This study is a systematic critical review aimed at rigorously evaluating the potential of Hermetia illucens larvae (black soldier fly larvae, BSFL) as a sustainable protein source for animal feed through a standardized methodological framework. To address the significant challenge posed by the increasing global demand for protein feed to agricultural sustainability, we retrieved relevant studies published between October 2008 and June 2025 from three core databases—PubMed, ScienceDirect, and Web of Science—and conducted study screening and data extraction in accordance with the PRISMA guidelines. BSFL represent a viable alternative, with a high protein content of 40–60% and efficient organic waste conversion capabilities. This systematic review explores the potential of BSFL to replace traditional protein sources such as fishmeal and soybean meal in animal feed, highlighting their advantages in enhancing growth performance, improving gut health, and reducing methane emissions in ruminants. However, there are still critical research gaps, including the need for standardized safety assessments regarding heavy metal accumulation and chitin digestibility. Addressing these challenges through optimized rearing techniques and rigorous safety evaluations will be crucial for scaling up BSFL production and advancing the development of circular agriculture.
Tricholoma matsutake, as a rare wild edible mushroom, is popular due to its unique flavor and taste, as well as high nutritional and economic value. Investigating the relationship between the complex structure and in vitro immunological activity of TMP-2a, a novel polysaccharide isolated from T. matsutake, was the aim of this study. The results showed that TMP-2a consisted of six monosaccharides, fucose, glucosamine hydrochloride, galactose, glucose, mannose, and glucuronic acid, with molar ratios of 8.8:0.6:23.4:48.1:15.1:4.0 and a molecular weight of 27,749 Da. Furthermore, TMP-2a was mainly composed of →6)-β-Glcp-(1→ with →3)-β-D-Glcp-(1→ forming the main chain, with a small amount of →2,6)-α-D-Manp-(1→ and →6)-α-D-Galp-(1→ structural units attached, and the branched chain was mainly composed of β-Glcp-(1→ or a small amount of α-L-Fucp-(1→ as a telosaccharide attached at the O-6 position of →3,6)-β-D-Glcp-(1→. TMP-2a enhanced the proliferation and phagocytic activity of mouse macrophage RAW264.7, as well as the secretion of NO and cytokines (TNF-α, IL-6, IL-1β) to a considerable degree, maybe attributable to its glucan structure and the elevated presence of (1→3)-β-D-Glcp glycosidic bonds. This study establishes a basis for the structural identification and comprehensive investigation of the functional activities of T. matsutake polysaccharides while also offering a theoretical framework for the creation of T. matsutake-related food products.