Displaying publications 1 - 20 of 38 in total

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  1. Fulltext Easy lens cleaning solution for laboratory microscopes
    Pramanik T, Ghosh A, Roychowdhury P
    Med J Malaysia, 2005 Mar;60(1):116.
    PMID: 16250297
    Matched MeSH terms: Detergents*
  2. Complete genome sequence of Bacillus Licheniformis NWMCC0046, a candidate for the laundry industry
    Zhou W, Zeng S, Yu J, Xiang J, Zhang F, Takriff MS, et al.
    J Basic Microbiol, 2023 Feb;63(2):223-234.
    PMID: 36538731 DOI: 10.1002/jobm.202200528
    In this study, selected properties of protease and the complete genome sequence of Bacillus licheniformis NWMCC0046 were investigated, to discover laundry applications and other potential probiotic properties of this strain. Partial characterization of B. licheniformis NWMCC0046 showed that its protease has good activity both in alkaline environments and at low temperatures. Also, the protease is compatible with commercial detergents and can be used as a detergent additive for effective stain removal at low temperatures. The complete genome sequence of B. licheniformis NWMCC0046 is comprised of a 4,321,565 bp linear chromosome with a G + C content of 46.78% and no plasmids. It had 4504 protein-encoding genes, 81 transfer RNA (tRNA) genes, and 24 ribosomal RNA (rRNA) genes. Genomic analysis revealed genes involved in exocellular enzyme production and probiotic properties. In addition, genomic sequence analysis revealed specific genes encoding carbohydrate metabolism pathways, resistance, and cold adaptation capacity. Overall, protease properties show its potential as a detergent additive enzyme. The complete genome sequence information of B. licheniformis NWMCC0046 was obtained, and functional prediction revealed its numerous probiotic properties.
    Matched MeSH terms: Detergents*
  3. Fulltext Characterization of Sphingobacterium sp. Ab3 Lipase and Its Coexpression with LEA Peptides
    Ng YK, Ikeno S, Kadhim Almansoori AK, Muhammad I, Abdul Rahim R
    Microbiol Spectr, 2022 Dec 21;10(6):e0142221.
    PMID: 36314920 DOI: 10.1128/spectrum.01422-21
    Sphingobacterium sp. is a yellowish Gram-negative bacterium that is usually characterized by high concentrations of sphingophospholipids as lipid components. As microbial enzymes have been in high demand in industrial fields in the past few decades, this study hopes to provide significant information on lipase activities of Sphingobacterium sp., since limited studies have been conducted on the Sphingobacterium sp. lipase. A microbe from one collected Artic soil sample, ARC4, was identified as psychrotolerant Sphingobacterium sp., and it could grow in temperatures ranging from 0°C to 24°C. The expression of Sphingobacterium sp. lipase was successfully performed through an efficient approach of utilizing mutated group 3 late embryogenesis abundant (G3LEA) proteins developed from Polypedilum vanderplanki. Purified enzyme was characterized using a few parameters, such as temperature, pH, metal ion cofactors, organic solvents, and detergents. The expressed enzyme is reported to be cold adapted and has the capability to work efficiently under neutral pH (pH 5.0 to 7.0), cofactors like Na+ ion, and the water-like solvent methanol. Addition of nonionic detergents greatly enhanced the activity of purified enzyme. IMPORTANCE The mechanism of action of LEA proteins has remained unknown to many; in this study we reveal their presence and improved protein expression due to the molecular shielding effect reported by others. This paper should be regarded as a useful example of using such proteins to influence an existing expression system to produce difficult-to-express proteins.
    Matched MeSH terms: Detergents/metabolism
  4. 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: Detergents/chemistry*
  5. Fulltext Evaluation of sodium deoxycholate as solubilization buffer for oil palm proteomics analysis
    Lau BYC, Othman A
    PLoS One, 2019;14(8):e0221052.
