Displaying publications 201 - 220 of 248 in total

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  1. Fulltext Enhancing food waste biodegradation rate in a food waste biodigester with the synergistic action of hydrolase-producing Bacillus paralicheniformis GRA2 and Bacillus velezensis TAP5 co-culture inoculation
    Roslan MAM, Jefri NQUA, Ramlee N, Rahman NAA, Chong NHH, Bunawan H, et al.
    Saudi J Biol Sci, 2021 May;28(5):3001-3012.
    PMID: 34012331 DOI: 10.1016/j.sjbs.2021.02.041
    Food waste (FW) minimization at the source by using food waste biodigester (FWBs) has a vast potential to lower down the impact of increasing organic fraction in municipal solid waste generation. To this end, this research sought to check the performance of locally isolated hydrolase-producing bacteria (HPB) to improve food waste biodegradation rate. Two under-explored HPB identified as Bacillus paralicheniformis GRA2 and Bacillus velezensis TAP5 were able to produce maximum amylase, cellulase, protease and lipase activities, and demonstrated a significant hydrolase synergy in co-culture fermentation. In vitro biodegradation analysis of both autoclaved and non-autoclaved FW revealed that the HPB inoculation was effective to degrade total solids (>62%), protein (>19%), total fat (>51), total sugar (>86%), reducing sugar (>38%) and starch (>50%) after 8-day incubation. All co-culture treatments were recorded superior to the respective monocultures and the uninoculated control. The results of FW biodegradation using batch-biodigester trial indicated that the 1500 mL and 1000 mL inoculum size of HPB inoculant reached a plateau on the 4th day, with gross biodegradation percentage (GBP) of >85% as compared to control (66.4%). The 1000 mL inoculum was sufficient to achieve the maximum GBP (>90%) of FW after an 8-day biodigestion in a FWB.
    Matched MeSH terms: Lipase
  2. Cold-adapted organic solvent tolerant alkalophilic family I.3 lipase from an Antarctic Pseudomonas
    Ganasen M, Yaacob N, Rahman RN, Leow AT, Basri M, Salleh AB, et al.
    Int J Biol Macromol, 2016 Nov;92:1266-1276.
    PMID: 27506122 DOI: 10.1016/j.ijbiomac.2016.06.095
    Lipolytic enzymes with cold adaptation are gaining increasing interest due to their biotechnological prospective. Previously, a cold adapted family I.3 lipase (AMS8 lipase) was isolated from an Antarctic Pseudomonas. AMS8 lipase was largely expressed in insoluble form. The refolded His-tagged recombinant AMS8 lipase was purified with 23.0% total recovery and purification factor of 9.7. The purified AMS8 lipase migrated as a single band with a molecular weight approximately 65kDa via electrophoresis. AMS8 lipase was highly active at 30°C at pH 10. The half-life of AMS8 lipase was reported at 4 and 2h under the incubation of 30 and 40°C, respectively. The lipase was stable over a broad range of pH. It showed enhancement effect in its relative activity under the presence of Li(+), Na(+), K(+), Rb(+) and Cs(+) after 30min treatment. Heavy metal ions such as Cu(2+), Fe(3+) and Zn(2+) inhibited AMS8 activity. This cold adapted alkalophilic AMS lipase was also active in various organic solvent of different polarity. These unique properties of this biological macromolecule will provide considerable potential for many biotechnological applications and organic synthesis at low temperature.
    Matched MeSH terms: Lipase/genetics; Lipase/isolation & purification; Lipase/chemistry*
  3. Fatty acid preference of mycelium-bound lipase from a locally isolated strain of Geotrichum candidum
    Loo JL, Lai OM, Long K, Ghazali HM
    World J Microbiol Biotechnol, 2007 Dec;23(12):1771-8.
    PMID: 27517833 DOI: 10.1007/s11274-007-9427-2
    Mycelium-bound lipase (MBL) was prepared using a strain of Geotrichum candidum isolated from local soil. At the time of maximum lipase activity (54 h), the mycelia to which the lipase was bound were harvested by filtration and centrifugation. Dry MBL was prepared by lyophilizing the mycelia obtained. The yield of MBL was 3.66 g/l with a protein content of 44.11 mg/g. The lipase activity and specific lipase activity were 22.59 and 510 U/g protein, respectively. The moisture content of the MBL was 3.85%. The activity of free (extracellular) lipase in the culture supernatant (after removal of mycelia) was less than 0.2 U/ml. The MBL showed selectivity for oleic acid over palmitic acid during hydrolysis of palm olein, indicating that the lipase from G. candidum displayed high substrate selectivity for unsaturated fatty acid containing a cis-9 double bond, even in crude form. This unique specificity of MBL could be a direct, simple and inexpensive way in the fats and oil industry for the selective hydrolysis or transesterification of cis-9 fatty acid residues in natural triacylglycerols.
