing structures' functionality. Proteins are among the most abundant and employed biomaterials in food technology. They are excellent candidates for creating novel food structures due to their nutritional value, biodegradability, biocompatibility, generally recognized as safe (GRAS) status and molecular characteristics. Additionally, the exploitation of proteins' gelation and aggregation properties can be used to encapsulate bioactive compounds inside their network and produce consistent delivery systems at macro-, micro-, and nanoscale. Consequently, bioactive compounds which are exposed to harsh storage and processing conditions and digestion environment may be protected and their bioavailability could be enhanced. In this review, a range of functional and structural properties of proteins which can be explored to develop macro-, micro-, and nanostructures with numerous promising food applications was discussed. Also, this review points out the relevance of scale on these structures' properties, allowing appropriate tailoring of protein-based systems such as hydrogels and micro-or nanocapsules to be used as bioactive compounds delivery systems. Finally, the behavior of these systems in the gastrointestinal tract (GIT) and the impact on bioactive compound bioavailability are thoroughly discussed.