    PMID: 31415606 DOI: 10.1371/journal.pone.0221052
    Protein solubility is a critical prerequisite to any proteomics analysis. Combination of urea/thiourea and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) have been routinely used to enhance protein solubilization for oil palm proteomics studies in recent years. The goals of these proteomics analysis are essentially to complement the knowledge regarding the regulation networks and mechanisms of the oil palm fatty acid biosynthesis. Through omics integration, the information is able to build a regulatory model to support efforts in improving the economic value and sustainability of palm oil in the global oil and vegetable market. Our study evaluated the utilization of sodium deoxycholate as an alternative solubilization buffer/additive to urea/thiourea and CHAPS. Efficiency of urea/thiourea/CHAPS, urea/CHAPS, urea/sodium deoxycholate and sodium deoxycholate buffers in solubilizing the oil palm (Elaeis guineensis var. Tenera) mesocarp proteins were compared. Based on the protein yields and electrophoretic profile, combination of urea/thiourea/CHAPS were shown to remain a better solubilization buffer and additive, but the differences with sodium deoxycholate buffer was insignificant. A deeper mass spectrometric and statistical analyses on the identified proteins and peptides from all the evaluated solubilization buffers revealed that sodium deoxycholate had increased the number of identified proteins from oil palm mesocarps, enriched their gene ontologies and reduced the number of carbamylated lysine residues by more than 67.0%, compared to urea/thiourea/CHAPS buffer. Although only 62.0% of the total identified proteins were shared between the urea/thiourea/CHAPS and sodium deoxycholate buffers, the importance of the remaining 38.0% proteins depends on the applications. The only observed limitations to the application of sodium deoxycholate in protein solubilization were the interference with protein quantitation and but it could be easily rectified through a 4-fold dilution. All the proteomics data are available via ProteomeXchange with identifier PXD013255. In conclusion, sodium deoxycholate is applicable in the solubilization of proteins extracted from oil palm mesocarps with higher efficiency compared to urea/thiourea/CHAPS buffer. The sodium deoxycholate buffer is more favorable for proteomics analysis due to its proven advantages over urea/thiourea/CHAPS buffer.
    Matched MeSH terms: Detergents/chemistry*
  6. Fulltext Molecular Cloning, Characterization, and Application of Organic Solvent-Stable and Detergent-Compatible Thermostable Alkaline Protease from Geobacillus thermoglucosidasius SKF4
    Allison SD, AdeelaYasid N, Shariff FM, Abdul Rahman N
    J Microbiol Biotechnol, 2024 Feb 28;34(2):436-456.
    PMID: 38044750 DOI: 10.4014/jmb.2306.06050
    Several thermostable proteases have been identified, yet only a handful have undergone the processes of cloning, comprehensive characterization, and full exploitation in various industrial applications. Our primary aim in this study was to clone a thermostable alkaline protease from a thermophilic bacterium and assess its potential for use in various industries. The research involved the amplification of the SpSKF4 protease gene, a thermostable alkaline serine protease obtained from the Geobacillus thermoglucosidasius SKF4 bacterium through polymerase chain reaction (PCR). The purified recombinant SpSKF4 protease was characterized, followed by evaluation of its possible industrial applications. The analysis of the gene sequence revealed an open reading frame (ORF) consisting of 1,206 bp, coding for a protein containing 401 amino acids. The cloned gene was expressed in Escherichia coli. The molecular weight of the enzyme was measured at 28 kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The partially purified enzyme has its highest activity at a pH of 10 and a temperature of 80°C. In addition, the enzyme showed a half-life of 15 h at 80°C, and there was a 60% increase in its activity at 10 mM Ca2+ concentration. The activity of the protease was completely inhibited (100%) by phenylmethylsulfonyl fluoride (PMSF); however, the addition of sodium dodecyl sulfate (SDS) resulted in a 20% increase in activity. The enzyme was also stable in various organic solvents and in certain commercial detergents. Furthermore, the enzyme exhibited strong potential for industrial use, particularly as a detergent additive and for facilitating the recovery of silver from X-ray film.
    Matched MeSH terms: Detergents*
  7. Fulltext Kinetic performance of Cross-Linked Enzyme Aggregates (CLEA)-Amylase from Zophobas Morio
    Easa M.N., Yusof, F., Abd. Halim, A.
