Malting Barley Grain Non‐specific Lipid‐Transfer Protein (ns‐LTP): Importance for Grain Protection

A basic protein (pI < 9) was isolated to homogeneity from a domestic cultivar of malting barley grain (Hordeum vulgare). In its unreduced form it exists as a dimer of a 9 kDa protomer with four disulphide bridges. These characteristics together with protein sequence data revealed that the isolated protein belongs to the class of ns‐LTP. The antifungal potency of malting barley grain ns‐LTP was examined on Saccharomyces cerevisiae, Candida albicans and the plant pathogen Fusarium solani growth in vitro. It was found that ns‐LTP inhibits Saccharomyces and Fusarium growth; the concentration required for 50% inhibition after 24 h of incubation (IC₅₀) was 100 and 80 μg/mL, respectively. On the basis of these results, the importance of ns‐LTP for barley grain protection from fungal diseases has been discussed.     

Gel‐enhancing effect and protein cross‐ linking ability of tilapia sarcoplasmic proteins

BACKGROUND: Tilapia (Oreochromis niloticus) sarcoplasmic proteins contain substantial transglutaminase (TGase) activity. The enzyme catalyzes the protein cross‐linking reaction, resulting in a more elastic gel. The objective was to investigate the gel‐enhancing effect of sarcoplasmic proteins from tilapia as related to TGase activity. RESULTS: Total TGase activity of sarcoplasmic proteins concentrate (SpC) increased about 3.6‐fold after ultrafiltration using 30 kDa membrane, but specific activity remained unchanged, indicating minimal TGase purification by ultrafiltration. Addition of 1 mg mL^?1 SpC containing 40 units TGase activity induced cross‐linking of tilapia actomyosin, and the extent of cross‐linking increased with added level of SpC. Myosin heavy chain (MHC) and troponin were preferably cross‐linked by tilapia SpC, while actin and tropomyosin were not affected. Higher retention of MHC was observed concomitantly with greater content of cross‐linked protein when SpC was added to lizardfish surimi. Lizardfish surimi with 10 g kg^?1 SpC added and pre‐incubated at 37 °C for 1 h exhibited 91.6% and 26.7% increase in breaking force and deformation, respectively, when compared to the control. CONCLUSIONS: Residual TGase activity in SpC played an important role in catalyzing the protein cross‐linking and enhancing actomyosin gelation. SpC could be a potential ingredient for improving textural properties of fish protein gel. Copyright © 2007 Society of Chemical Industry     

Antioxidant activities of pepsin hydrolysates of water‐ and salt‐soluble protein extracted from pork hams

The objective of this study was to evaluate the antioxidant activities of pepsin‐digested water‐soluble protein (WSP) and salt‐soluble protein (SSP) extracted from pork ham. WSP and SSP were hydrolysed by pepsin for 2–10 h with 2‐h increments. The protein hydrolysates by pepsin were analysed by sodium dodecyl sulphate‐polyacrylamide gel electrophoresis, and reducing power of the hydrolysates was measured. In addition, antioxidant activity of the hydrolysates was determined using linoleic acid emulsion system. Protein bands with molecular weight higher than 7 kDa in WSP and SSP were completely hydrolysed by pepsin after 2 h of digestion time. WSP hydrolysates (WSPH) and SSP hydrolysates (SSPH) had higher ferric reducing power than controls (WSP and SSP without pepsin digestion). Reducing powers of WSPH were higher than those of SSPH, regardless of digestion time. The oxidative activity of linoleic acid was predominantly inhibited by the addition of WSPH and SSPH, especially 0.5% protein hydrolysate. These results indicate that several functional peptides of pork protein digested by pepsin might have antioxidant activity, and thus they may be used as an antioxidant agent in muscle food system.     

