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International Dairy Journal 97 (2019) 111E119

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International Dairy Journal 97 (2019) 111E119 International Dairy Journal 97 (2019) 111e119 Contents lists available at ScienceDirect International Dairy Journal journal homepage: www.elsevier.com/locate/idairyj Physicochemical properties and issues associated with trypsin hydrolyses of bovine casein-dominant protein ingredients * Aaron S.L. Lim, Mark A. Fenelon, Noel A. McCarthy Food Chemistry & Technology Department, Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland article info abstract Article history: Milk protein concentrate (MPC) and sodium caseinate (NaCas) were hydrolysed using the enzyme trypsin Received 25 March 2019 and the subsequent physical properties of the two ingredients were examined. Trypsin hydrolysis was Received in revised form carried out at pH 7 and at 45 C on 11.1% (w/w) protein solutions. Heat inactivation of trypsin was carried 23 May 2019 out when the degree of hydrolysis reached either 10 or 15%. Size-exclusion chromatography and elec- Accepted 23 May 2019 trophoresis confirmed a significant reduction in protein molecular weight in both ingredients. However, Available online 6 June 2019 whey proteins in MPC were more resistant to trypsin hydrolysis than casein. Oil-in-water emulsions were prepared using intact or hydrolysed protein, maltodextrin, and sunflower oil. Protein hydrolysis had a negative effect on the subsequent physical properties of emulsions, compared with non-hydrolysed proteins, with a larger particle size (only for NaCas stabilised emulsions), faster creaming rate, lower heat stability, and increased sedimentation observed in hydrolysed protein emulsions. © 2019 Elsevier Ltd. All rights reserved. 1. Introduction with a protein content of ~90% (w/w) and approximately 1.3% (w/ w) sodium content on a dry basis (Augustin, Oliver, & Hemar, 2011). Casein-dominant protein ingredients are widely used in dairy- Although MPC and NaCas are highly nutritious food ingredients, based formulations due to their amphiphilic nature and good cow milk allergy (CMA) generally occurs in children and is often heat stability. Caseins represent ~80% (w/w) of the total nitrogen in out-grown by the age of four, although, CMA may also last for life or bovine milk and are utilised in food products such as cream li- alternatively commence in adulthood (El-Agamy, 2007). Allergy queurs, coffee whiteners, whipping creams, cheese analogues, symptoms due to CMA can be immediate as a result of Immuno- cereal goods, artificial meats, and dietetic foods (Fox & Kelly, 2004). globulin E-induced reactions leading to respiratory, cutaneous or Milk protein concentrates (MPC) are obtained from pasteurised intestinal symptoms, as well as anaphylactic shock or can result in a skimmed milk using membrane separation, namely, ultrafiltration delayed reaction that could lead to skin or intestinal discomfort and diafiltration followed by evaporation and spray drying (Mistry (Sicherer, 2000; Taylor, 1986). Therefore, the use of milk protein & Hassan, 1991). Diafiltration is used to obtain MPC with a protein hydrolysates in food products can be beneficial in improving content of 70% (w/w) by further filtering out lactose and minerals hypoallergenicity and ease of digestion (O'Mahony, Ramanujam, present in the retentate (Mistry, 2002). MPC powders are cat- Burgher, & O'Callaghan, 2011; Sinha, Radha, Prakash, & Kaul, egorised by their protein content (w/w), with the ratio of casein to 2007; Terracciano, Isoardi, Arrigoni, Zoja, & Martelli, 2002)as whey protein remaining the same as those naturally found in skim well as providing compounds with useful biological activity milk (Kelly, 2011). Alternatively, sodium caseinate (NaCas), a form (Fekete, Givens, & Lovegrove, 2015; Hernandez-Ledesma, Miguel, of water-soluble casein, is obtained by adding dilute acid or lactic Amigo, Aleixandre, & Recio, 2007; Sakana, Tachibana, Ishihara, & acid starter cultures to skim milk until pH 4.6 is achieved, resulting Juneja, 2005). Pre-digested milk proteins have beneficial proper- in the solubilisation of calcium phosphate and precipitation of ties such as lowering gastrointestinal irritation and have better gut casein. With the whey separated, sodium hydroxide is then added digestibility and adsorption compared to intact proteins to neutralise the acid casein resulting in the formation of NaCas (Hernandez-Ledesma, García-Nebot, Fernandez-Tom e, Amigo, & Recio, 2014). Hydrolysis of milk protein is often achieved using proteolytic enzymes, namely, trypsin, papain, pepsin, chymotrypsin or subtil- * þ Corresponding author. Tel.: 353 2542238. & E-mail address: [email protected] (N.A. McCarthy). isin (Banach, Lin, Lamsal, 2013; Carreira, De Marco, Dias, Morais, https://doi.org/10.1016/j.idairyj.2019.05.014 0958-6946/© 2019 Elsevier Ltd. All rights reserved. 