    International Food Research Journal, 2017;24(101):0-0.
    MyJurnal
    Many studies have been done on various species of insects to investigate their potential use in industries. This is because insects have high protein content which could be further manipulated. Due to its eating habit, Zophobas morio larvae, also known as super mealworm has been shown to have high amylase activity. In this study, amylase from super mealworm has been immobilized via Cross-Linked Enzyme Aggregates (CLEA) technique and its kinetic performance, evaluated. CLEA is one of the best immobilization method with respect to enzyme stability and reusability. Kinetic performance of both free and CLEA-amylase were evaluated based on the Michaelis-Menten model. Results obtained based on Hanes-Woolf, LineweaverBurk, Eadie-Hofstee and Hyperbolic Regression plots showed that the kinetic parameters, Vmax and KM, changed upon immobilization. For CLEA-amylase, Hanes-Woolf plot showed the bestfitted model based on R2 with Vmax= 1.068 mM/min and KM= 0.182 mM, however, LineweaverBurk plot was used to obtain the kinetic parameters for free amylase, with Vmax and KM of 17.230 mM/min and 2.470 mM, respectively. Thus it is observed that upon immobilization, Vmax for amylase dropped appreciably, however, much lower substrate concentration is needed to saturate the enzymatic sites to reach its maximum catalytic efficiency. The result from this study might open the new path in discovering the potential use of insects in industrial applications, for example, making use of the recovered enzymes in the detergent industry.
    Matched MeSH terms: Detergents
  8. Fulltext Genome sequence data of Mangrovimonas sp. strain CR14 isolated from mangrove forest at Tanjung Piai National Park, Malaysia
    Zakaria MR, Lam MQ, Chen SJ, Abdul Karim MH, Tokiman L, Yahya A, et al.
    Data Brief, 2020 Jun;30:105658.
    PMID: 32426431 DOI: 10.1016/j.dib.2020.105658
    Mangrovimonas sp. strain CR14 is a halophilic bacterium affiliated with family Flavobacteriaceae which was successfully isolated from mangrove soil samples obtained from Tanjung Piai National Park, Johor. The whole genome of strain CR14 was sequenced on an Illumina HiSeq 2500 platform (2 × 150 bp paired end). Herein, we report the genome sequence of Mangrovimonas sp. strain CR14 in which its assembled genome consisted 20 contigs with a total size of 3,590,195 bp, 3209 coding sequences, and an average 36.08% G + C content. Genome annotation and gene mining revealed that this bacterium demonstrated proteolytic activity which could be potentially applied in detergent industry. This whole-genome shotgun data of Mangrovimonas sp. strain CR14 has been deposited at DDBJ/ENA/GenBank under the accession JAAFZY000000000. The version described in this paper is version JAAFZY010000000.
    Matched MeSH terms: Detergents
  9. Pulmonary oedema due to inhalation of detergent aerosol
    Rao J, Das PK
    Malays J Pathol, 1994 Dec;16(2):165-6.
    PMID: 9053567
    Healthy adult male albino rats were subjected to inhalation of increasing doses of detergent (dioctyl sodium sulfo-succinate) aerosol ranging from 100 mg to 500 mg. Administration of 500 mg of detergent aerosol resulted in peribronchial and focal alveolar oedema in 3 out of 5 animals. The lungs of control animals which were subjected to inhalation of vehicle aerosol (ethanol and saline) did not show any abnormality. It is possible that pulmonary oedema observed in detergent aerosol inhalation may be due to the action of detergents on the surfactant system of the lung.
    Matched MeSH terms: Detergents/administration & dosage; Detergents/toxicity*
  10. Fulltext Performance of Green Surfactants in the Formulation of Heavy-Duty Laundry Liquid Detergents (HDLD) with Special Emphasis on Palm Based Alpha Methyl Ester Sulfonates (α-MES)
    Low SY, Tan JY, Ban ZH, Siwayanan P
    J Oleo Sci, 2021 Aug 05;70(8):1027-1037.
