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Extraction of proteins from microalgae using integrated method of sugaring-out assisted liquid biphasic flotation (LBF) and ultrasound

Sankaran R, Manickam S, Yap YJ, Ling TC, Chang JS, Show PL

Ultrason Sonochem, 2018 Nov;48:231-239.
PMID: 30080546 DOI: 10.1016/j.ultsonch.2018.06.002

In this study, a simple sugaring-out supported by liquid biphasic flotation technique combined with ultrasonication was introduced for the extraction of proteins from microalgae. Sugaring-out as a phase separation method is novel and has been used in the extraction of metal ions, biomolecules and drugs. But, its functioning in protein separation from microalgae is still unknown. In this work, the feasibility of sugaring-out coupled with ultrasound for the extraction of protein was investigated. Primary studies were carried out to examine the effect of sonication on the microalgae cell as well as the separation efficiency of the integrated method. Effect of various operating parameters such as the concentration of microalgae biomass, the location of sonication probe, sonication time, ultrasonic pulse mode (includes varying ON and OFF duration of sonication), concentration of glucose, types of sugar, concentration of acetonitrile and the flow rate in the flotation system for achieving a higher separation efficiency and yield of protein were assessed. Besides, a large-scale study of the integration method was conducted to verify the consistency of the followed technique. A maximum efficiency (86.38%) and yield (93.33%) were attained at the following optimized conditions: 0.6% biomass concentration, 200 g/L of glucose concentration, 100% acetonitrile concentration with 5 min of 5 s ON/10 s OFF pulse mode and at a flow rate of 100 cc/min. The results obtained for large scale were 85.25% and 92.24% for efficiency and yield respectively. The proposed liquid biphasic flotation assisted with ultrasound for protein separation employing sugaring-out demonstrates a high production and separation efficiency and is a cost-effective solution. More importantly, this method provides the possibility of extending its application for the extraction of other important biomolecules.

Matched MeSH terms: Plant Proteins/isolation & purification*
Development and characteristics of polymer monoliths for advanced LC bioscreening applications: A review

Acquah C, Moy CKS, Danquah MK, Ongkudon CM

J Chromatogr B Analyt Technol Biomed Life Sci, 2016 Mar 15;1015-1016:121-134.
PMID: 26919447 DOI: 10.1016/j.jchromb.2016.02.016

Biomedical research advances over the past two decades in bioseparation science and engineering have led to the development of new adsorbent systems called monoliths, mostly as stationary supports for liquid chromatography (LC) applications. They are acknowledged to offer better mass transfer hydrodynamics than their particulate counterparts. Also, their architectural and morphological traits can be tailored in situ to meet the hydrodynamic size of molecules which include proteins, pDNA, cells and viral targets. This has enabled their development for a plethora of enhanced bioscreening applications including biosensing, biomolecular purification, concentration and separation, achieved through the introduction of specific functional moieties or ligands (such as triethylamine, N,N-dimethyl-N-dodecylamine, antibodies, enzymes and aptamers) into the molecular architecture of monoliths. Notwithstanding, the application of monoliths presents major material and bioprocess challenges. The relationship between in-process polymerisation characteristics and the physicochemical properties of monolith is critical to optimise chromatographic performance. There is also a need to develop theoretical models for non-invasive analyses and predictions. This review article therefore discusses in-process analytical conditions, functionalisation chemistries and ligands relevant to establish the characteristics of monoliths in order to facilitate a wide range of enhanced bioscreening applications. It gives emphasis to the development of functional polymethacrylate monoliths for microfluidic and preparative scale bio-applications.

Matched MeSH terms: Proteins/isolation & purification
Novel lipase purification methods - a review of the latest developments

Tan CH, Show PL, Ooi CW, Ng EP, Lan JC, Ling TC

Biotechnol J, 2015 Jan;10(1):31-44.
PMID: 25273633 DOI: 10.1002/biot.201400301

Microbial lipases are popular biocatalysts due to their ability to catalyse diverse reactions such as hydrolysis, esterification, and acidolysis. Lipases function efficiently on various substrates in aqueous and non-aqueous media. Lipases are chemo-, regio-, and enantio-specific, and are useful in various industries, including those manufacturing food, detergents, and pharmaceuticals. A large number of lipases from fungal and bacterial sources have been isolated and purified to homogeneity. This success is attributed to the development of both conventional and novel purification techniques. This review highlights the use of these techniques in lipase purification, including conventional techniques such as: (i) ammonium sulphate fractionation; (ii) ion-exchange; (iii) gel filtration and affinity chromatography; as well as novel techniques such as (iv) reverse micellar system; (v) membrane processes; (vi) immunopurification; (vi) aqueous two-phase system; and (vii) aqueous two-phase floatation. A summary of the purification schemes for various bacterial and fungal lipases are also provided.

