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Response Surface Methodology (RSM) for Optimizing Protein Extraction from Housefly (Musca domestica) Larvae Fed with Toad and Its Structural Characterization.
Miao, Jingnan; Yu, Chenglu; Cheng, Xianhe; Qiu, Junqiang; Liu, Shumin.
Afiliación
  • Miao J; Graduate School, Institute of Traditional Chinese Medicine, Heilongjiang University of Chinese Medicine, Harbin 150040, China.
  • Yu C; Graduate School, Institute of Traditional Chinese Medicine, Heilongjiang University of Chinese Medicine, Harbin 150040, China.
  • Cheng X; Graduate School, Institute of Traditional Chinese Medicine, Heilongjiang University of Chinese Medicine, Harbin 150040, China.
  • Qiu J; Key Laboratory of Tropical Translational Medicine of Ministry of Education, International Joint Research Center of Human-Machine Intelligent Collaborative for Tumor Precision Diagnosis and Treatment of Hainan Province, School of Pharmacy, Hainan Medical University, Haikou 570100, China.
  • Liu S; Graduate School, Institute of Traditional Chinese Medicine, Heilongjiang University of Chinese Medicine, Harbin 150040, China.
Molecules ; 29(11)2024 May 31.
Article en En | MEDLINE | ID: mdl-38893470
ABSTRACT
With the global population on the rise, an escalating interest exists in environmentally sustainable and friendly protein sources. Insects have emerged as multifaceted resources, viewed not only as potential food items, but also as sources of traditional medicines and proteins. This study utilized response surface methodology (RSM) to ascertain the optimal extraction conditions for proteins from Musca domestica used in toad feeding, denoted as MDPs-T. The yield of MDPs-T was elevated to 18.3% ± 0.2% under these optimized conditions. Subsequently, the particle size, ζ-potentials, and structures of MDPs-T were analyzed and compared with the proteins derived from Musca domestica fed on a normal diet (MDPs-ND). This comparative analysis utilized a range of advanced techniques, involving UV spectroscopy, Fourier transform infrared spectroscopy (FT-IR), X-ray diffraction (XRD), high-performance gel permeation chromatography (HPGPC), and scanning electron microscopy (SEM). The outcomes have revealed a marginal disparity in the physical and chemical properties between MDPs-T and MDPs-ND. Derosination led to a reduction in the particle size of the MDPs by 10.98% to 62.81%. MDPs-T exhibited a higher proportion of low-molecular-weight components relative to MDPs-ND. Additionally, in a comparative analysis of amino acids, MDPs-T displayed a greater abundance of essential and total amino acids relative to MDPs-ND. Consequently, MDPs-T holds potential as a valuable food supplement for human consumption or as a nutrient-rich feed supplement for animals.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Insectos / Moscas Domésticas / Larva Límite: Animals Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Insectos / Moscas Domésticas / Larva Límite: Animals Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Suiza