    PMID: 34248098 DOI: 10.5650/jos.ess21078
    Liquid detergent has an increasing demand in North America, Western Europe, and Southeast Asia countries owing to its convenience to use and efficiency to clean. Alpha methyl ester sulfonates (α-MES), an anionic surfactant derived from palm oil based methyl ester, was reported to have lower manufacturing cost, good detergency with less dosage, excellent biodegradability, higher tolerance to hard water, and lower eco-toxicity as compared to linear alkylbenzene sulfonates (LABS). LABS was known as the workhorse of the detergent industry in the 20th century. Although palm-based α-MES was successfully used as the sole surfactant in powder detergent, there are still some unsettled technical issues related to phase stability and viscosity when using this anionic surfactant in heavy-duty laundry liquid detergent formulations. This paper will review not only the market overview of detergents, the application and performance of green surfactants in laundry detergents but also will highlight the technical issues related to the application of palm-based α-MES in laundry liquid detergent and some of the possible methods to overcome the formulation adversities.
    Matched MeSH terms: Detergents/toxicity; Detergents/chemistry*
  11. Effect of feeding Pleurotus pulmonarius-treated empty fruit bunch on nutrient digestibility and milk fatty acid profiles in goats
    Zailan MZ, Salleh SM, Abdullah S, Yaakub H
    Trop Anim Health Prod, 2023 Nov 10;55(6):402.
    PMID: 37950132 DOI: 10.1007/s11250-023-03817-8
    This study aimed to evaluate the effect of feeding P. pulmonarius-treated empty fruit bunch (FTEFB) on the nutrient intakes, digestibility, milk yield and milk profiles of lactating Saanen goats. A total of nine lactating Saanen goats were used in an incomplete cross-over experimental design. The balanced dietary treatments contain different replacement levels of Napier grass with FTEFB at 0% (0-FT), 25% (25-FT) and 50% (50-FT). The FTEFB contained crude protein (CP), neutral detergent fibre (NDF), acid detergent fibre (ADF) and acid detergent lignin (ADL) at 4.10, 94.6, 70.8 and 19.4% DM, respectively. The replacement of FTEFB in 25-FT did not alter dry matter, NDF, hemicellulose, ADL, ether extract and gross energy intakes when compared to the control fed group (0-FT). The ADF and cellulose intake was higher in 25-FT than in the others (P  0.05). There are no differences in milk fatty profiles between dietary treatments (P > 0.05), except for OCFA. Goat fed with 25-FT had the lowest OCFA (P 
    Matched MeSH terms: Detergents/metabolism; Detergents/pharmacology
  12. Fulltext Nerolidol: A Sesquiterpene Alcohol with Multi-Faceted Pharmacological and Biological Activities
    Chan WK, Tan LT, Chan KG, Lee LH, Goh BH
    Molecules, 2016 Apr 28;21(5).
    PMID: 27136520 DOI: 10.3390/molecules21050529
    Nerolidol (3,7,11-trimethyl-1,6,10-dodecatrien-3-ol) is a naturally occurring sesquiterpene alcohol that is present in various plants with a floral odor. It is synthesized as an intermediate in the production of (3E)-4,8-dimethy-1,3,7-nonatriene (DMNT), a herbivore-induced volatile that protects plants from herbivore damage. Chemically, nerolidol exists in two geometric isomers, a trans and a cis form. The usage of nerolidol is widespread across different industries. It has been widely used in cosmetics (e.g., shampoos and perfumes) and in non-cosmetic products (e.g., detergents and cleansers). In fact, U.S. Food and Drug Administration (FDA) has also permitted the use of nerolidol as a food flavoring agent. The fact that nerolidol is a common ingredient in many products has attracted researchers to explore more medicinal properties of nerolidol that may exert beneficial effect on human health. Therefore, the aim of this review is to compile and consolidate the data on the various pharmacological and biological activities displayed by nerolidol. Furthermore, this review also includes pharmacokinetic and toxicological studies of nerolidol. In summary, the various pharmacological and biological activities demonstrated in this review highlight the prospects of nerolidol as a promising chemical or drug candidate in the field of agriculture and medicine.