Matched MeSH terms: Bacterial Proteins/isolation & purification; Fungal Proteins/isolation & purification
Direct recovery of recombinant nucleocapsid protein of Nipah virus from unclarified Escherichia coli homogenate using hydrophobic interaction expanded bed adsorption chromatography

Chong FC, Tan WS, Biak DR, Ling TC, Tey BT

J Chromatogr A, 2010 Feb 19;1217(8):1293-7.
PMID: 20044094 DOI: 10.1016/j.chroma.2009.12.039

A direct recovery of recombinant nucleocapsid protein of Nipah virus (NCp-NiV) from crude Escherichia coli (E. coli) homogenate was developed successfully using a hydrophobic interaction expanded bed adsorption chromatography (HI-EBAC). The nucleic acids co-released with the recombinant protein have increased the viscosity of the E. coli homogenate, thus affected the axial mixing in the EBAC column. Hence, DNase was added to reduce the viscosity of feedstock prior to its loading into the EBAC column packed with the hydrophobic interaction chromatography (HIC) adsorbent. The addition of glycerol to the washing buffer has reduced the volume of washing buffer applied, and thus reduced the loss of the NCp-NiV during the washing stage. The influences of flow velocity, degree of bed expansion and viscosity of mobile phase on the adsorption efficiency of HI-EBAC were studied. The dynamic binding capacity at 10% breakthrough of 3.2mg/g adsorbent was achieved at a linear flow velocity of 178 cm/h, bed expansion of two and feedstock viscosity of 3.4 mPas. The adsorbed NCp-NiV was eluted with the buffer containing a step gradient of salt concentration. The purification of hydrophobic NCp-NiV using the HI-EBAC column has recovered 80% of NCp-NiV from unclarified E. coli homogenate with a purification factor of 12.5.

Matched MeSH terms: Recombinant Proteins/isolation & purification*; Nucleocapsid Proteins/isolation & purification*
Direct recovery of enhanced green fluorescent protein from unclarified Escherichia coli homogenate using ion exchange chromatography in stirred fluidized bed

Song CP, Ooi CW, Tey BT, Lu CX, Liu BL, Chang YK

Int J Biol Macromol, 2020 Dec 01;164:4455-4465.
PMID: 32937154 DOI: 10.1016/j.ijbiomac.2020.09.051

A stirred fluidized bed (SFB) ion exchange chromatography was successfully applied in the direct recovery of recombinant enhanced green fluorescent protein (EGFP) from the unclarified Escherichia coli homogenate. Optimal conditions for both adsorption and elution processes were determined from the packed-bed adsorption systems conducted at a small scale using the clarified cell homogenate. The maximal adsorption capacity and dissociation constant for EGFP-adsorbent complex were found to be 6.3 mg/mL and 1.3 × 10-3 mg/mL, respectively. In an optimal elution of EGFP with 0.2 M of NaCl solution (pH 9) and at 200 cm/h, the recovery percent of the EGFP was approximately 93%. The performances of SFB chromatography for direct recovery of EGFP was also evaluated under different loading volumes (50-200 mL) of crude cell homogenate. The single-step purification of EGFP by SFB recorded in a high yield (95-98%) and a satisfactory purification factor (~3 folds) of EGFP from the cell homogenate at 200 rpm of rotating speed.

Matched MeSH terms: Recombinant Proteins/isolation & purification*; Green Fluorescent Proteins/isolation & purification*
Fulltext Single-step purification of the recombinant green fluorescent protein from intact Escherichia coli cells using preparative PAGE

Chew FN, Tan WS, Ling TC, Tey BT

Electrophoresis, 2009 Sep;30(17):3017-3023.
PMID: 19685471 DOI: 10.1002/elps.200900246

Mechanical and non-mechanical breakages of bacterial cells are usually the preliminary steps in intracellular protein purification. In this study, the recombinant green fluorescent protein (GFP) was purified from intact Escherichia coli cells using preparative PAGE. In this purification process, cells disruption step is not needed. The cellular content of E. coli was drifted out electrically from cells and the negatively charged GFP was further electroeluted from polyacrylamide gel column. SEM investigation of the electrophoresed cells revealed substantial structural damage at the cellular level. This integrated purification technique has successfully recovered the intracellular GFP with a yield of 82% and purity of 95%.

