Food Processing Aid Research Articles

Sodium reduction in processed foods, including processed meats, in Africa: A systemic review

The use of sodium in processed foods, including meats, has been in existent over centuries. Its use is mainly as a food and meat processing aid, and a preservative and flavourant. Even with modern methods of food processing, sodium is still essential in food and meat derivatives due to different dietary demands by consumers. Sodium chloride, sodium nitrate and nitrite are common in meat processing for various uses such as curing, smoking and brining. Due to the increasing global sodium intake, chronic adverse health effects, such as cardiovascular diseases, hypertension, stroke, cancers, among others, have also been on the rise, particularly in urban areas. African countries have a proportional increase of dietary sodium due to the adoption of western diets with high sodium and saturated fats. Subsequently, South Africa promulgated legislation that prescribed the first mandatory sodium limits in 2013. The purpose of this review is to determine, (1) the sodium reduction interventions agreed by African states in forums and meetings in the past five years (2017-2021) and, (2) sodium reduction strategies recommended through research by African scholars. This systemic review was conducted from English literature published between 2017 and 2021, using Science web, MEDLINE, CINAHL, PsycINFO, Science Direct, PubMed, Google Scholar, with a specific focus on African countries. From the findings of this systemic review, there were minimal sodium reduction interventions by African states, emanating from published forums and meetings, to establish collaborated sodium reduction strategies in processed foods. The studies conducted by African scholars in the past five years recommended sodium reduction interventions, such as legislative framework, product reformulation, monitoring models and consumer awareness, with most studies done in South Africa. It is evident that to have a meaningful impact on the control and reduction of dietary sodium, African countries require existing diplomacies to collaborate on sodium reduction efforts with public and private partnerships; this can be coordinated through inter-trade treaties among the African states. This requires an increase in research, commitment and the will to reduce dietary sodium in processed foods and meat by all member states. Key words: sodium, reduction, processed, meat, processing, effects, hypertension, nitrate, nitrite

Enzymes as Potencial Source for Clean Label Bakery Product: Part 1, Mechanism and Application Single Enzym

Background: Increased public awareness of consuming healthy food has driven bakery industry to applied production methods and components of food products that are tailored to the market needs. Food product can be positioned as natural, organic, or free from additives/ preservatives which often referred to clean label trend. Bakery industry commonly using chemical emulsifier as component which improve characteristic and quality baked goods. Usage of chemical component is not appropriate with perception of clean label, although it is not yet clear what a clean label exactly means. Chemical emulsifier has potentially negative effect to health such as intestinal inflammation, obesity, metabolic syndrome and glucose resistance based on several research. Food enzyme can be alternative to replace chemical emulsifier and potentially source of clean label bakery product. Therefore, sustainable study was needed to find role single enzym as food additive and processing aid in bakery product application.Scope and approach: This review explain about the role single enzyme application in bakery product which discuss under three main headings include (i) enzyme as food additive and processing aid, ii) Characteristic enzyme to improve bakery product processing (dough mixing, fermentation, baking), sensories properties and appearance iii) Enzyme mechanism and application to enhance bakery product quality. Optimization of the role and function of enzymes can be conduct by enzyme quality validation through baking tests including formulation development, process parameters (dough rheology, handling machine and baking parameter), product appearance and sensory characteristics.Key findings and conclusion: Food enzymes play a role in enzymatic modifications as biodegradable proteins which not affected to nutritional value baked goods. Enzyme technology is a clean process with low energy consumption, low waste production, safe and less toxic working environment. Therefore, enzyme has potential to fulfill clean label trends and encourage researchers and developers in food industry to explore potential use of food enzymes in bakery products. Enzymes which usually used in bakery come from hydrolase class (amylase, protease, hemicellulase, lipase, xylanase and asparaginase), oxidoreductase class (lipoxygenase and glucose oxidase) and transferase class (transglutaminase). Application enzymes in bakery processs have their respective roles according to enzymes specific characteristics. Enzymes has the main role such as improve rheological and functional properties of dough according to baked goods type, enhance quality and characteristics baked goods including volume, crumb texture, color, taste and extend shelf life (antistaling). Sustainable research and development was needed to optimize the role of enzyme in baked goods by several approach such as (i) incorporation enzymes with other ingredients in the food matrix, (ii) parameters which affect to the work of enzymes in food systems (iii) potential of enzyme combinations to improve baked goods quality and (iv) understanding of usage regulation enzymes as food additives and food processing. Keyword: enzyme, clean label, food additive, processing aid, bakery product