    Matched MeSH terms: Lipase
  4. Fulltext Expression and characterization of thermotolerant lipase with broad pH profiles isolated from an Antarctic Pseudomonas sp strain AMS3
    Latip W, Raja Abd Rahman RNZ, Chor Leow AT, Mohd Shariff F, Mohamad Ali MS
    PeerJ, 2016;4:e2420.
    PMID: 27781152 DOI: 10.7717/peerj.2420
    A gene encoding a thermotolerant lipase with broad pH was isolated from an Antarctic Pseudomonas strain AMS3. The recombinant lipase AMS3 was purified by single-step purification using affinity chromatography, yielding a purification fold of approximately 1.52 and a recovery of 50%. The molecular weight was approximately ∼60 kDa including the strep and affinity tags. Interestingly, the purified Antarctic AMS3 lipase exhibited broad temperature profile from 10-70 °C and stable over a broad pH range from 5.0 to pH 10.0. Various mono and divalent metal ions increased the activity of the AMS3 lipase, but Ni(2+) decreased its activity. The purified lipase exhibited the highest activity in the presence of sunflower oil. In addition, the enzyme activity in 25% v/v solvents at 50 °C particularly to n-hexane, DMSO and methanol could be useful for catalysis reaction in organic solvent and at broad temperature.
    Matched MeSH terms: Lipase
  5. Fulltext Lid opening and conformational stability of T1 Lipase is mediated by increasing chain length polar solvents
    Maiangwa J, Mohamad Ali MS, Salleh AB, Rahman RNZRA, Normi YM, Mohd Shariff F, et al.
    PeerJ, 2017;5:e3341.
    PMID: 28533982 DOI: 10.7717/peerj.3341
    The dynamics and conformational landscape of proteins in organic solvents are events of potential interest in nonaqueous process catalysis. Conformational changes, folding transitions, and stability often correspond to structural rearrangements that alter contacts between solvent molecules and amino acid residues. However, in nonaqueous enzymology, organic solvents limit stability and further application of proteins. In the present study, molecular dynamics (MD) of a thermostable Geobacillus zalihae T1 lipase was performed in different chain length polar organic solvents (methanol, ethanol, propanol, butanol, and pentanol) and water mixture systems to a concentration of 50%. On the basis of the MD results, the structural deviations of the backbone atoms elucidated the dynamic effects of water/organic solvent mixtures on the equilibrium state of the protein simulations in decreasing solvent polarity. The results show that the solvent mixture gives rise to deviations in enzyme structure from the native one simulated in water. The drop in the flexibility in H2O, MtOH, EtOH and PrOH simulation mixtures shows that greater motions of residues were influenced in BtOH and PtOH simulation mixtures. Comparing the root mean square fluctuations value with the accessible solvent area (SASA) for every residue showed an almost correspondingly high SASA value of residues to high flexibility and low SASA value to low flexibility. The study further revealed that the organic solvents influenced the formation of more hydrogen bonds in MtOH, EtOH and PrOH and thus, it is assumed that increased intraprotein hydrogen bonding is ultimately correlated to the stability of the protein. However, the solvent accessibility analysis showed that in all solvent systems, hydrophobic residues were exposed and polar residues tended to be buried away from the solvent. Distance variation of the tetrahedral intermediate packing of the active pocket was not conserved in organic solvent systems, which could lead to weaknesses in the catalytic H-bond network and most likely a drop in catalytic activity. The conformational variation of the lid domain caused by the solvent molecules influenced its gradual opening. Formation of additional hydrogen bonds and hydrophobic interactions indicates that the contribution of the cooperative network of interactions could retain the stability of the protein in some solvent systems. Time-correlated atomic motions were used to characterize the correlations between the motions of the atoms from atomic coordinates. The resulting cross-correlation map revealed that the organic solvent mixtures performed functional, concerted, correlated motions in regions of residues of the lid domain to other residues. These observations suggest that varying lengths of polar organic solvents play a significant role in introducing dynamic conformational diversity in proteins in a decreasing order of polarity.