Water‐soluble myofibrillar proteins prepared by high‐pressure homogenisation: a comparison study on the composition and functionality

To expand utilisation of meat in various products, the characterisation and functionalities of water‐soluble myofibrillar proteins (WSMP) induced by high‐pressure homogenisation (HPH) were determined by comparison with those of soy protein isolate (SPI) and whey protein isolate (WPI). WSMP had high contents of protein (87.40%), which was mainly composed of myosin, actin and tropomyosin. The essential amino acids of WSMP achieved the FAO/WHO/UNO (2007) standards for preschool children, and the contents of lysine and sulphur‐containing amino acids of WSMP were higher than those of SPI, making it desirable for children formulations. WSMP showed higher surface hydrophobicity while its water solubility was similar to that of SPI, but lower than that of WPI. WSMP demonstrated superior water/oil absorption capacities and emulsifying properties. The fibrous structure and high hydrophobic activity characteristics of WSMP were able to stabilise oil droplets with submicron droplet size, consequently responsible for its excellent emulsifying properties.     

Protein quality of drum‐processed cereal–bean–sardine composite supplementary foods for preschool‐age children

Acute, severe undernutrition during childhood remains a common health problem in many parts of the world and makes a significant contribution to childhood mortality. This study was conducted to evaluate the protein quality and growth/rehabilitation potential of supplementary foods developed from locally produced materials in Tanzania. Six diets, namely rice meal (RM), bean meal (BM), rice–bean meal (RBM), rice–bean–sardines meal (RBSM), corn–bean–sardines meal (CBSM) and corn–bean meal (CBM), were formulated to maximise the amino acid score as recommended by FAO/WHO/UNU for preschool children. Biological qualities of the diets, including apparent and true protein digestibility, net protein retention ratio, food efficiency ratio, protein digestibility‐corrected amino acid score and rehabilitation potential, were evaluated using Sprague Dawley weanling rats. Net protein retention ratio varied significantly (p < 0.05) among control diet (0.93), RBSM (0.92), CBSM (0.86), RM (0.66), RBM (0.44), CBM (0.28), BM (0.12) and corn meal (CM) diet (?0.40). True protein digestibility ranged between 82 and 99%, with BM showing the lowest digestibility. The protein digestibility‐corrected amino acid scores were 100% (control diet), 77% (CBSM), 89% (RBSM), 58% (RM), 90% (RBM), 47% (CBM), 85% (BM) and 48% (CM). Two test diets, CBSM and RBSM, showed the greatest potential to support growth and rehabilitation of undernourished rats, while CBM, RBM, BM and CM did not display acceptable growth. These results suggest that cereal–bean–sardine composites are of high quality and have potential for use as supplementary/rehabilitation foods for preschool‐ and school‐age children as well as adults. Copyright © 2004 Society of Chemical Industry     

Lactic acid‐mediated isolation of alpha‐, beta‐ and kappa‐casein fractions by isoelectric precipitation coupled with cold extraction from defatted cow milk

The present study focused on the isolation of individual caseins (α, β and κ) from defatted cow's milk using lactic acid‐mediated isoelectric precipitation coupled with cold extraction technique, followed by purification using sucrose‐based density gradient centrifugation method. In vitro characterisation of the isolated casein fractions confirmed preservation of micellar morphology throughout the experimental conditions with anionic surface charge and wider particle size range. The RP‐HPLC analysis showed a peak at retention time of 25.13 min and 27.84 min for α‐casein and β‐casein, respectively. Results confirmed isolation of pure casein fractions from cow's milk which could serve as a rich source of bioactive peptides for nutraceutical/pharmaceutical applications.     