112 A.S.L. Lim et al. / International Dairy Journal 97 (2019) 111e119 & Silvestre, 2004; Hong et al., 2015; Rajarathnam, Nongonierma, 2.2. Preparation of milk protein concentrate and sodium caseinate O'Sullivan, Flynn, & FitzGerald, 2016), with the amount of peptide hydrolysates bonds cleaved during the hydrolysis process determining the de- gree of hydrolysis (DH) (Adler-Nissen, 1986). Controlled hydrolysis MPC and NaCas powders were dispersed and stirred in deion- of casein and whey proteins using enzymes results in a mixture of ised water (11.1%, protein basis, w/w, in water) at 50 C for 2 h and hydrolysed protein, unhydrolysed protein, and low molecular left overnight at 4 C. Subsequently, ultrasonication of the disper- weight material (Kilara & Chandan, 2011). sions was carried out using an ultrasound device (Hielscher The use and effective delivery of pre-digested milk protein UIP1000hd, Hielscher Ultrasonics Gmbh, Warthestrabe 21 D-14513, ingredients in complete nutritional formulations means their Berlin, Germany), fitted with a 22 mm diameter BS2d22 (F) sono- incorporation in to complex emulsion systems. Oil-in-water (O/ trode for 30 s at 100 kHz to ensure complete hydration. Hydrolysis W) emulsions are an integral part of the macronutrient compo- was carried out using trypsin at pH 7.0 (45 C). An enzyme: protein sition of specialised nutrition formulations, with the utilisation ratio of 1:50 and 1:10 was applied to achieve a 10 and 15% DH, of hypoallergenic and high-tolerance formulae for clinical and respectively. Protein dispersions were stirred with an over-head infant nutrition purposes produced with milk protein hydroly- stirrer at 300 rpm and the pH was maintained at pH 7.0 with 1 N sates (Schroder,€ Berton-Carabin, Venema, & Cornacchia, 2017). NaOH using a Metrohm 842 Titrando pH stat dosing unit (Metrohm Milk protein hydrolysates have been used successfully as an Ltd., Herisau, Switzerland) with Metrohm TiAMO software. The DH emulsifier to form O/W emulsion based model systems in is described as the number of peptide bonds cleaved (h) over the numerous studies (Drapala, Auty, Mulvihill, & O'Mahony, 2016; number of total peptide bonds (htot), as described in equation (1) Euston, Finnigan, & Hirst, 2001; Schroder€ et al., 2017). Howev- (Adler-Nissen, 1986): er, Singh and Dalgleish (1998) reported that whey protein hy- drolysates with a DH of more than 28% have sub-standard 1 1 1 % DH ¼ 100 Â B Â NB Â Â Â (1) emulsifying ability, with emulsification capacity greatest at a MP htot 10e20% DH. According to Chobert, Bertrand-Harb, and Nicolas (1988), hydrolysates should have a molecular mass distribution where B is the volume of base solution, Nb is the normality of the base, 1/a is the average dissociation degree of a-NH groups (2.71 at of above 5 kDa to maintain its emulsifying property. Good emulsifying properties have been found in peptides with a chain pH 7.0 and 45 C), MP is the molecular mass of protein and htot is the ¼ length of 20 amino acids or more (Chaplin & Andrew, 1989; Lee, number of peptide bonds in the protein substrate (i.e., MPC 8.32 ¼ Shimizu, Kaminogawa, & Yamauchi, 1987). It has been suggested and casein 8.2). Enzymatic hydrolysis was terminated by heating the protein that the peptide length has less of an impact on emulsifying ability compared with the hydrophobic/hydrophilic sequence of dispersions in a water bath at 85 C for 20 min. The pH stat dosing unit was also used to adjust unhydrolysed protein dispersions (MPC the amino acids that form the peptides (Rahali, Chobert, Haertle, & and NaCas) to pH 7.0 using 1 N NaOH at 45 C followed by heating in Gueguen, 2000). Numerous studies have reported work on whey protein hy- a water bath at 85 C for 20 min. drolysis and their use in subsequent emulsion systems (Drapala et al., 2016; Schroder€ et al., 2017). However, studies on hydroly- 2.3. Protein and protein hydrolysate analysis sis of micellar casein and caseinates with the goal of forming stable O/W emulsions have been limited. The use and interest in 2.3.1. Electrophoresis ® using casein hydrolysates is becoming more industrially relevant, Electrophoresis was carried out using NuPAGE bis-Tris mainly due to the rapid development and expansion of whey electrophoresis system (Life Technologies, Carlsbad, California, protein production, and thus the significant development of both USA), under reducing conditions. Protein dispersions were À micellar and non-micellar casein streams. The significant pro- diluted to 3 mg mL 1 with Milli-Q water and mixed with 2.5 mL ® ® duction of casein needs to be absorbed and new uses for these NuPAGE LDS sample buffer (4 Â)and1mL NuPAGE reducing ingredients are been sought. Uses in specialised infant formulas agent (10 Â). The mixtures were then heated for 10 min at 80 C and other medical nutritional products add high-value to these using an incubator. Protein samples and a molecular mass ingredients, but there are significant processing challenges for standard (Mark12™ Unstained Standard, Thermo Fisher Scien- ® industry. The current study aimed to highlight some of these is- tific Inc.) were loaded into pre-casted NuPAGE 4e12% gradient ® sues and add to the limited previous knowledge on casein hy- bis-Tris gel with NuPAGE MOPS SDS running buffer. Electro- drolyses. Therefore, the aim of this study was to develop phoresiswasrunatinXCellSureLockTM Mini-Cell with constant emulsions using casein-based hydrolysates from MPC and NaCas voltage of 200 V for 50 min.
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