Matched MeSH terms: Recombinant Proteins/isolation & purification*; Green Fluorescent Proteins/isolation & purification*
Fulltext Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein from Spiroplasma melliferum KC3

Boyko K, Gorbacheva M, Rakitina T, Korzhenevskiy D, Vanyushkina A, Kamashev D, et al.

Acta Crystallogr F Struct Biol Commun, 2015 Jan 01;71(Pt 1):24-7.
PMID: 25615963 DOI: 10.1107/S2053230X14025333

HU proteins belong to the nucleoid-associated proteins (NAPs) that are involved in vital processes such as DNA compaction and reparation, gene transcription etc. No data are available on the structures of HU proteins from mycoplasmas. To this end, the HU protein from the parasitic mycoplasma Spiroplasma melliferum KC3 was cloned, overexpressed in Escherichia coli and purified to homogeneity. Prismatic crystals of the protein were obtained by the vapour-diffusion technique at 4°C. The crystals diffracted to 1.36 Å resolution (the best resolution ever obtained for a HU protein). The diffraction data were indexed in space group C2 and the structure of the protein was solved by the molecular-replacement method with one monomer per asymmetric unit.

Matched MeSH terms: Bacterial Proteins/isolation & purification; DNA-Binding Proteins/isolation & purification
Purification of recombinant nucleocapsid protein of Newcastle disease virus from unclarified feedstock using expanded bed adsorption chromatography

Tan YP, Ling TC, Tan WS, Yusoff K, Tey BT

Protein Expr Purif, 2006 Mar;46(1):114-21.
PMID: 16139513

In the present work, a single-step purification of recombinant nucleocapsid protein (NP) of the Newcastle disease virus (NDV) directly from unclarified feedstock using an expanded bed adsorption chromatography (EBAC) was developed. Streamline 25 column (ID = 25 mm) was used as a contactor and Streamline chelating adsorbent immobilized with Ni2+ ion was used as affinity adsorbent. The dynamic binding capacity of Ni2+ -loaded Streamline chelating adsorbent for the NP protein in unclarified feedstock was found to be 2.94 mg ml(-1) adsorbent at a superficial velocity of 200 cm h(-1). The direct purification of NP protein from unclarified feedstock using expanded bed adsorption has resulted in a 31% adsorption and 9.6% recovery of NP protein. The purity of the NP protein recovered was about 70% and the volume of processing fluid was reduced by a factor of 10. The results of the present study show that the IMA-EBAC developed could be used to combine the clarification, concentration and initial purification steps into a single-step operation.

Matched MeSH terms: Recombinant Proteins/isolation & purification; Nucleocapsid Proteins/isolation & purification*
Effect of deprotenizing agent and quantification of donepezil hydrochloride in human plasma

Liew KB, Peh KK, Fung Tan YT

Pak J Pharm Sci, 2014 Sep;27(5):1303-7.
PMID: 25176366

The effect of deprotenizing agents on recovery of donepezil hydrochloride in the development of a simple, rapid, selective and sensitive high performance liquid chromatography method for quantification of donepezil hydrochloride in human plasma was described. The deprotenizing agents were comprised of, perchloric acid, methanol, acetonitrile, chloroform and their mixtures. The chromatographic separation was carried out using reversed phase C18 column (Agilent Eclipse Plus C18) with UV detection at 268 nm. The mobile phase was comprised of 0.01 M potassium dihydrogen phosphate buffer, methanol and acetronitrile (50:30:20, v/v) adjusted to pH 2.7 with phosphoric acid (80%). A combination of perchloric acid and methanol gave a cleaner sample with a good recovery of donepezil hydrochloride of above 96%. The method showed intraday precision and accuracy in the range of 6.82% to 1.5% and 3.13% to 1.12% respectively, while interday precision and accuracy ranged between 1.06% to 4.71% and 13.01% to 6.43% respectively. The standard calibration curve was linear from 30ng/mL to 4000ng/mL, with a correlation coefficient of 0.9965±0.0034. The retention time of donepezil was 5.9 min with a run time of 7.0 min. The method can be applied to analyze large batch plasma samples in pharmacokinetic studies.