Appraisal of cytotoxicity and acrylamide mitigation potential of L-asparaginase SlpA from fish gut microbiome.

L-asparaginase catalyzes the hydrolysis of L-asparagine toL-aspartic acid and ammonia. It has application in the treatment of acute lymphoblastic leukemia in children, as well as in other malignancies, in addition to its role as a food processing aid for the mitigation of acrylamide formation in the baking industry. Its use in cancer chemotherapy is limited due to problems such as its intrinsic glutaminase activity and associated side effects, leading to anincreased interest in the search for novel L-asparaginases without L-glutaminase activity. This study reports the cloning and expression of an L-asparaginase contig obtained from whole metagenome shotgun sequencing of Sardinella longiceps gut microbiota. Purified recombinant glutaminase-free L-asparaginase SlpA was a 74kDa homodimer, with maximal activity at pH 8 and 30°C. Km and Vmax of SlpA were determined to be 3.008mM and 0.014mM/min, respectively. SlpA displayed cytotoxic activity against K-562 (chronic myeloid leukemia) and MCF-7 (breast cancer) cell lines with IC50 values of 0.3443 and 2.692 U/mL, respectively. SlpA did not show any cytotoxic activity against normal lymphocytes and was proved to be hemocompatible. Pre-treatment of biscuit and bread dough with different concentrations of SlpA resulted in a clear, dose-dependent reduction of acrylamide formation during baking. KEY POINTS: • Cloned and expressed L-asparaginase (SlpA) from fish gut microbiota • Purified SlpA displayed good cytotoxicity against K-562 and MCF-7 cell lines • SlpA addition caused a significant reduction of acrylamide formation during baking.

Optimization by fractional factorial design to initiate L-asparaginase production by Enterobacter xiangfangenesis

L-asparaginase has been used world wide as a potential anticancerous agent as well as an excellent food processing aid. In industrial production processes, process optimization is critical because even minor improvements can make a big difference in terms of commercial success. The adjustment of nutritional and physical parameters in any bioprocess would result in an increase in the productivity of any metabolite. The production of L-asparaginase in the current study with implementation of statistical design (fractional factorial design) increased to about 109.72 IU/ml by Enterobacter xiangfangensis. The significant factors that raised the L-asparaginase production were: Lasparagine (1g%) [Factor: A], maltose (0.25g%) [Factor: B], pH (6.3)[Factor : C] and KH2PO4 (0.2 g%) [Factor : D]. The sequential contributing factors that increased L-asparaginase production according to the model represented by Pareto charts were Lasparagine [Factor: A], maltose [Factor: B] and combination of L-asparagine – maltose [Factors AB] respectively. The normal plot represented the model to be acceptable and considerable. The predicted as well as experimental values appeared closed to each other graphically. The model F-value was 9.62 indicating that the model was statistically significant.

