Journal Articles

Permanent URI for this collectionhttps://mro.massey.ac.nz/handle/10179/7915

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Subject: search.filters.subject.Alternative proteins

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    Unveiling anti-inflammatory peptides from Lion's Mane mushroom (Hericium erinaceus): Preparation, bioactivity assessment, and peptides identification
    (Elsevier B V, 2025-12-01) Silva B; Sringarm K; Potikanond S; Tangjaidee P; Buacheen P; Rachtanapun P; Donlao N; Singh J; Kaur L; Issara U; Kingwascharapong P; Phongthai S
    Lion's Mane mushroom (Hericium erinaceus) is acknowledged worldwide for its substantial contribution of medicinal compounds and nutrients, including protein. The efficient extraction and hydrolysis of proteins are essential for revealing their bioactive properties. This study demonstrates that the optimal pulsed electric field (PEF)-assisted extraction achieved a 42.44 % increase in protein extraction efficiency relative to traditional alkaline extraction (p < 0.05). H. erinaceus protein contained 44.59 % essential amino acids and exhibited 71.33 % in vitro digestibility. Pepsin-trypsin hydrolysis produced the most significant anti-inflammatory activity, resulting in a 36.2 % reduction in nitric oxide and a 31.8 % decrease in interleukin-6 levels (p < 0.05). Subsequent fractionations employing membrane ultrafiltration and size exclusion chromatography effectively purified the peptides, resulting in enhanced anti-inflammatory activity (p < 0.05). This research discovered nine important peptide sequences containing 50–100 % hydrophobic amino acids in Lion's Mane mushroom proteins, which could aid in the synthesis of natural anti-inflammatory peptides.
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    Alternative proteins vs animal proteins: The influence of structure and processing on their gastro-small intestinal digestion
    (Elsevier Ltd, 2022-04) Kaur L; Mao B; Beniwal AS; Abhilasha; Kaur R; Chian FM; Singh J
    Background: Digestibility, an indicator of protein bioavailability, is essentially a measure of the susceptibility of a protein towards proteolysis. Proteins with higher digestibility have been linked with better health outcomes. Animal proteins are generally considered to be of better nutritional value than plant proteins not only because they are a good source of essential amino acids but also due to their higher digestibility in the human gastro-intestinal tract. With the recent emergence of alternative food protein sources, which are now processed in a completely new way to design new foods or new versions of the conventional foods, it has become extremely important to understand their digestion characteristics. Scope and approach: This review discusses the factors that affect protein digestibility, including protein source, structure, type of processing, and modification, with a particular focus on the effects of non-protein components present in food matrix. Key findings and conclusions: To obtain the desired functionality, particularly for alternate proteins, numerous physical, chemical, and enzymatic methods for modification have been reported. These modifications may alter structural characteristics of proteins by inducing structural modifications such as protein unfolding, crosslinking, and aggregation. Depending upon the protein reactivity during processing, the susceptibility of proteins towards hydrolysis by digestive enzymes might change, affecting not only the overall protein digestibility but also the rates of release of polypeptides and amino acids. The faster rates of protein digestion have been linked with muscle anabolism, suggesting the need and importance of classifying the new, emerging and alternative protein sources according to their rates of digestion into rapidly (RDP), slowly digestible (SDP) and resistant (RP) proteins. More research needs to be focussed on converting, through processing, the undigestible or RP into RDP or SDP to achieve better health outcomes.