Displaying publications 181 - 200 of 248 in total

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  1. Khanahmadi S, Yusof F, Chyuan Ong H, Amid A, Shah H
    J Biotechnol, 2016 Aug 10;231:95-105.
    PMID: 27184429 DOI: 10.1016/j.jbiotec.2016.05.015
    Enzymatic reactions involving lipases as catalyst in transesterification can be an excellent alternative to produce environmental-friendly biodiesel. In this study, lipase extracted from Cocoa Pod Husk (CPH) and immobilized through cross linked enzyme aggregate (CLEA) technology catalysed the transesterification of Jatropha curcas oil successfully. Face centered central composite design (FCCCD) under response surface methodology (RSM) was used to get the optimal conditions of 3% (w/w) enzyme loading, 4h reaction time and 1:6 oil/ethanol ratio to achieve the highest conversion of free fatty acid and glycerides into biodiesel (93%). The reusability of CLEA-lipase was tested and after seven cycles, the conversion percentage reduced to 58%. The results revealed that CLEA lipase from CPH is a potential catalyst for biodiesel production.
    Matched MeSH terms: Lipase/metabolism*
  2. Azeman NH, Yusof NA, Abdullah J, Yunus R, Hamidon MN, Hajian R
    Molecules, 2015;20(7):12328-40.
    PMID: 26198220 DOI: 10.3390/molecules200712328
    In this paper, a comprehensive study has been made on the detection of free fatty acids (FFAs) in palm oil via an optical technique based on enzymatic aminolysis reactions. FFAs in crude palm oil (CPO) were converted into fatty hydroxamic acids (FHAs) in a biphasic lipid/aqueous medium in the presence of immobilized lipase. The colored compound formed after complexation between FHA and vanadium (V) ion solution was proportional to the FFA content in the CPO samples and was analyzed using a spectrophotometric method. In order to develop a rapid detection system, the parameters involved in the aminolysis process were studied. The utilization of immobilized lipase as catalyst during the aminolysis process offers simplicity in the product isolation and the possibility of conducting the process under extreme reaction conditions. A good agreement was found between the developed method using immobilized Thermomyces lanuginose lipase as catalyst for the aminolysis process and the Malaysian Palm Oil Board (MPOB) standard titration method (R2 = 0.9453).
    Matched MeSH terms: Lipase/chemistry*
  3. Ahmad B, Friar EP, Taylor E, Vohra MS, Serpell CJ, Garrett MD, et al.
    Eur J Pharmacol, 2023 Jan 05;938:175445.
    PMID: 36473593 DOI: 10.1016/j.ejphar.2022.175445
    In this study, the anti-obesity effects of 5,7,3',4',5-pentamethoxyflavone (PMF) and 6,2',4'-trimethoxyflavone (TMF) were evaluated through two distinct mechanisms of action: inhibition of crude porcine pancreatic lipase (PL), and inhibition of adipogenesis in 3T3-L1 pre-adipocytes. Both flavones show dose dependent, competitive inhibition of PL activity. Molecular docking studies revealed binding of the flavones to the active site of PL. In 3T3-L1 adipocytes, both flavones reduced the accumulation of lipids and triglycerides. PMF and TMF also lowered the expression of adipogenic and lipogenic genes. They both reduced the expression of peroxisome proliferator-activated receptor-gamma (PPAR-γ), CCAAT/enhancer-binding protein α and β (C/EBP α and β), sterol regulatory element-binding protein 1 (SREBF 1), fatty acid synthase (FASN), adipocyte binding protein 2 (aP2), and leptin gene. In addition, these flavones enhanced adiponectin mRNA expression, increased lipolysis and enhanced the expression of lipolytic genes: adipose triglycerides lipase (ATGL), hormone sensitive lipase (HSL) and monoglycerides lipase (MAGL) in mature 3T3-L1 adipocytes. Overall, PMF was seen to be a more potent inhibitor of both PL activity and adipogenesis versus TMF. These results suggest that PMF and TMF possess anti-obesity activities and can be further evaluated for their anti-obesity effects.
    Matched MeSH terms: Lipase/metabolism
  4. Yaacob N, Ahmad Kamarudin NH, Leow ATC, Salleh AB, Raja Abd Rahman RNZ, Mohamad Ali MS
    Molecules, 2017 Aug 12;22(8).