Heterologous expression and molecular modelling of L-asparaginase from Bacillus subtilis ETMC-2

Bacterial L-asparaginase is the key therapeutic enzyme in cancer therapy and is also witnessing demand as a food processing aid. In this study, L-asparaginase of newly isolated Bacillus subtilis ETMC-2 was cloned and over-expressed in Escherichia coli as an active soluble protein using ligation independent cloning strategy. The molecular mass was estimated to be 40 kDa and was optimally active at 50 °C. Zymography revealed that the enzyme was active in homo-tetramer state (~160 KDa). The encoded protein after BLASTp analysis on NCBI showed 99.73% similarity with L-ASNase that of Bacillus sp. Physico-chemical properties were predicted using Protparam leading to categorization of the enzyme as a stable protein with an instability index (II) of 19.02. The calculated aliphatic index (85.44) indicated the high thermal stability of the protein with GRAVY value of −0.317. Protein-Ligand docking revealed that the residues Thr89, Thr121, and Asp122 were fundamental in protein–ligand complexation. After homology modelling, model validation was performed using Ramachandran plot, VERIFY3D, and RMSD. The paper describes cloning, heterologous expression, catalytic characteristics and physico-chemical properties of the type II B. subtilis L-ASNase.

Production of Spray-dried “Terung Asam” (Solanum lasiocarpum Dunal) Powder

Easily perishable and highly seasonal “Terung Asam” (Solanum lasiocarpum Dunal) fruit, a geographical indication plant of Sarawak, was converted into powder for shelf life extension. Spray drying was employed with a range of inlet temperature (140 - 180 °C) and the slurry was cooperated with food graded maltodextrin (5 - 25 % w/w) as food processing aid. The spray-dried “Terung Asam” powders were analysed for process yield, moisture content (Mc), water activity (Aw), hygroscopicity (Hg), water solubility index (WSI), bulk density and colour. The reconstituted powders were assessed by determining total soluble solid (TSS), pH, viscosity and colour. The results indicated that the increase in inlet temperature had resulted in reduction in Mc, Aw, and Hg. In addition, higher concentration of maltodextrin led to reduction in Mc and Hg. At the spray drying inlet temperature of 160 °C and feed added with 25 % w/w maltodextrin, “Terung Asam” powder with the following optimal physicochemical properties was produced: Mc, 2.95±0.42 %; Aw, 0.11±0.02; Hg, 17.76±0.28 %; WSI, 98.89±1.37 %; and wettability, 621.60±119.03 s. The optimized reconstituted powder had lower L*, a* and b* values than the fresh juice, indicating it is lighter in colour, less reddish and less yellowish. Overall, the production of “Terung Asam” using spray drying is feasible with the addition of food processing aid.

The use of microbial transglutaminase in a bread system: A study of gluten protein structure, deamidation state and protein digestion

Microbial transglutaminase (mTG) catalyses the formation of protein crosslinks, deamidating glutamine in a side-reaction. Gluten deamidation by human tissue transglutaminase is critical to activate celiac disease pathogenesis making the addition of mTG to wheat-based products controversial. The ability of mTG (0–2000 U.kg−1) to alter gluten’s structure, digestibility and the deamidation state of six immunogenic gluten peptides within bread was investigated. Gluten’s structure was altered when mTG exceeded 100 U.kg−1, determined by confocal microscopy, extractability and free sulfhydryl assays. The effect of mTG on six immunogenic peptides was investigated by in vitro digestion (INFOGEST) and mass spectrometry. The addition of mTG to bread (0–2000 U.kg−1) did not alter the deamidation state or digestibility of the immunogenic peptides investigated. Overall, this investigation indicated that the addition of mTG to bread does not create activated gluten peptides. This analysis provides evidence for risk assessments of mTG as a food processing aid.

Optimization of process conditions and evaluation of pH & thermal stability of recombinant l-Asparaginase II of Erwinia carotovora subsp. atroseptica SCRI 1043 in E. coli