Matched MeSH terms: Blood Proteins/isolation & purification
A comparative study of physicochemical characteristics and functionalities of pinto bean protein isolate (PBPI) against the soybean protein isolate (SPI) after the extraction optimisation

Tan ES, Ying-Yuan N, Gan CY

Food Chem, 2014;152:447-55.
PMID: 24444960 DOI: 10.1016/j.foodchem.2013.12.008

Optimisation of protein extraction yield from pinto bean was investigated using response surface methodology. The maximum protein yield of 54.8 mg/g was obtained with the optimal conditions of: temperature=25 °C, time=1 h and buffer-to-sample ratio=20 ml/g. PBPI was found to obtain high amount of essential amino acids such as leucine, lysine, and phenylalanine compared to SPI. The predominant proteins of PBPI were vicilin and phytohemagglutinins whereas the predominant proteins of SPI were glycinin and conglycinins. Significantly higher emulsifying capacity was found in PBPI (84.8%) compared to SPI (61.9%). Different isoelectric points were found in both PBPI (4.0-5.5) and SPI (4.0-5.0). Also, it was found that PBPI obtained a much higher denaturation temperature of 110.2 °C compared to SPI (92.5 °C). Other properties such as structural information, gelling capacity, water- and oil-holding capacities, emulsion stability as well as digestibility were also reported.

Matched MeSH terms: Plant Proteins/isolation & purification
Mimotopes of heat shock proteins of Salmonella enterica serovar Typhi identified from phage-displayed peptide library

Yuen HL, Shamala D, Thong KL

J Infect Dev Ctries, 2008 Aug 30;2(4):313-23.
PMID: 19741295

BACKGROUND: Heat shock proteins (HSPs) are known to be involved in the pathogenesis of Salmonella enterica serovar Typhi (S. Typhi), the causative agent of typhoid fever. The objective of this study was to apply a phage display library to identify mimotopes of two HSPs, HSP90 and DnaK in S. Typhi.
METHODOLOGY: A 12-mer random peptide library expressed on the surface of the filamentous phage, M13, was used to select the mimotopes of two S. Typhi heat shock proteins by biopanning with monoclonal antibodies (mAbs), DnaK and HSP90. The immunogenicity of the selected peptides was determined through binding affinity with polyclonal antibodies from pooled typhoid-confirmed patients' sera and purified HSPs mAb using Western blotting and ELISA.
RESULTS: Five rounds of biopanning resulted in enrichment of phage clones expressing the binding motifs TDxSTRP and FPSHYWLYPPPT, respectively. The selected peptides showed strong immunoreactivity with patients' sera. Thus, monoclonal antibodies against HSP and patient sera can select common mimotopes from the random peptide library.
CONCLUSION: These findings may provide fundamental information for further studies on diagnostic application or vaccine design against this aetiologic agent of typhoid fever.

Matched MeSH terms: HSP90 Heat-Shock Proteins/isolation & purification*
New mechanical disruption method for extraction of whole cell protein from Candida albicans

Wong SF, Mak JW, Pook PC

Southeast Asian J. Trop. Med. Public Health, 2007 May;38(3):512-8.
PMID: 17877228

Cell disruption or lysis is a crucial step to obtain cellular components for various biological studies. We subjected different concentrations of Candida albicans to 5, 10, 15 and 20 cycles of disruption. The degree of cell lysis was observed using light microscopy and the yields obtained were measured and analysed. The optimum extraction with 1 x 10(10) yeast cells/ml was achieved after 5 cycles of disruption with 1.0 mm diameter glass beads at 5,000 rpm. Approximately 80% of the cells were lysed and the protein yield was 6,000 microg/ml. SDS-PAGE analysis revealed approximately 25 distinct protein bands with molecular weights ranging from 8 kDa to 220 kDa. We conclude that this mechanical disruption of fungal cells is a rapid, efficient and inexpensive technique for extracting whole cell proteins from yeast cells.

Matched MeSH terms: Fungal Proteins/isolation & purification*
Honey protein extraction and determination by mass spectrometry

Chua LS, Lee JY, Chan GF

Anal Bioanal Chem, 2013 Apr;405(10):3063-74.
PMID: 23292042 DOI: 10.1007/s00216-012-6630-2

There are relatively limited studies on the protein of honey samples mainly because of the low amount of protein in honey (0.1-0.5 %), the difficulty in extracting honey protein from the sugar-rich environment, and the hindrance of protein characterization by conventional approaches. Several protein extraction methods such as mechanical (ultrafiltration and ultracentrifugation) and chemical (precipitation) techniques have been applied to different types of honey samples. Most of these studies reported the quantity and molecular size of honey protein from gel electrophoresis, but were unable to identify and characterize the protein. This limitation might be due to the low capacity of analytical equipment in those days. Although different precipitants have also been used, not all them are compatible with mass spectrometric methods during downstream analysis. As a result, the sample preparation step is essential in order to confidently characterize the low and varied amount of honey protein. Nowadays, honey protein is getting attention from researchers because of its potential activity in pharmacological applications. Therefore, honey protein extraction and determination by mass spectrometry are critically reviewed in order to stimulate further honey protein research.