Degradation of N‐(1‐Deoxy‐d‐xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d‐xylulos‐1‐yl)proline using thermal treatment

The formation and degradation of N‐(1‐Deoxy‐d ‐xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d ‐xylulos‐1‐yl)proline, derived from the secondary amine Maillard reaction in xylose‐amino acid model solutions, were detailed in this study. The identification and quantitative analysis of N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)proline were carried out using high‐performance anion‐exchange chromatography and high‐performance liquid chromatography. The formation of intermediate and advanced products derived from N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)proline was also tested using an UV‐Vis spectrophotometer to gain a better comparing of the degradation process of the two important Maillard reaction products using thermal treatment. Results showed that the degradation of N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)glycine was more significant than N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)proline. Moreover, xylose was tested in the degradation products of both N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)proline, which indicated that the degradation of N‐substituted 1‐amino‐1‐deoxyketoses was a reversible reaction to form reducing sugar.     

Protein digestibility‐corrected amino acid scores,acceptability and storage stability of ready‐to‐eat supplementary foods for pre‐school age children in Tanzania

This study was conducted to evaluate protein quality, acceptability and storage stability of processed cereal–bean–sardine composite foods for pre‐school age children in Tanzania. Four composite products namely corn–bean–sardine meal (CBSM), bean meal (BM), sorghum–bean–sardine meal (SBSM) and rice–bean–sardine meal (RBSM) were formulated to maximize the amino acid score for pre‐school age children and were processed by extrusion, drum‐processing and conventional cooking. The products were evaluated for true protein digestibility (TPD) and protein digestibility‐corrected amino acid score (PDCAAS). The TPD and PDCAAS were highest in the extruded products. The TPD values for the products ranged from 82 to 93%. The PDCAAS values for the composite foods were 64–86% and were greater than the minimum value of 60% recommended by FAO/WHO/UNU. There were no significant (p > 0.05) variations in the amino acid contents for foods processed by extrusion, drum‐processing or conventional cooking. Threonine was most limiting in the CBSM, SBSM and RBSM while methionine + cysteine were most limiting in the BM. Sensory evaluation showed that, relative to the traditional cornmeal—Uji, the extruded CBSM and SBSM had significantly superior (p ≤ 0.05) texture and highly acceptable color and taste. Storage of the products up to 16 weeks at 38 °C resulted in a small but significant increase (p ≤ 0.05) in the malondialdehyde concentrations; nevertheless, the levels remained within the acceptable range found in processed commercial supplements. Total acids, pH and organoleptic attributes did not change significantly (p > 0.05) during storage and the foods were acceptable to the end of the storage period. Copyright © 2005 Society of Chemical Industry     

3‐Chloropropane‐1,2‐diol (3‐MCPD) in Soy Sauce: A Review on the Formation,Reduction, and Detection of This Potential Carcinogen

Soy sauce, a dark‐colored seasoning, is added to enhance the sensory properties of foods. Soy sauce can be consumed as a condiment or added during the preparation of food. There are 3 types of soy sauce: fermented, acid‐hydrolyzed vegetable protein (acid‐ HVP), and mixtures of these. 3‐Chloropropane‐1,2‐diol (3‐MCPD) is a heat‐produced contaminants formed during the preparation of soy sauce and was found to be a by‐product of acid‐HVP‐produced soy sauce in 1978. 3‐MCPD has been reported to be carcinogenic, nephrotoxic, and reproductively toxic in laboratory animal testing and has been registered as a chemosterilant for rodent control. 3‐MCPD is classified as a possible carcinogenic compound, and the maximum tolerated limit in food has been established at both national and international levels. The purpose of this review is to provide an overview on the detection of 3‐MCPD in soy sauce, its toxic effects, and the potential methods to reduce its concentration, especially during the production of acid‐HVP soy sauce. The methods of quantification are also critically reviewed with a focus on efficiency, suitability, and challenges encountered in analysis.     