l-asparaginase (EC 3.5.1.1) is an important antineoplastic agent, used in the acute lymphoblastic leukemia chemotherapy and well known as food processing aid for reducing the acrylamide formation in starch rich foods. In the present study, we have cloned, expressed and purified recombinant l-asparaginase II of Erwinia carotovora subsp. atroseptica SCRI 1043 in E. coli. To study the best condition for performance of recombinant enzymes, pH and temperature of process conditions were optimized using response surface methodology. Optimal pH and temperature for enzyme were found to be 7.79 and 47.21 °C. Furthermore, the purified recombinant enzyme was subjected to thermal deactivation studies. pH and thermal stability of enzyme was studied at various combinations of pH and temperature. In addition, thermodynamic parameters of recombinant l-asparaginase II were evaluated. It was observed that recombinant l-asparaginase II enzyme is more stable at pH 8.5 at 35 °C relatively pH 6.5, 7.5 and 9.5. It was also observed that recombinant l-asparaginase II is more stable at pH 8.5 than pH 9.6 and 7.6 at higher temperature.

Translation of plasma technology from the lab to the food industry

The potential of cold plasma as a food processing aid has been demonstrated for a range of processes and products. The potential applications of plasma technology are extensive and include microbial decontamination, pest control, toxin elimination, food and package functionalisation and many others. However, studies reported to date have principally been at laboratory scale. This paper discusses the status and challenges of transferring the technology to the industry. The major challenges discussed for adoption of atmospheric plasma as a food processing tool by industry are (1) demonstration of product/process specific efficacies; (2) development of process compatible technology designs and scale‐up; (3) effective process control and validation; (4) regulatory approval; and (5) consumer acceptance.

Encapsulation of protease from Aspergillus oryzae and lipase from Thermomyces lanuginoseus using alginate and different copolymer types

Although the application of enzymes in food as a food processing aid and enzyme supplement is of interest and widely used, the enzymes can be easily deactivated or lose their activity due to many causes such as pH and moisture as well as through the introduction of incompatible ingredients during food processing and storage. These problems can be solved by the encapsulation technique, especially in a gel matrix. The influences were studied of the alginate concentration, types of copolymer and their concentrations on the bead size, encapsulation yield (EY), encapsulation efficiency (EE), leakage and the retention of enzyme activity during storage period of encapsulated protease from Aspergillus oryzae and lipase from Thermomyces lanuginosus beads. A solution of purified protease or lipase was encapsulated in calcium alginate-chitosan beads (CACB), calcium alginate-xanthan gum beads (CAXB) and calcium alginate-maltodextrin beads (CAMB) using the extrusion method. Increasing the alginate and copolymer concentrations in the solution increased the bead size, EY, EE and the retention of enzyme activity during the storage period and reduced leakage of both the encapsulated protease and lipase. In addition, different types of copolymer significantly (p ≤ 0.05) affected these properties of both encapsulated enzymes. Furthermore, protease encapsulated using 2.0% alginate and 0.2% chitosan provided the highest EY (81.7%) and EE (77.2%) with a bead size of 1.85 mm and 8.1% leakage. The retention of encapsulated protease activity and the shelf-life of encapsulated enzyme which was expressed as half-life, the time required for the enzyme activity to decrease by half (thalf life) were 75.8% and 27.2 wk, respectively after storage at 4 °C for 10 wk. For lipase, encapsulation using 2.0% alginate and 0.4% xanthan gum provided the highest EY (42.5%) and EE (43.9%) and the bead size and leakage were 1.81 mm and 6.2%, respectively. The retention of encapsulated lipase activity and the thalf life were 77.9% and 27.8 wk, respectively after storage at 4 °C for 10 wk. CACB was a suitable complex polymer for encapsulating protease while CAXB was suitable for lipase. EY and EE values of CACB-protease were higher than those of CAXB-lipase. Therefore, the encapsulation method, gelling conditions and interactions between carriers and lipase should be further studied.