Matched MeSH terms: Proteins/isolation & purification*
The manufacture of gloves from natural rubber latex

Yip E, Cacioli P

J Allergy Clin Immunol, 2002 Aug;110(2 Suppl):S3-14.
PMID: 12170237 DOI: 10.1067/mai.2002.124499

Gloves that will provide a barrier of protection from infectious organisms are an essential feature of medical practice for the protection of both patients and medical personnel. Natural rubber latex has consistently been the most satisfactory raw material for the manufacture of gloves. Certain latex proteins, carried over into the finished product by inadequate manufacturing processes, may pose a risk of provoking allergic reactions in some patients and medical workers. As with any allergy, the risk depends on the route of exposure and dose. Hence, the method of manufacture, including the means used to coat gloves to make donning easy, can influence the eventual exposure of sensitive people to latex allergens. In this article, we describe the several processes in use and their effects on latex protein content.

Matched MeSH terms: Plant Proteins/isolation & purification
Protein purification for the Lowry assay: acid precipitation of proteins in the presence of sodium dodecyl sulfate and other biological detergents

Yeang HY, Yusof F, Abdullah L

Anal Biochem, 1998 Dec 15;265(2):381-4.
PMID: 9882418
Matched MeSH terms: Proteins/isolation & purification*
Protein variation and systematics in Malayan rats of the subgenus Lenothrix (Rodentia: Muridae, genus Rattus Fischer)

Chan KL, Dhaliwal SS, Yong HS

Comp. Biochem. Physiol., B, 1978;59(4):345-51.
PMID: 318285

1. Electrophoretic variations of 9 erythrocyte proteins, coded by a separate gene locus each, were analysed in and among the 5 Malayan species of Rattus belonging to the subgenus Lenothrix. 2. The average proportion of loci heterozygous per individual for the taxa analysed is 0.037. 3. The results obtained confirm the specific status of the 5 taxa studied. With respect to the relative affinities among the species studied, the present results could resolve the discrepancies between conclusions based on morphological evidence and those based on cytological evidence. 4. The 5 species of Rattus studied may be assigned to 4 groups and comparative data suggest that these groups are relatively distantly related to one another.

Matched MeSH terms: Blood Proteins/isolation & purification*
Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion

Hossain Brishti F, Chay SY, Muhammad K, Rashedi Ismail-Fitry M, Zarei M, Karthikeyan S, et al.

Food Chem, 2021 May 15;344:128643.
PMID: 33246681 DOI: 10.1016/j.foodchem.2020.128643

Mung bean protein isolate was texturized at different feed moisture contents (30.0, 49.3, and 60.0%) at a constant temperature (144.57 °C) to evaluate the changes in protein profile, solubility, thermal, structural (at secondary and tertiary levels) and rheological properties. SDS-PAGE, surface hydrophobicity, circular dichroism, FTIR spectroscopy, and fluorescence analyses revealed protein unfolding, aggregation, and structural rearrangement as a function of feed moisture content. Extrusion at 49.3% feed moisture produced texturized mung bean protein (TMBP) with favourable partial denaturation, the formation of small aggregates, improved solubility, and digestibility with strong gel forming behaviour, whereas 30.0 and 60.0% moisture content resulted in complete protein denaturation, the undesirable formation of large aggregates and weak gels. In conclusion, protein denaturation and formation of aggregates can be controlled by manipulating feed moisture content during extrusion, with 49.3% feed moisture prompting favourable partial denaturation to produce TMBP with desirable qualities for use as a vegetarian-based meat extender.

Matched MeSH terms: Plant Proteins/isolation & purification*
Fulltext Optimal protein extraction methods from diverse sample types for protein profiling by using Two-Dimensional Electrophoresis (2DE)

Tan AA, Azman SN, Abdul Rani NR, Kua BC, Sasidharan S, Kiew LV, et al.