    Matched MeSH terms: Detergents/pharmacology; Detergents/chemistry
  13. Fulltext The encapsulation of flavourzyme in nanoliposome by heating method
    Jahadi M, Khosravi-Darani K, Ehsani MR, Mozafari MR, Saboury AA, Pourhosseini PS
    J Food Sci Technol, 2015 Apr;52(4):2063-72.
    PMID: 25829586 DOI: 10.1007/s13197-013-1243-0
    The main objective of this study was to use heating method (HM) to prepare liposome without employing any chemical solvent or detergent. Plackett-Burman design (PBD) was applied for the screening of significant process variables including the lecithin proportion, the cholesterol/lecithin ratio, the pH of solution for liposome preparation, the enzyme/lecithin ratio, the stirring time, the process temperature, the speed of stirrer, the ratio of stirrer to the tank diameter, the application of homogenization, the method of adding enzyme and centrifugation conditions on the encapsulation efficiency (EE %) of liposome and the activity of liposomal Flavourzyme (LAPU(-1)) (P 
    Matched MeSH terms: Detergents
  14. Cross flow ultrafiltration studies on solutions of pectin with pulsatile flow in-situ cleaning
    Shamel MM, Sulaiman NM, Sulaiman MZ
    Artif Cells Blood Substit Immobil Biotechnol, 1999 Sep-Nov;27(5-6):447-53.
    PMID: 10595447
    A study was conducted to evaluate the cross flow tubular ultrafiltration behavior of aqueous solutions of pectin. The effectiveness of pulsatile flow as a cleaning-in-place (CIP) technique to improve permeate flux was undertaken on the above mentioned solution. This investigation is part of a study to apply membrane filtration in the clarification of tropical fruit juice. The main variables, which were investigated, include the concentration of pectin, pulse frequency and amplitude. It was found that the amount of pectin in the solution significantly affects its ultrafiltration behavior. From the observed profiles, it is evident that the formation of gel layer on the membrane surface is responsible for the leveling of flux at high pressures. The presence of pectin was found to affect the properties of the solution such as viscosity, pH and the size of pectin colloid. Improvements in the permeate flux for pectin solution were obtained by employing pulsatile flow cleaning-in-place technique. Both pulse frequency and amplitude are important parameters that can improve the improvement of in-situ cleaning method. Similar to several findings reported in the literature, pulsatile flow showed significant effectiveness of about 60% higher flux when the ultrafiltration process is operated under laminar condition.
    Matched MeSH terms: Detergents
  15. Fulltext Utilization of acid pre-treated coconut dregs as a substrate for production of detergent compatible lipase by Bacillus stratosphericus
    Mohd Zin NB, Mohamad Yusof B, Oslan SN, Wasoh H, Tan JS, Ariff AB, et al.
    AMB Express, 2017 Dec;7(1):131.
    PMID: 28651380 DOI: 10.1186/s13568-017-0433-y
    In recent years, many efforts have been directed to explore the methods to reduce the production costs of industrial lipase by improving the yield and the use of low-cost agricultural wastes. Coconut dregs, which is a lignocellulosic by-product from coconut oil and milk processing plants, is rich in cellulose (36%) and crude fat (9%). A newly isolated Bacillus stratosphericus has been demonstrated to perform cellulose hydrolysis on coconut dregs producing fermentable sugars. The highest extracellular lipase activity of 140 U/mL has been achieved in submerged fermentation with acid pre-treated coconut dregs. The lipase was found to be active over a wide range of temperatures and pHs. The activity of lipase can be generally increased by the presence of detergent ingredients such as Tween-80, cetyltrimethylammonium bromide, hydrogen peroxide and phosphate per sulphate. The great compatibility of lipase in commercial detergents has also underlined its potential as an additive ingredient in biodetergent formulations.
    Matched MeSH terms: Detergents
  16. Fulltext Potential of four corn varieties at different harvest stages for silage production in Malaysia
    Nazli MH, Halim RA, Abdullah AM, Hussin G, Samsudin AA
    Asian-Australas J Anim Sci, 2019 Feb;32(2):224-232.