REFOLDING PROTEIN, NIES39_A07830 FROM Arthrospira platensis AND ITS L-ASPARAGINASE ACTIVITY

Ponte Academic JournalDec 2016, Volume 72, Issue 12 REFOLDING PROTEIN, NIES39_A07830 FROM Arthrospira platensis AND ITS L-ASPARAGINASE ACTIVITYAuthor(s): Asep A. Prihanto ,Happy Nursyam, Center for Coastal and marine Studies, Institute of Community Service, Brawijaya UniversityJ. Ponte - Dec 2016 - Volume 72 - Issue 12 doi: 10.21506/j.ponte.2016.12.14 Abstract:L-Asparaginase (E.C. 3.5.1.1) is an amidohydrolase enzyme which catalyze L-asparagine to L-aspartate and generate ammonia. This enzyme has an important application on medicine and food processing aid. In this research, L-asparaginase from food grade microorganism, Arthrospira platensis was cloned and expressed in Escherichia coli system. The expression of cloned gene resulted in the inclusion body form. It was found that deduced protein was located and accumulated in pellet fraction, inclusion bodies. Hence, to achieve active form of the enzyme, it need to be correctly folded with steps as follow solubilization and refolding. Here, we report the recovering activity of the enzyme throughout our refolding process. Several denaturant agents were used to completely denature a protein from inclusion body. Urea, triton-X 100, and sarkosyl are able to denature the protein. The refolding process was conducted by dilution and dialysis methods. After experienced refolding process, L-asparaginase activity was detected. The highest activity was achieved from dialysis methods (64 U). We, therefore, reported the activity in the refolded enzyme even though the process needs to be optimized. Download full text:Check if you have access through your login credentials or your institution Username Password

Reduction of acrylamide level through blanching with treatment by an extremely thermostable L-asparaginase during French fries processing.

Bacterial L-asparaginase catalyzes the hydrolysis of L-asparagine to L-aspartic acid. It is normally used as an antineoplastic drug applied in lymphoblastic leukemia chemotherapy and as a food processing aid in baked or fried food industry to inhibit the formation of acrylamide. The present study demonstrates cloning, expression, and characterization of a thermostable L-asparaginase from Thermococcus zilligii AN1 TziAN1_1 and also evaluates the potential for enzymatic acrylamide mitigation in French fries using this enzyme. The recombinant L-asparaginase was purified to homogeneity by nickel-affinity chromatography. The purified enzyme displayed the maximum activity at pH 8.5 and 90 °C, and the optimum temperature was the highest ever reported. The K m, k cat, and k cat/K m values toward L-asparagine were measured to be 6.08 mM, 3267 s(-1), and 537.3 mM(-1) s(-1), respectively. The enzyme retained 70 % of its original activity after 2 h of incubation at 85 °C. When potato samples were treated with 10 U/mL of L-asparaginase at 80 °C for only 4 min, the acrylamide content in final French fries was reduced by 80.5 % compared with the untreated control. Results of this study revealed that the enzyme was highly active at elevated temperatures, reflecting the potential of the T. zilligii L-asparaginase in the food processing industry.

Statistical screening of process variables for the production of L-asparaginase from cornflour by Aspergillus terreus MTCC 1782 in submerged fermentation

L-asparaginase has been used as anti-tumor agent for the effective treatment of acute lymphoblastic leukemia and as food processing aid to reduce the formation of acrylamide during frying of starchy foods at high temperature. Objective of the present work was to study the effect of process variables such as cornflour (as natural substrate), urea (as supplementary nitrogen source), L-asparagine, glucose, di-potassium hydrogen phosphate, potassium chloride, inoculum size and pH on the production of extracellular L-asparaginase by Aspergillus terreus MTCC 1782 in shake culture fermentation. The effect and significance of these variables was studied using 2-level Plackett-Burman statistical design. The experimental L-asparaginase activity was subjected to statistical analysis using MINITAB 14 software. It was found that L-asparagine, cornflour and urea significantly influenced as most important factors on L-asparaginase production. Keywords: Extracellular L-asparaginase, acute lymphoblastic leukemia, food processing aid, PlackettBurman design, fermentation.