    PMID: 28805665 DOI: 10.3390/molecules22081312
    The alkaline cold-active lipase from Pseudomonas fluorescens AMS8 undergoes major structural changes when reacted with hydrophobic organic solvents. In toluene, the AMS8 lipase catalytic region is exposed by the moving hydrophobic lid 2 (Glu-148 to Gly-167). Solvent-accessible surface area analysis revealed that Leu-208, which is located next to the nucleophilic Ser-207 has a focal function in influencing substrate accessibility and flexibility of the catalytic pocket. Based on molecular dynamic simulations, it was found that Leu-208 strongly facilitates the lid 2 opening via its side-chain. The KM and Kcat/KM of L208A mutant were substrate dependent as it preferred a smaller-chain ester (pNP-caprylate) as compared to medium (pNP-laurate) or long-chain (pNP-palmitate) esters. In esterification of ethyl hexanoate, L208A promotes a higher ester conversion rate at 20 °C but not at 30 °C, as a 27% decline was observed. Interestingly, the wild-type (WT) lipase's conversion rate was found to increase with a higher temperature. WT lipase AMS8 esterification was higher in toluene as compared to L208A. Hence, the results showed that Leu-208 of AMS8 lipase plays an important role in steering a broad range of substrates into its active site region by regulating the flexibility of this region. Leu-208 is therefore predicted to be crucial for its role in interfacial activation and catalysis in toluene.
    Matched MeSH terms: Lipase/metabolism*; Lipase/chemistry*
  5. Rahman RN, Chin JH, Salleh AB, Basri M
    Mol Genet Genomics, 2003 May;269(2):252-60.
    PMID: 12756537
    A Bacillus sphaericus strain (205y) that produces an organic solvent-tolerant lipase was isolated in Port Dickson, Malaysia. The gene for the lipase was recovered from a genomic library and sequenced. Phylogenetic analysis was performed based on an alignment of thirteen microbial lipase sequences obtained from the NCBI database. The analysis suggested that the B. sphaericus lipase gene is a novel gene, as it is distinct from other lipase genes in Families I.4 and I.5 reported so far. Expression in Escherichia coli under the control of the lacZ promoter resulted in an eight-fold increase in enzyme activity after a 3-h induction with 1 mM IPTG. The crude enzyme thus obtained showed a slight (10%) enhancement in activity after a 30-min incubation in 25% (v/v) n-hexane at 37 degrees C, and retained 90% of its activity after a similar period in 25% (v/v) p-xylene.
    Matched MeSH terms: Lipase/genetics; Lipase/chemistry
  6. Leow TC, Rahman RN, Basri M, Salleh AB
    Biosci Biotechnol Biochem, 2004 Jan;68(1):96-103.
    PMID: 14745170
    A thermostable extracellular lipase of Geobacillus sp. strain T1 was cloned in a prokaryotic system. Sequence analysis revealed an open reading frame of 1,251 bp in length which codes for a polypeptide of 416 amino acid residues. The polypeptide was composed of a signal peptide (28 amino acids) and a mature protein of 388 amino acids. Instead of Gly, Ala was substituted as the first residue of the conserved pentapeptide Gly-X-Ser-X-Gly. Successful gene expression was obtained with pBAD, pRSET, pET, and pGEX as under the control of araBAD, T7, T7 lac, and tac promoters, respectively. Among them, pGEX had a specific activity of 30.19 Umg(-1) which corresponds to 2927.15 Ug(-1) of wet cells after optimization. The recombinant lipase had an optimum temperature and pH of 65 degrees C and pH 9, respectively. It was stable up to 65 degrees C at pH 7 and active over a wide pH range (pH 6-11). This study presents a rapid cloning and overexpression, aimed at improving the enzyme yield for successful industrial application.
    Matched MeSH terms: Lipase/genetics*; Lipase/metabolism*
  7. Safwani WK, Makpol S, Sathapan S, Chua KH
    Cell Tissue Bank, 2013 Jun;14(2):289-301.