R‐Index Measure of Microencapsulated Tributyrin in Gamma‐Cyclodextrin Influenced by Drying Method

Microencapsulation is commonly used in the food industry for a variety of purposes including added ingredient functionally and taste‐masking for those ingredients with negative sensory qualities. Tributyrin (TB), a source intestinally‐essential butyric acid, possesses negative aroma (cheesy, fecal) and taste (bitter) qualities. This has significantly limited its use in food applications for the potential improvement of intestinal health. Utilizing spray drying and low‐temperature oven drying, microcapsules containing TB were produced using whey (WPI), WPI and inulin, and gamma‐cyclodextrin (GCD). To determine how microcapsule formulation and drying method affected the perception of TB relative to a control, microencapsulated and free TB were added to an infant formula system and evaluated using the rating method to determine R‐index measures. Pooled R‐index measures (α = 0.01, 2‐tailed, and n = 170) indicated that the only microcapsule not significantly different from the control (R‐index below 57.95%) was the GCD and TB oven dried (GCT OD) microcapsule. All other WPI, WPI–inulin, and GCD and TB spray‐dried (GCT SD) microcapsules were all significantly different from the control. Average individual R‐index results indicated that all microcapsules in infant formula, except for GCT OD, were significantly different (P < 0.01) from the control formula but not from free TB. Spray drying may create microcapsules with surface TB and disturb the GCD–TB complex, allowing free, and surface TB to be perceived by the panelists. The GCT OD microcapsule has the potential to be used for the potential oral treatment of intestinal disorders in functional food applications without the negative sensory qualities of TB.     

Angiotensin‐converting enzyme‐inhibitory activity in protein hydrolysates from normal and anthracnose disease‐damaged Phaseolus vulgaris seeds

BACKGROUND: Bean seeds are an inexpensive source of protein. Anthracnose disease caused by the fungus Colletotrichum lindemuthianum results in serious losses in common bean (Phaseolus vulgaris L.) crops worldwide, affecting any above‐ground plant part, and protein dysfunction, inducing the synthesis of proteins that allow plants to improve their stress tolerance. The aim of this study was to evaluate the use of beans damaged by anthracnose disease as a source of peptides with angiotensin‐converting enzyme (ACE‐I)‐inhibitory activity. RESULTS: Protein concentrates from beans spoiled by anthracnose disease and from regular beans as controls were prepared by alkaline extraction and precipitation at isolelectric pH and hydrolysed using Alcalase 2.4 L. The hydrolysates from spoiled beans had ACE‐I‐inhibitory activity (IC₅₀ 0.0191 mg protein mL^?1) and were very similar to those from control beans in terms of ACE‐I inhibition, peptide electrophoretic profile and kinetics of hydrolysis. Thus preparation of hydrolysates using beans affected by anthracnose disease would allow for revalorisation of this otherwise wasted product. CONCLUSION: The present results suggest the use of spoiled bean seeds, e.g. anthracnose‐damaged beans, as an alternative for the isolation of ACE‐I‐inhibitory peptides to be further introduced as active ingredients in functional foods. © 2012 Society of Chemical Industry     

Barley Grain Non‐specific Lipid‐Transfer Proteins (ns‐LTPs) in Beer Production and Quality

Plant non‐specific lipid‐transfer proteins (ns‐LTPs) are known for their ability to transfer various lipids between membranes in vitro. These ubiquitous basic proteins, that all share alpha structure stabilized by four disulphide bridges, are characterized by the presence of a hydrophobic cavity able to accommodate lipid molecules. According to molecular mass, this multigene family is subdivided into two subfamilies, ns‐LTP1 (9 kDa) and ns‐LTP2 (7 kDa); both located in the aleurone layer of the cereal grain endosperm. Ns‐LTP1 is a prominent protein in barley grain, malt and beer. Numerous studies performed on its structure and function confirm its important role in grain protection, as well as brewing technology. As the major beer protein crucial for many aspects of brewing, ns‐LTP1 can affect beer production and quality. Comparatively, there is less data available on the less abundant ns‐LTP2. In this review, the focus is on recent progress on the structure, biological and technological function of barley grain ns‐LTP1 and ns‐LTP2, with an emphasis on their importance in brewing.