    Matched MeSH terms: Lipase
  6. Fulltext Enhancement of a protocol purifying T1 lipase through molecular approach
    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
  7. Fulltext Valorizing cabbage (Brassica oleracea L. var. capitata) and capsicum (Capsicum annuum L.) wastes: in vitro health-promoting activities
    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
  8. Fulltext Optimization of thermostable organic solvent-tolerant lipase production by thermotolerant Rhizopus sp. using solid-state fermentation of palm kernel cake
    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
  9. Fulltext Improving the Efficiency of New Automatic Dishwashing Detergent Formulation by Addition of Thermostable Lipase, Protease and Amylase
    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
  10. Fulltext Medicinal Plants and Their Inhibitory Activities against Pancreatic Lipase: A Review
    Seyedan A, Alshawsh MA, Alshagga MA, Koosha S, Mohamed Z
    Evid Based Complement Alternat Med, 2015;2015:973143.
    PMID: 26640503 DOI: 10.1155/2015/973143
    Obesity is recognized as a major life style disorder especially in developing countries and it is prevailing at an alarming speed in new world countries due to fast food intake, industrialization, and reduction of physical activity. Furthermore, it is associated with a vast number of chronic diseases and disabilities. To date, relatively effective drugs, from either natural or synthetic sources, are generally associated with serious side effects, often leading to cessation of clinical trials or even withdrawal from the market. In order to find new compounds which are more effective or with less adverse effects compared to orlistat, the drug that has been approved for obesity, new compounds isolated from natural products are being identified and screened for antiobesity effects, in particular, for their pancreatic lipase inhibitory effect. Pancreatic lipase inhibitory activity has been extensively used for the determination of potential efficacy of natural products as antiobesity agents. In attempts to identify natural products for overcoming obesity, more researches have been focused on the identification of newer pancreatic lipase inhibitors with less unpleasant adverse effects. In this review, we consider the potential role of plants that have been investigated for their pancreatic lipase inhibitory activity.
    Matched MeSH terms: Lipase
  11. Fulltext Enhanced biocatalytic esterification with lipase-immobilized chitosan/graphene oxide beads
    Lau SC, Lim HN, Basri M, Fard Masoumi HR, Ahmad Tajudin A, Huang NM, et al.
    PLoS One, 2014;9(8):e104695.
    PMID: 25127038 DOI: 10.1371/journal.pone.0104695
    In this work, lipase from Candida rugosa was immobilized onto chitosan/graphene oxide beads. This was to provide an enzyme-immobilizing carrier with excellent enzyme immobilization activity for an enzyme group requiring hydrophilicity on the immobilizing carrier. In addition, this work involved a process for the preparation of an enzymatically active product insoluble in a reaction medium consisting of lauric acid and oleyl alcohol as reactants and hexane as a solvent. This product enabled the stability of the enzyme under the working conditions and allowed the enzyme to be readily isolated from the support. In particular, this meant that an enzymatic reaction could be stopped by the simple mechanical separation of the "insoluble" enzyme from the reaction medium. Chitosan was incorporated with graphene oxide because the latter was able to enhance the physical strength of the chitosan beads by its superior mechanical integrity and low thermal conductivity. The X-ray diffraction pattern showed that the graphene oxide was successfully embedded within the structure of the chitosan. Further, the lipase incorporation on the beads was confirmed by a thermo-gravimetric analysis. The lipase immobilization on the beads involved the functionalization with coupling agents, N-hydroxysulfosuccinimide sodium (NHS) and 1-ethyl-(3-dimethylaminopropyl) carbodiimide (EDC), and it possessed a high enzyme activity of 64 U. The overall esterification conversion of the prepared product was 78% at 60 °C, and it attained conversions of 98% and 88% with commercially available lipozyme and novozyme, respectively, under similar experimental conditions.
    Matched MeSH terms: Lipase/metabolism*
  12. Interesterification of engkabang (Shorea macrophylla) fat--canola oil blend with lipase from Candida antarctica to simulate the properties of lard
    Illiyin MR, Marikkar JM, Loke MK, Shuhaimi M, Mahiran B, Miskandar MS
    J Oleo Sci, 2014;63(1):39-46.