    PMID: 22476937 DOI: 10.1007/s10561-012-9309-1
    Adipose tissue is a source of multipotent stem cells and it has the ability to differentiate into several types of cell lineages such as neuron cells, osteogenic and adipogenic cells. Most studies on human adipose-derived stem cells (ASCs) have been carried out at the early passages. For clinical usage, ASCs need to be expanded in vitro for a period of time to get sufficient cells for transplantation into patients. However, the impact of long-term culture on ASCs molecular characteristics has not been established yet. Several studies have also shown that osteogenic and adipogenic cells have the ability to switch pathways during in vitro culture as they share the same progenitor cells. This data is important to ensure their functionality and efficacy before being used clinically in the treatment of bone diseases. Therefore, we aim to investigate the effect of long-term culture on the adipogenic, stemness and osteogenic genes expression during osteogenic induction of ASCs. In this study, the molecular characteristics of ASCs during osteogenic induction in long-term culture was analysed by observing their morphological changes during induction, analysis of cell mineralization using Alizarin Red staining and gene expression changes using quantitative RT-PCR. Morphologically, cell mineralization at P20 was less compared to P5, P10 and P15. Adipogenesis was not observed as negative lipid droplets formation was recorded during induction. The quantitative PCR data showed that adipogenic genes expression e.g. LPL and AP2 decreased but PPAR-γ was increased after osteogenic induction in long-term culture. Most stemness genes decreased at P5 and P10 but showed no significant changes at P15 and P20. While most osteogenic genes increased after osteogenic induction at all passages. When compared among passages after induction, Runx showed a significant increased at P20 while BSP, OSP and ALP decreased at later passage (P15 and P20). During long-term culture, ASCs were only able to differentiate into immature osteogenic cells.
    Matched MeSH terms: Lipoprotein Lipase/genetics; Lipoprotein Lipase/metabolism
  8. Show PL, Tan CP, Shamsul Anuar M, Ariff A, Yusof YA, Chen SK, et al.
    Bioresour Technol, 2012 Jul;116:226-33.
    PMID: 22061444 DOI: 10.1016/j.biortech.2011.09.131
    An extractive fermentation technique was developed using a thermoseparating reagent to form a two-phase system for simultaneous cell cultivation and downstream processing of extracellular Burkholderia cepacia lipase. A 10% (w/w) solution of ethylene oxide-propylene oxide (EOPO) with a molecular mass of 3900 g/mol and pH 8.5, a 200 rpm speed, and 30 °C were selected as the optimal conditions for lipase production (55 U/ml). Repetitive batch fermentation was performed by continuous replacement of the top phase every 24h, which resulted in an average cell growth mass of 4.7 g/L for 10 extractive batches over 240 h. In scaling-up the process, a bench-scale bioreactor was tested under the conditions that had been optimized in flasks. The production rate and recovery yield were higher in the bioreactor compared to fermentation performed in flasks.
    Matched MeSH terms: Lipase/biosynthesis*; Lipase/isolation & purification
  9. Kadhum AA, Shamma MN
    Crit Rev Food Sci Nutr, 2017 Jan 02;57(1):48-58.
    PMID: 26048727
    Lipid is the general name given to fats and oils, which are the basic components of cooking oils, shortening, ghee, margarine, and other edible fats. The chosen term depends on the physical state at ambient temperature; fats are solids and oils are liquids. The chemical properties of the lipids, including degree of saturation, fatty acid chain length, and acylglycerol molecule composition are the basic determinants of physical characteristics such as melting point, cloud point, solid fat content, and thermal behavior. This review will discuss the major lipid modification strategies, hydrogenation, and chemical and enzymatic interesterification, describing the catalysts used mechanisms, kinetics, and impacts on the health-related properties of the final products. Enzymatic interesterification will be emphasized as method that produces a final product with good taste, zero trans fatty acids, and a low number of calories, requires less contact with chemicals, and is cost efficient.
    Matched MeSH terms: Lipase/metabolism; Lipase/chemistry
  10. Ado MA, Abas F, Mohammed AS, Ghazali HM
    Molecules, 2013;18(12):14651-69.
