Hydrolysis by Alcalase Improves Hypoallergenic Properties of Goat Milk Protein

Abstract

Goat milk is highly nutritious and is consumed in many countries, but the development of functional foods from goat milk has been slow compared to that for other types of milk. The aim of this study was to develop a goat milk protein hydrolysate (GMPH) with enhanced digestibility and better hypoallergenic properties in comparison with other protein sources such as ovalbumin and soy protein. Goat milk protein was digested with four commercial food-grade proteases (separately) under various conditions to achieve the best hydrolysis of αs -casein and β-lactoglobulin. It was shown that treatment with alcalase (0.4%, 60℃ for 30 min) effectively degraded these two proteins, as determined by SDS-PAGE, measurement of nonprotein nitrogen content, and reverse-phase high-performance liquid chromatography. Hydrolysis with alcalase resulted in a significant decrease in β-lactoglobulin concentration (almost to nil) and a ~40% reduction in the level of αs-casein. Quantification of histamine and TNF-α released from HMC-1 cells (human mast cell line) showed that the GMPH did not induce an allergic response when compared to the control. Hence, the GMPH may be useful for development of novel foods for infants, the elderly, and convalescent patients, to replace cow milk.

Identification and molecular docking study of novel cholesterol esterase inhibitory peptides from camel milk proteins

“…These results are attributed to the preferential cleavage of the enzyme used. Cleavage sites of alcalase are located in areas with a high density of hydrophobic AA, whereas bromelain and papain specifically cleave at AA adjacent to lysine, arginine, and phenyl-alanine, and bromelain preferred AA next to lysine, arginine, phenylalanine, and tyrosine (Jung et al, 2016).…”

Development and Characterization of a Hydrolyzed Goat Milk Protein/Chitosan Oligosaccharide Nano-Delivery System

“…그러나 산양유에는 젖소유와 마찬가지로 모유에 존재 하지 않는 주요 알레르기원인 베타락토글로불린이 존재하며 (Haenlein, 2004) 또한 젖소유에 비해 적은양이지만 위에서 응고되어 소 화를 방해할 뿐만 아니라 주요 알레르기원으로 작용하는 α s1 -카제인 이 존재한다 (Bernacka, 2011;Jung et al, 2016). 이러한 단점을 개선하기 위해 단백질 분해효소를 이용하여 베타락토글로불린과 α s1 -카제인을 포함한 산양유 단백질을 가수분해하여 유단백질의 알레르 기 항원성을 저감하는 연구가 수행되었다 (Jung et al, 2016) …”

Thermoase‐hydrolysed pigeon pea protein and its membrane fractions possess in vitro bioactive properties (antioxidative, antihypertensive, and antidiabetic)

“…Enzymatic hydrolysis is an important processing technique that has been reportedly used in liberating bioactive peptides from proteins (Saadi, Saari, Anwar, Abdul Hamid, & Ghazali, 2015). Different enzymes such as trypsin (Awosika & Aluko, 2019b; Kareem, 2018), pepsin (Lee & Byun, 2019; Vanvi & Tsopmo, 2016), alcalase (Ayala‐Niño et al, 2019; Jung et al., 2016; Nourmohammadi, Mahoonak, Alami, & Ghorbani, 2017; Saidi, Bellevile, Deratani, & Amar, 2016), pancreatin (Adiamo, Gbadamosi, & Abiose, 2016; Wijatniko & Murdiati, 2019) have been employed in the hydrolysis of proteins from an array of plant and animal materials. Thermoase is a bacterial neutral metalloprotease derived from Bacillus stearothermophilus ; it is an isoform of thermolysin (an endopeptidase) with specificity to rapidly hydrolyse peptide bonds at the N ‐terminal side of aromatic and hydrophobic amino acid (Nwachukwu, Girgih, Malomo, Onuh, & Aluko, 2014), which is quite different from the specificity of some other proteases.…”