    PMID: 29879832 DOI: 10.5713/ajas.18.0175
    OBJECTIVE: Apart from various climatic differences, corn harvest stage and varieties are two major factors that can influence the yield and quality of corn silage in the tropics. A study was conducted to determine the optimum harvest stage of four corn varieties for silage production in Malaysia.

    METHODS: Corn was harvested at four growth stages; silking, milk, dough, and dent stages from four varieties; Sweet Corn hybrid 926, Suwan, breeding test line (BTL) 1 and BTL 2. Using a split plot design, the treatments were then analysed based on the plant growth performance, yield, nutritive and feeding values followed by a financial feasibility study for potential commercialization.

    RESULTS: Significant differences and interactions were detected across the parameters suggesting varying responses among the varieties towards the harvest stages. Sweet Corn was best harvested early in the dough stage due to high dry matter (DM) yield, digestible nutrient, and energy content with low fibre portion. Suwan was recommended to be harvested at the dent stage when it gave the highest DM yield with optimum digestible nutrient and energy content with low acid detergent fibre. BTL 1 and BTL 2 varieties can either be harvested at dough or dent stages as the crude protein, crude fibre, DM yield, DM content, digestible nutrient and energy were not significantly different at either stage. Further financial analysis showed that only Sweet Corn production was not financially feasible while Suwan had the best financial appraisal values among the grain varieties.

    CONCLUSION: In conclusion, only the grain varieties tested had the potential for silage making according to their optimum harvest stage but Suwan is highly recommended for commercialization as it was the most profitable.

    Matched MeSH terms: Detergents
  17. Detergency stability and particle characterization of phosphate-free spray dried detergent powders incorporated with palm C16 methyl ester sulfonate (C16MES)
    Siwayanan P, Aziz R, Bakar NA, Ya H, Jokiman R, Chelliapan S
    J Oleo Sci, 2014;63(6):585-92.
    PMID: 24829132
    Phosphate-free spray dried detergent powders (SDDP) comprising binary anionic surfactants of palm C16 methyl ester sulfonate (C16MES) and linear alkyl benzene sulfonic acid (LABSA) were produced using a 5 kg/h-capacity co-current pilot spray dryer (CSD). Six phosphate-free detergent (PFD) formulations comprising C16MES/LABSA in various ratios under pH 7-8 were studied. Three PFD formulations having C16MES/LABSA in respective ratios of 0:100 (control), 20:80 and 40:60 ratios were selected for further evaluation based on their optimum detergent slurry concentrations. The resulting SDDP from these formulations were analysed for its detergency stability (over nine months of storage period) and particle characteristics. C16MES/LABSA of 40:60 ratio was selected as the ideal PFD formulation since its resulting SDDP has consistent detergency stability (variation of 2.3% in detergency/active over nine months storage period), excellent bulk density (0.37 kg/L), fine particle size at 50% cumulative volume percentage (D50 of 60.48 μm), high coefficient of particle size uniformity (D60/D10 of 3.86) and large spread of equivalent particle diameters. In terms of surface morphology, the SDDP of the ideal formulation were found to have regular hollow particles with smooth spherical surfaces. Although SDDP of the ideal formulation have excellent characteristics, but in terms of flowability, these powders were classified as slightly less free flowing (Hausner ratio of 1.27 and Carr's index of 21.3).
    Matched MeSH terms: Detergents/chemical synthesis*
  18. Biochemical Characterization of Thermostable and Detergent-Tolerant β-Agarase, PdAgaC, from Persicobacter sp. CCB-QB2
    Hafizah NF, Teh AH, Furusawa G
    Appl Biochem Biotechnol, 2019 Mar;187(3):770-781.