    PMID: 24287996 DOI: 10.3390/molecules181214651
    Plants that help in slowing down the digestion of triacylglycerols (TAGs) in the pancreas and small intestine of humans play an important role in the reduction of obesity. On the other hand, there may be plants or plant parts that stimulate intestinal lipolytic activity, thus contributing to greater TAG assimilation. The aim of this study was to evaluate the aqueous methanolic extracts of ninety eight (98) medicinal, herbal and aquatic plant materials from Malaysia for their effect on porcine pancreatic lipase (PPL) activity and to identify the structure of an anti-lipase compound from one of the sources. The degree of inhibition was also quantified as relative to orlistat activity against PPL (orlistat equivalents). Results revealed that while 19.4% of the extracts were found to have anti-lipase activity ≥80%, 12% were actually found to promote PPL activity. Twenty two percent (22.4%) exhibited moderate inhibition (41%-80%) and 2% were neutral toward PPL activity. The ripe fruit of Averrhoa carambola and the leaves of Archidendron jiringa (Jack) I.C Nielsen L. (jering), Cynometra cauliflora (nam-nam) and Aleurites moluccana (L.) Willd (candle nut/buah keras) had the highest (100%) anti-lipase activity and are equivalent to 0.11 µg orlistat/mL. Plants that stimulated lipase activity included Pimpinella anisum L. (aniseed/jintan manis), activating the enzyme by 186.5%. Kaempferol 3-O-rhamnoside was isolated from the ethyl acetate fraction of C. cauliflora leaves and found to be an active lipase inhibitor. The structure was elucidated using 1H-NMR, 13C-NMR and 2D-NMR analyses.
    Matched MeSH terms: Lipase/antagonists & inhibitors; Lipase/chemistry*
  11. Naganthran A, Masomian M, Rahman RNZRA, Ali MSM, Nooh HM
    Molecules, 2017 Sep 19;22(9).
    PMID: 28925972 DOI: 10.3390/molecules22091577
    The use of T1 lipase in automatic dishwashing detergent (ADD) is well established, but efficiency in hard water is very low. A new enzymatic environmentally-friendly dishwashing was formulated to be efficient in both soft and hard water. Thermostable enzymes such as T1 lipase from Geobacillus strain T1, Rand protease from Bacillussubtilis strain Rand, and Maltogenic amylase from Geobacillus sp. SK70 were produced and evaluated for an automatic dishwashing detergent formulation. The components of the new ADD were optimized for compatibility with these three enzymes. In compatibility tests of the enzymes with different components, several criteria were considered. The enzymes were mostly stable in non-ionic surfactants, especially polyhydric alcohols, Glucopon UP 600, and in a mixture of sodium carbonate and glycine (30:70) buffer at a pH of 9.25. Sodium polyacrylate and sodium citrate were used in the ADD formulation as a dispersing agent and a builder, respectively. Dishwashing performance of the formulated ADDs was evaluated in terms of percent of soil removed using the Leenert's Improved Detergency Tester. The results showed that the combination of different hydrolysis enzymes could improve the washing efficiency of formulated ADD compared to the commercial ADD "Finish" at 40 and 50 C.
    Matched MeSH terms: Lipase
  12. Riyadi FA, Alam MZ, Salleh MN, Salleh HM
    3 Biotech, 2017 Oct;7(5):300.
    PMID: 28884067 DOI: 10.1007/s13205-017-0932-1
    This study enhanced the production of thermostable organic solvent-tolerant (TS-OST) lipase by locally isolated thermotolerant Rhizopus sp. strain using solid-state fermentation (SSF) of palm kernel cake (PKC). The optimum conditions were achieved using a series of statistical approaches. The cultivation parameters, which include fermentation time, moisture content, temperature, pH, inoculum size, various carbon and nitrogen sources, as well as other supplements, were initially screened by the definitive screening design, and one-factor-at-a-time using PKC as the basal medium. Three significant factors (olive oil concentration, pH, and inoculum size) were further optimized using face-centred central composite design. The results indicated a successful and significant improvement of lipase activity by almost two-fold compared to the initial screening production. The findings showed that the optimal conditions were 2% (v/w) inoculum size, 2% (v/w) olive oil, 0.6% (w/w) peptone, 2% (v/w) ethanol, 70% moisture content at initial pH 10.0 and 45 °C within 72 h of fermentation. Process optimization resulted in maximum lipase activity of 58.63 U/gram dry solids (gds). The analysis of variance showed that the statistical model was significant (p value <0.0001) and reliable with a high value of R2 (0.98) and adjusted R2 (0.96). This indicates a better correlation between the actual and predicted responses of lipase production. By considering this study, the low-cost PKC through SSF appears to be promising in the utilization of agro-industrial waste for TS-OST lipase production. This is because satisfactory enzyme activity could be attained that promises industrial applications.
