Department of Chemical Engineering, University of Granada, Spain.
Food Funct. 2020 May 1;11(5):4376-4386. doi: 10.1039/d0fo00734j. Epub 2020 May 6.
The increasing world population has led to the need to search for new protein sources, such as insects, the harvesting of which can be economical and environmentally sustainable. This study explores the biological activities (angiotensin-converting enzyme (ACE) inhibition, antioxidant capacity, and dipeptidyl peptidase IV (DPP-IV) inhibition) of Tenebrio molitor hydrolysates produced by a set of food-grade proteases, namely subtilisin, trypsin, ficin and flavourzyme, and the degree of hydrolysis (DH), ranging from 5% to 20%. Trypsin hydrolysates exhibited the highest ACE inhibitory activity at a DH of 10% (IC 0.27 mg mL) in the experimental series, which was attributed to the release of short peptides containing Arg or Lys residues in the C terminus, and described as the ACE-inhibition feature. The levels of in vitro antioxidant activities were comparable to those reported for insect species. Subtilisin and trypsin hydrolysates at a DH of 10% displayed optimal DPPH scavenging and ferric reducing activities, which was attributed to the presence of 5-10-residue active peptides, as reported in the literature. Iron chelating activity was significantly favoured by increasing the DH, attaining a minimal IC of 0.8 mg mL at a DH of 20% regardless of the enzymatic treatment. Similarly, in vitro antidiabetic activity was significantly improved by extensive hydrolysis, and, more specifically, the presence of di- and tripeptides. In this regard, the combined treatment of subtilisin-flavourzyme at a DH of 20% showed maximal DPP-IV inhibition (IC 2.62 mg mL). To our knowledge, this is the first study evaluating the DPP-IV activity of Tenebrio molitor hydrolysates obtained from these commercial proteases. We conclude that Tenebrio molitor hydrolysates produced with food-grade proteases are a valuable source of active peptides that can be used as functional ingredients in food and nutraceutical preparations.
世界人口的增长导致人们需要寻找新的蛋白质来源，例如昆虫，其收获可以经济且环境可持续。本研究探索了由一组食品级蛋白酶（即枯草杆菌蛋白酶、胰蛋白酶、ficin 和风味蛋白酶）生产的黄粉虫水解物的生物活性（血管紧张素转换酶（ACE）抑制、抗氧化能力和二肽基肽酶 IV（DPP-IV）抑制）和水解度（DH），范围从 5%到 20%。在实验系列中，胰蛋白酶水解物在 DH 为 10%时表现出最高的 ACE 抑制活性（IC 0.27 mg mL），这归因于含有 Arg 或 Lys 残基的 C 末端短肽的释放，并被描述为 ACE 抑制特征。体外抗氧化活性水平与昆虫物种报道的水平相当。DH 为 10%的枯草杆菌蛋白酶和胰蛋白酶水解物表现出最佳的 DPPH 清除和铁还原活性，这归因于存在 5-10 个残基的活性肽，如文献中报道的。铁螯合活性随着 DH 的增加而显著增加，在 DH 为 20%时，IC 达到 0.8 mg mL 的最小值，无论酶处理如何。同样，广泛水解显著提高了体外抗糖尿病活性，更具体地说，二肽和三肽的存在。在这方面，枯草杆菌蛋白酶-风味蛋白酶在 DH 为 20%的联合处理显示出最大的 DPP-IV 抑制（IC 2.62 mg mL）。据我们所知，这是首次评估这些商业蛋白酶获得的黄粉虫水解物的 DPP-IV 活性的研究。我们得出结论，用食品级蛋白酶生产的黄粉虫水解物是具有生物活性的肽的有价值来源，可作为功能性成分用于食品和营养保健品制剂。