Trop Biomed, 2011 Dec;28(3):620-9.
PMID: 22433892 MyJurnal

There is a great diversity of protein samples types and origins, therefore the optimal procedure for each sample type must be determined empirically. In order to obtain a reproducible and complete sample presentation which view as many proteins as possible on the desired 2DE gel, it is critical to perform additional sample preparation steps to improve the quality of the final results, yet without selectively losing the proteins. To address this, we developed a general method that is suitable for diverse sample types based on phenolchloroform extraction method (represented by TRI reagent). This method was found to yield good results when used to analyze human breast cancer cell line (MCF-7), Vibrio cholerae, Cryptocaryon irritans cyst and liver abscess fat tissue. These types represent cell line, bacteria, parasite cyst and pus respectively. For each type of samples, several attempts were made to methodically compare protein isolation methods using TRI-reagent Kit, EasyBlue Kit, PRO-PREP™ Protein Extraction Solution and lysis buffer. The most useful protocol allows the extraction and separation of a wide diversity of protein samples that is reproducible among repeated experiments. Our results demonstrated that the modified TRI-reagent Kit had the highest protein yield as well as the greatest number of total proteins spots count for all type of samples. Distinctive differences in spot patterns were also observed in the 2DE gel of different extraction methods used for each type of sample.

Matched MeSH terms: Proteins/isolation & purification*
Fulltext Subcritical Water Technology for Enhanced Extraction of Biochemical Compounds from Chlorella vulgaris

Awaluddin SA, Thiruvenkadam S, Izhar S, Hiroyuki Y, Danquah MK, Harun R

Biomed Res Int, 2016;2016:5816974.
PMID: 27366748 DOI: 10.1155/2016/5816974

Subcritical water extraction (SWE) technology has been used for the extraction of active compounds from different biomass materials with low process cost, mild operating conditions, short process times, and environmental sustainability. With the limited application of the technology to microalgal biomass, this work investigates parametrically the potential of subcritical water for high-yield extraction of biochemicals such as carbohydrates and proteins from microalgal biomass. The SWE process was optimized using central composite design (CCD) under varying process conditions of temperature (180-374°C), extraction time (1-20 min), biomass particulate size (38-250 μm), and microalgal biomass loading (5-40 wt.%). Chlorella vulgaris used in this study shows high volatile matter (83.5 wt.%) and carbon content (47.11 wt.%), giving advantage as a feedstock for biofuel production. The results showed maximum total carbohydrate content and protein yields of 14.2 g/100 g and 31.2 g/100 g, respectively, achieved under the process conditions of 277°C, 5% of microalgal biomass loading, and 5 min extraction time. Statistical analysis revealed that, of all the parameters investigated, temperature is the most critical during SWE of microalgal biomass for protein and carbohydrate production.

Matched MeSH terms: Proteins/isolation & purification*
Fulltext Ultrasound in the deproteinization process for chitin and chitosan production

Vallejo-Domínguez D, Rubio-Rosas E, Aguila-Almanza E, Hernández-Cocoletzi H, Ramos-Cassellis ME, Luna-Guevara ML, et al.

Ultrason Sonochem, 2021 Apr;72:105417.
PMID: 33352467 DOI: 10.1016/j.ultsonch.2020.105417

Recently, chitin and chitosan are widely investigated for food preservation and active packaging applications. Chemical, as well as biological methods, are usually adopted for the production of these biopolymers. In this study, modification to a chemical method of chitin synthesis from shrimp shells has been proposed through the application of high-frequency ultrasound. The impact of sonication time on the deproteinization step of chitin and chitosan preparation was examined. The chemical identities of chitin and chitosan were verified using infrared spectroscopy. The influence of ultrasound on the deacetylation degree, molecular weight and particle size of the biopolymer products was analysed. The microscopic characteristics, crystallinity and the colour characteristics of the as-obtained biopolymers were investigated. Application of ultrasound for the production of biopolymers reduced the protein content as well as the particle size of chitin. Chitosan of high deacetylation degree and medium molecular weight was produced through ultrasound assistance. Finally, the as-derived chitosan was applied for beef preservation. High values of luminosity, chromatid and chrome were noted for the beef samples preserved using chitosan films, which were obtained by employing biopolymer subjected to sonication for 15, 25 and 40 min. Notably; these characteristics were maintained even after ten days of packaging. The molecular weight of these samples are 73.61 KDa, 86.82 KDa and 55.66 KDa, while the deacetylation degree are 80.60%, 92.86% and 94.03%, respectively; in the same order, the particle size of chitosan are 35.70 μm, 25.51 μm and 20.10 μm.

Matched MeSH terms: Proteins/isolation & purification*

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