    Matched MeSH terms: Lipase
  13. Abd Manan FM, Attan N, Zakaria Z, Mahat NA, Abdul Wahab R
    J Biotechnol, 2018 May 28;280:19-30.
    PMID: 29852195 DOI: 10.1016/j.jbiotec.2018.05.015
    To overcome drawbacks in the conventional chemical route to synthesize eugenyl benzoate, immobilized Rhizomucor miehei lipase (RML) as the biocatalyst was proposed. The RML conjugated to a hybrid support consisting of biopolymers, chitosan (CS) and chitin nanowhiskers (CNWs). 1-ethyl-3-[3-dimethylaminopropyl]carbodiimide hydrochloride (EDAC) was used as the crosslinker to bind the lipase. Immobilization of RML was the highest on crosslinked CS/CNWs which gave a protein loading of ∼8.12 mg/g, corresponding to specific and residual activity of 537 U/g and 137%, respectively. Fourier transform infrared spectroscopy, thermogravimetric analysis-differential thermogravimetry, field emission scanning electron and atomic force microscopy of RML-CS/CNWs revealed that RML was successfully attached to the surface of crosslinked CS/CNWs. Under an optimized condition, the highest yield of eugenyl benzoate (56.3%) was attained after 5 h using 3 mg/mL of RML-CS/CNWs with molar ratio of eugenol: benzoic acid of 3:1, as compared to only 47.3% for the free RML. Analyses of FTIR and NMR on purified eugenyl benzoate affirmed that the ester was successfully produced in the enzymatic esterification. Therefore, the use of the RML-CS/CNWs biocatalysts appears promising to afford good yields of eugenyl benzoate within a relatively shorter reaction time.
    Matched MeSH terms: Lipase
  14. Che Hussian CHA, Raja Abd Rahman RNZ, Thean Chor AL, Salleh AB, Mohamad Ali MS
    PeerJ, 2018;6:e5833.
    PMID: 30479887 DOI: 10.7717/peerj.5833
    T1 Lipase is a thermostable secretary protein of Geobacillus zalihae strain previously expressed in a prokaryotic system and purified using three-step purification: affinity 1, affinity 2, and ion exchange chromatography (IEX). This approach is time consuming and offers low purity and recovery yield. In order to enhance the purification strategy of T1 lipase, affinity 2 was removed so that after affinity 1, the cleaved Glutathione S-transferase (GST) and matured T1 lipase could be directly separated through IEX. Therefore, a rational design of GST isoelectric point (pI) was implemented by prediction using ExPASy software in order to enhance the differences of pI values between GST and matured T1 lipase. Site-directed mutagenesis at two locations flanking the downstream region of GST sequences (H215R and G213R) was successfully performed. Double point mutations changed the charge on GST from 6.10 to 6.53. The purified lipase from the new construct GST tag mutant-T1 was successfully purified using two steps of purification with 6,849 U/mg of lipase specific activity, 33% yield, and a 44-fold increase in purification. Hence, the increment of the pI values in the GST tag fusion T1 lipase resulted in a successful direct separation through IEX and lead to successful purification.
    Matched MeSH terms: Lipase
  15. Ibrahim M, Abdul Azziz SSS, Wong CF, Bakri YM, Abdullah F
    Curr Comput Aided Drug Des, 2020;16(6):698-706.
    PMID: 31648647 DOI: 10.2174/1573409915666191015112320
    BACKGROUND: Obesity is one serious health condition that contributes to various chronic diseases. The inhibition of pancreatic lipase is a promising treatment for obesity.

    OBJECTIVE: The present study was designed to investigate anti-porcine pancreatic lipase effect of isolated compounds from Aquilaria subintegra and its mechanism.

    METHODS: Compounds were isolated with serial column chromatography and their structure were identified using spectroscopic methods. Isolated compounds were tested for anti-lipase potential activity using colorimetric assay. The prediction of energy binding between isolated compounds and enzyme was described using YASARA software.