    PMID: 24389796
    A study was carried out to compare the composition and thermal properties of lard (LD) and engkabang fat (EF) - canola oil (CaO) blend interesterified with Candida antartica lipase (C. antartica). A fat blend EF-4 (40% EF in CaO) was prepared and interesterified using C. antartica lipase at 60°C for different time intervals (6 h, 12 h and 24 h) with 200 rpm agitation. The fat blends before and after interesterification were compared to LD with respect to their slip melting points (SMP), fatty acid and triacyglycerol (TAG) compositions, melting, solidification and polymorphic properties. Result showed that the slip melting point (SMP) of the fat blend interesterified for 6 h was the closest to that of LD. The solid fat content (SFC) values of fat blends interesterified for 12 and 24 h were found to become equal to those of LD within the temperature range of 0 to 20°C. In addition, all three interesterified blends had SFC values similar to those of LD within the temperature range of 30-40°C. According to thermal analysis, the transition of the fat blend interesterified for 24 h appearing at -2.39°C was similar to the low melting thermal transition of LD and the transition of the fat blend interesterified for 12 h appearing at 26.25°C was similar to the high melting thermal transition of LD. However, there is no compatibility between LD and all three interesterified blends with regard to polymorphic behaviour.
    Matched MeSH terms: Lipase/chemistry*
  13. Enantioseparation of (R,S)-ketoprofen using Candida antarctica lipase B in an enzymatic membrane reactor
    Ong AL, Kamaruddin AH, Bhatia S, Aboul-Enein HY
    J Sep Sci, 2008 Jul;31(13):2476-85.
    PMID: 18646277 DOI: 10.1002/jssc.200800086
    An enzymatic membrane reactor (EMR) for enantioseparation of (R,S)-ketoprofen via Candida antarctica lipase B (CALB) as biocatalyst was investigated. A comparative study of free and immobilized CALB was further conducted. The catalytic behaviour of CALB in an EMR was affected by the process parameters of enzyme load, substrate concentration, substrate molar ratio, lipase solution pH, reaction temperature, and substrate flow rate. Immobilization of CALB in the EMR was able to reduce the amount of enzyme required for the enantioseparation of (R,S)-ketoprofen. Immobilized CALB in the EMR assured higher reaction capacity, better thermal stability, and reusability. It was also found to be more cost effective and practical than free CALB in a batch reactor.
    Matched MeSH terms: Lipase*
  14. Studies of reaction parameters on synthesis of Citronellyl laurate ester via immobilized Candida rugosa lipase in organic media
    Serri NA, Kamaruddin AH, Long WS
    Bioprocess Biosyst Eng, 2006 Oct;29(4):253-60.
    PMID: 16868763
    Immobilized Candida rugosa lipase was used for the synthesis of citronellyl laurate from citronellol and lauric acid. Screening of different types of support (Amberlite MB-1 and Celite) for immobilization of lipase and solvent (n-hexane, n-heptane, and iso-octane) and optimization of reaction conditions, such as catalyst loading, effect of substrates molar ratio and temperature, have been studied. The maximum enzyme activity was obtained at 310 K. The immobilized C. rugosa lipase onto Amberlite MB-1 support was found to be the best support with a conversion of 89% of citronellyl laurate ester in iso-octane compared to Celite 545. Deactivation of C. rugosa lipase at 313, 318 and 323 K were observed. Ordered bi bi mechanism with dead end complex of lauric acid was found to fit the initial rate data and the kinetic parameters were obtained by non-linear regression analysis.
    Matched MeSH terms: Lipase/chemistry*
  15. Effect of enzymatic interesterification on melting point of palm olein
    Yassin AA, Mohamed IO, Ibrahim MN, Yusoff MS
    Appl Biochem Biotechnol, 2003 Jul;110(1):45-52.
    PMID: 12909731
    Immobilized PS-C 'Amano' II lipase was used to catalyze the interesterification of palm olein (POo) with 30, 50, and 70% stearic acid in n-hexane at 60 degrees C. The catalytic performance of the immobilized lipase was evaluated by determining the composition change of fatty acyl groups and triacylglycerol (TAG) by gas liquid chromatography and high-performance liquid chromatography, respectively. The interesterification process resulted in the formation of new TAGs, mainly tripalmitin and dipalmitostearin, both of which were absent in the original oil. These changes in TAG composition resulted in an increase in slip melting point, from the original 25.5 degrees C to 36.3, 37.0, and 40.0 degrees C in the modified POo with 30, 50, and 70% stearic acid, respectively. All the reactions attained steady state in about 6 h. This type of work will find great applications in food industries, such as confectionery.