Inhibition spectrum studies of microthecin and other anhydrofructose derivatives using selected strains of Gram-positive and -negative bacteria, yeasts and moulds, and investigation of the cytotoxicity of microthecin to malignant blood cell lines

To prepare 1,5-anhydro-d-fructose (AF) derivatives, test their microbial inhibition spectrum, and to further examine the most effective AF derivative against Pseudomonas aeruginosa and malignant blood cell lines. Microthecin and nine other AF derivatives were synthesized from AF. The 10 compounds were tested in vitro against Gram-positive (GP) and Gram-negative (GN) bacteria, yeasts and moulds using a well diffusion method and in a Bioscreen growth analyser. Of the test compounds, microthecin exhibited the most significant antibacterial activity at 100-2000 ppm against both GP and GN bacteria, including Ps. aeruginosa. Further tests with three malignant blood cell lines (Mutu, Ramos, Raji) and one normal cell line indicated that microthecin was a cell toxin, with a cell mortality >85% at 50 ppm. The other nine AF derivatives demonstrated low or no antimicrobial activity. Microthecin was active 100-2000 ppm against GP and GN bacteria including Ps. aeruginosa, but was inactive against yeasts and moulds. Microthecin was also a cytotoxin to some mammalian cell lines. Microthecin might have potential for development as a novel drug against Ps. aeruginosa and to target cancer cells. It might also be developed as a food processing aid to control bacterial growth.

원양산 오징어(Illex argentinus) 내장으로부터 Endoprotease의 분획

To evaluate the effective use of endoprotease from squid viscera as a food processing aid, various methods of fractionating endoprotease from viscera of the Argentina shortfin squid (Illex argentinus) were evaluated. The endoprotease-positive fractions of each fractionation were fraction II (30-40%, w/w) with cold acetone, fraction IV (50-60% saturation) with ammonium sulfate, fraction UF with anion exchange chromatography, and fraction II (15-24 kDa) with gel filtration. The specific activities (approximately 25 U/mg) of the fractions using ammonium sulfate and gel filtration were higher than the others. Total azocaseinolytic activity and recovery of the positive fraction using gel filtration were 806.95U and 37.82%, respectively, and were the highest among the positive fractions. Based on the results, gel filtration was the most efficient method for fractionating endoprotease from the viscera of Illex argentinus.

Food Processing with Added Ascorbic Acid

The use of L-ascorbic acid in processing food was reviewed by Bauernfeind in 1953. By that time, several hundred papers had already been published on studies of various applications of this compound in food processing. L-Ascorbic acid, a 6-carbon compound and a water-soluble vitamin also known as vitamin C (for cevitamic acid), exists in both the reduced and the oxidized forms (dehydroascorbic acid) in nature. It is found in all living tissues. Citrus fruits, tomatoes, potatoes, and cabbage are the important natural dietary sources for man, but content varies depending on variety, environmental factors, and processing. L-Ascorbic acid (vitamin C) is added to processed fruit, vegetables, meat, fish, milk, fats, oils, flour, soft drinks, malt beverages, wine, confections, and synthetic foods. It may be added to enhance nutritional value, or to improve keeping qualities, color, stability, palatability, clarity, or baking quality. This chapter looks at ascorbic acid as an added nutrient. The use of L-ascorbic acid to inhibit or prevent undesirable oxidative changes in the processing of foodstuffs has been largely empirical. It discusses ascorbic acid as synergist in fat protection, preventive of fruit browning, preventive of vegetable discolorations, inhibitor of oxidative rancidity in fish, stabilizer of meat color, flour or bread improver, oxygen acceptor in beer processing, reducing agent in wine, oxidation inhibition in dairy products, and other miscellaneous uses. The use of ascorbic acid in a nutrient capacity or as a food processing aid is subject to government regulation in many countries. The status of ascorbic acid addition in each instance of desired use should be determined by consulting the pertinent regulation. A brief review of the regulatory requirements in some countries is given here. This chapter ends with the discussion of L-Ascorbic acid vs. erythorbic acid.