    RESULTS: Four compounds were successfully isolated from the bark of A. subintegra, namely, 5- hydroxy-7,4'-dimethoxyflavone, luteolin-7,3',4'-trimethyl ether, 5,3'-dihydroxy-7,4'-dimethoxyflavone and β-sitosterol. The results indicated that all compounds displayed promising pancreatic lipase inhibitory activity ranging between of 6% to 53% inhibition. Compound 5-hydroxy-7,4'- dimethoxyflavone was a competitive inhibitor and decreases the enzyme catalysis. Meanwhile, β- sitosterol was a non- competitive inhibitor since the latter was bind allosterically toward enzyme.

    CONCLUSION: This finding is significant for further investigation of bioactive compounds from A. subintegra on animal study.

    Matched MeSH terms: Lipase
  16. Musa H, Kasim FH, Gunny AAN, Gopinath SCB, Ahmad MA
    3 Biotech, 2019 Aug;9(8):314.
    PMID: 31406636 DOI: 10.1007/s13205-019-1845-y
    Initially, a new moderate halophilic strain was locally isolated from seawater. The partial 16S rRNA sequence analysis positioned the organism in Marinobacter genus and was named 'Marinobacter litoralis SW-45'. This study further demonstrates successful utilization of the halophilic M. litoralis SW-45 lipase (MLL) for butyl ester synthesis from crude palm fruit oil (CPO) and kernel oil (CPKO) in heptane and solvent-free system, respectively, using hydroesterification. Hydrolysis and esterification of enzymatic [Thermomyces lanuginosus lipase (TLL)] hydrolysis of CPO and CPKO to free fatty acids (FFA) followed by MLL-catalytic esterification of the concentrated FFAs with butanol (acyl acceptor) to synthesize butyl esters were performed. A one-factor-at-a-time technique (OFAT) was used to study the influence of physicochemical factors on the esterification reaction. Under optimal esterification conditions of 40 and 45 °C, 150 and 230 rpm, 50% (v/v) biocatalyst concentration, 1:1 and 5:1 butanol:FFA, 9% and 15% (w/v) NaCl, 60 and 15 min reaction time for CPO- and CPKO-derived FFA esterification system, maximum ester conversion of 62.2% and 69.1%, respectively, was attained. Gas chromatography (GC) analysis confirmed the products formed as butyl esters. These results showed halophilic lipase has promising potential to be used for biosynthesis of butyl esters in oleochemical industry.
    Matched MeSH terms: Lipase
  17. Liang JL, Yeow CC, Teo KC, Gnanaraj C, Chang YP
    J Food Sci Technol, 2019 Oct;56(10):4696-4704.
    PMID: 31686701 DOI: 10.1007/s13197-019-03912-5
    The capsicum seed core and cabbage outer leaves are common wastes generated in the vegetable processing industry. We explored the in vitro health-promoting activity of these waste products for valorization. Freeze-dried and pulverized cabbage wastes had a high bile acid binding capacity and the capsicum wastes inhibited glucose dialysis more effectively. Methanolic extracts prepared with conventional solvent extraction and ultrasound-assisted extraction were analyzed to determine their 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging capacity, in vitro α-amylase inhibitory, in vitro lipase inhibitory, and prebiotic activity. Crude extracts of cabbage and capsicum wastes were screened using GC-MS analysis. The cabbage waste extracts showed high antioxidant activities but did not inhibit α-amylase. The capsicum waste extracts inhibited both lipase and α-amylase activities and supported the growth of the probiotic bacterium, Lactobacilli brevis. Volatile compounds of the vegetables consisted mainly of phenols and fatty acid esters. In all assays except the α-amylase inhibition assay, the extracts prepared with ultrasound-assisted solvent extraction showed higher activity than those prepared using the conventional method. The capsicum seed core and cabbage outer leaves are potential sources of phytochemicals and antioxidant fibers. Capsicum waste extract supported probiotic bacterial growth without a lag phase. These waste products may be processed into high-value functional ingredients.
    Matched MeSH terms: Lipase
  18. Adlan NA, Sabri S, Masomian M, Ali MSM, Rahman RNZRA
    Front Microbiol, 2020;11:565608.