    PMID: 30073451 DOI: 10.1007/s12010-018-2849-5
    Persicobacter sp. CCB-QB2 belonging to the family Flammeovirga is an agarolytic bacterium and exhibits a diauxic growth in the presence of tryptone and agarose. A glycoside hydrolase (GH) 16 β-agarase, PdAgaC, was identified in the genome of the bacterium and was highly expressed during the second growth phase, indicating the agarase may play an important role in the diauxic growth. In this study, the catalytic domain of PdAgaC (PdAgaCgh) was cloned and characterized. PdAgaCgh showed thermostability at 50 °C and tolerance towards several detergents. In addition, the activity of PdAgaCgh after incubation with 0.1% of SDS and Triton X-100 increased approximately 1.2-fold. On the other hand, PdAgaCgh was sensitive to Fe2+, Ni2+, and Cu2+. The Km and Vmax of PdAgaCgh were 5.15 mg/ml and 2.9 × 103 U/mg, respectively. Interestingly, although the major hydrolytic product was neoagarobiose (NA2), monomeric sugar was also detected by thin-layer chromatographic analysis.
    Matched MeSH terms: Detergents/pharmacology*
  19. Preparation, characterization, immobilization, and molecular docking analysis of a novel detergent-stable subtilisin-like serine protease from Streptomyces mutabilis strain TN-X30
    Mechri S, Allala F, Bouacem K, Hasnaoui I, Gwaithan H, Chalbi TB, et al.
    Int J Biol Macromol, 2022 Dec 01;222(Pt A):1326-1342.
    PMID: 36242508 DOI: 10.1016/j.ijbiomac.2022.09.161
    We recently described the production of a detergent-biocompatible crude protease from Streptomyces mutabilis strain TN-X30. Here, we describe the purification, characterization, and immobilization of the serine alkaline protease (named SPSM), as well as the cloning, sequencing, and over-expression of its corresponding gene (spSM). Pure enzyme was obtained after ammonium sulphate precipitation followed by heat-treatment and Sephacryl® S-200 column purification. The sequence of the first 26 NH2-terminal residues of SPSM showed a high sequence identity to subtilisin-like serine proteases produced by actinobacteria. The spSM gene was heterologously expressed in Escherichia coli BL21(DE3)pLysS and E. coli BL21-AI™ strains using pTrc99A (rSPSM) and Gateway™ pDEST™ 17 [(His)6-tagged SPSM] vectors, respectively. Results obtained indicated that the (His)6-tagged SPSM showed the highest stability. The SPSM was immobilized using encapsulation and adsorption-encapsulation approaches and three different carriers. Features of SPSM in soluble and immobilized forms were analyzed by Fourier transform infrared (FTIR) spectroscopy in attenuated total reflection (ATR) mode, X-ray diffraction (XRD), zeta potential measurements, and field emission scanning electron microscopy (FE-SEM). The white clay and kaolin used in this study are eco-friendly binders to alginate-SPSM and show great potential for application of the immobilized SPSM in various industries. Molecular modeling and docking of N-succinyl-l-Phe-l-Ala-l-Ala-l-Phe-p-nitroanilide in the active site of SPSM revealed the involvement of 21 amino acids in substrate binding.
    Matched MeSH terms: Detergents*
  20. Fulltext Production of a solvent, detergent, and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations
    Khoramnia A, Ebrahimpour A, Beh BK, Lai OM
    J Biomed Biotechnol, 2011;2011:702179.
    PMID: 21960739 DOI: 10.1155/2011/702179
    The lipase production ability of a newly isolated Acinetobacter sp. in submerged (SmF) and solid-state (SSF) fermentations was evaluated. The results demonstrated this strain as one of the rare bacterium, which is able to grow and produce lipase in SSF even more than SmF. Coconut oil cake as a cheap agroindustrial residue was employed as the solid substrate. The lipase production was optimized in both media using artificial neural network. Multilayer normal and full feed forward backpropagation networks were selected to build predictive models to optimize the culture parameters for lipase production in SmF and SSF systems, respectively. The produced models for both systems showed high predictive accuracy where the obtained conditions were close together. The produced enzyme was characterized as a thermotolerant lipase, although the organism was mesophile. The optimum temperature for the enzyme activity was 45°C where 63% of its activity remained at 70°C after 2 h. This lipase remained active after 24 h in a broad range of pH (6-11). The lipase demonstrated strong solvent and detergent tolerance potentials. Therefore, this inexpensive lipase production for such a potent and industrially valuable lipase is promising and of considerable commercial interest for biotechnological applications.
    Matched MeSH terms: Detergents/chemistry
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