    PMID: 33013795 DOI: 10.3389/fmicb.2020.565608
    The deposition of paraffin wax in crude oil is a problem faced by the oil and gas industry during extraction, transportation, and refining of crude oil. Most of the commercialized chemical additives to prevent wax are expensive and toxic. As an environmentally friendly alternative, this study aims to find a novel thermophilic bacterial strain capable of degrading paraffin wax in crude oil to control wax deposition. To achieve this, the biodegradation of crude oil paraffin wax by 11 bacteria isolated from seawater and oil-contaminated soil samples was investigated at 70°C. The bacteria were identified as Geobacillus kaustophilus N3A7, NFA23, DFY1, Geobacillus jurassicus MK7, Geobacillus thermocatenulatus T7, Parageobacillus caldoxylosilyticus DFY3 and AZ72, Anoxybacillus geothermalis D9, Geobacillus stearothermophilus SA36, AD11, and AD24. The GCMS analysis showed that strains N3A7, MK7, DFY1, AD11, and AD24 achieved more than 70% biodegradation efficiency of crude oil in a short period (3 days). Notably, most of the strains could completely degrade C37-C40 and increase the ratio of C14-C18, especially during the initial 2 days incubation. In addition, the degradation of crude oil also resulted in changes in the pH of the medium. The degradation of crude oil is associated with the production of degradative enzymes such as alkane monooxygenase, alcohol dehydrogenase, lipase, and esterase. Among the 11 strains, the highest activities of alkane monooxygenase were recorded in strain AD24. A comparatively higher overall alcohol dehydrogenase, lipase, and esterase activities were observed in strains N3A7, MK7, DFY1, AD11, and AD24. Thus, there is a potential to use these strains in oil reservoirs, crude oil processing, and recovery to control wax deposition. Their ability to withstand high temperature and produce degradative enzymes for long-chain hydrocarbon degradation led to an increase in the short-chain hydrocarbon ratio, and subsequently, improving the quality of the oil.
    Matched MeSH terms: Lipase
  19. Cheng TH, Ismail N, Kamaruding N, Saidin J, Danish-Daniel M
    Biotechnol Rep (Amst), 2020 Sep;27:e00482.
    PMID: 32514406 DOI: 10.1016/j.btre.2020.e00482
    Industrial enzymes are important for various biotechnological applications. Currently, the diversity of industrial enzymes-producing marine bacteria from Malaysia remains mostly unknown. This study investigated the diversity of industrial enzyme-producing marine bacteria from culture collections at the Institute of Marine Biotechnology, Universiti Malaysia Terengganu. Out of 200 bacterial isolates revived, 163 bacteria isolate were successfully growth. Marine bacteria produced enzymes with total scoring higher than four were selected for molecular identification using 16S rDNA. About 161 bacteria isolate secreted amylase (68.7 %), lipase (88.3 %) and protease (68.7 %). The phylogenetic analysis led to the identification of three major phyla, namely Proteobacteria, Firmicutes and Bacteroidetes. These phyla were differentiated into nine genera consisted of Bacillus, Chryseomicrobium, Photobacterium, Pseudoalteromonas, Ruegeria, Shewanella, Solibacillus, Tenacibaculum and Vibrio. Genetic variation was more likely to occur within similar marine bacteria species. The microbial community was found to affect the production of industrial enzymes and the diversity of marine bacteria.
    Matched MeSH terms: Lipase
  20. Al Kuddoos NM, Ismail AK, Shen KWC, Shibraumalisi NA, Yunus AY
    Bull Emerg Trauma, 2020 Oct;8(4):249-252.
    PMID: 33426141 DOI: 10.30476/beat.2020.85719
    Pancreatic injury in paediatrics is a rare condition and can be difficult to diagnose. The diagnostic challenge is due to its symptom of vague abdominal pain which usually results in late presentation. Elevated biochemical markers such as amylase and lipase can aid in the evaluation of pancreatic injury, however, it is not specific and is only evident after several hours of trauma. Ultrasound is commonly used as a primary modality to evaluate abdominal organ injuries, but its role in detecting pancreatic injury is limited due to low sensitivity. High index of suspicion is needed to avoid undiagnosed pancreatic injury which could be lethal to children. We herein report a case of delayed presentation of isolated pancreatic tail injury in a child who was sufficiently diagnosed with ultrasound and treated conservatively. Proper initial assessment and diagnosis will allow appropriate management of pancreatic injury. Conservative management should include serial imaging to look at the evolution of pancreatic injury and detect complications such as pseudocyst or abscess formation.
    Matched MeSH terms: Lipase
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