    Matched MeSH terms: Lipase/chemistry*
  16. Fulltext A multi-ethnic study of a PNPLA3 gene variant and its association with disease severity in non-alcoholic fatty liver disease
    Zain SM, Mohamed R, Mahadeva S, Cheah PL, Rampal S, Basu RC, et al.
    Hum Genet, 2012 Jul;131(7):1145-52.
    PMID: 22258181 DOI: 10.1007/s00439-012-1141-y
    The adiponutrin (PNPLA3) rs738409 polymorphism has been found to be associated with susceptibility to non-alcoholic fatty liver disease (NAFLD) in various cohorts. We further investigated the association of this polymorphism with non-alcoholic steatohepatitis (NASH) severity and with histological features of NAFLD. A total of 144 biopsy-proven NAFLD patients and 198 controls were genotyped for PNPLA3 gene polymorphism (rs738409 C>G). The biopsy specimens were histologically graded by a qualified pathologist. We observed an association of G allele with susceptibility to NAFLD in the pooled subjects (OR 2.34, 95% CI 1.69-3.24, p < 0.0001), and following stratification, in each of the three ethnic subgroups, namely Chinese, Indian and Malay (OR 1.94, 95% CI 1.12-3.37, p = 0.018; OR 3.51, 95% CI 1.69-7.26, p = 0.001 and OR 2.05, 95% CI 1.25-3.35, p = 0.005, respectively). The G allele is associated with susceptibility to NASH (OR 2.64, 95% CI 1.85-3.75, p < 0.0001), with NASH severity (OR 1.85, 95% CI 1.05-3.26, p = 0.035) and with presence of fibrosis (OR 1.95, 95% CI 1.17-3.26, p = 0.013) but not with simple steatosis nor with other histological parameters. Although the serum triglyceride level is significantly higher in NAFLD patients compared to controls, the G allele is associated with decreased level of triglycerides (p = 0.029) in the NAFLD patients. Overall, the rs738409 G allele is associated with severity of NASH and occurrence of fibrosis in patients with NAFLD.
    Matched MeSH terms: Lipase/genetics*
  17. Proline-Modified UIO-66 as Nanocarriers to Enhance Candida rugosa Lipase Catalytic Activity and Stability for Electrochemical Detection of Nitrofen
    Cheng Y, Lai OM, Tan CP, Panpipat W, Cheong LZ, Shen C
    ACS Appl Mater Interfaces, 2021 Jan 27;13(3):4146-4155.
    PMID: 33440928 DOI: 10.1021/acsami.0c17134
    Immobilization can be used to improve the stability of lipases and enhances lipase recovery and reusability, which increases its commercial value and industrial applications. Nevertheless, immobilization frequently causes conformational changes of the lipases, which decrease lipase catalytic activity. in the present work, we synthesized UIO-66 and grafted UIO-66 crystals with proline for immobilization of Candida rugosa lipase (CRL). As indicated by steady-state fluorescence microscopy, grafting of proline onto UIO-66 crystals induced beneficial conformational change in CRL. CRL immobilized on UIO-66/Pro (CRL@UIO-66/Pro) demonstrated higher enzyme activity and better recyclability than that immobilized on UIO-66 (CRL@UIO-66) in both hydrolysis (CRL@UIO-66/Pro: 0.34 U; CRL@UIO-66: 0.15 U) and transesterification (CRL@UIO-66/Pro: 0.93 U; CRL@UIO-66: 0.25 U) reactions. The higher values of kcat and kcat/Km of CRL@UIO-66/Pro also showed that it had better catalytic efficiency as compared to CRL@UIO-66. It is also worth noting that CRL@UIO-66/Pro (0.93 U) demonstrated a much higher transesterification activity as compared to free CRL (0.11 U), indicating that UIO-66/Pro has increased the solvent stability of CRL. Both CRL@UIO-66 and CRL@UIO-66/Pro were also used for the fabrication of biosensors for nitrofen with a wide linear range (0-100 μM), lower limit of detection, and good recovery rate.
    Matched MeSH terms: Lipase/chemistry*
  18. Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters
    Zaidan UH, Abdul Rahman MB, Othman SS, Basri M, Abdulmalek E, Rahman RN, et al.
    Biosci Biotechnol Biochem, 2011;75(8):1446-50.
    PMID: 21821960
    The utilization of natural mica as a biocatalyst support in kinetic investigations is first described in this study. The formation of lactose caprate from lactose sugar and capric acid, using free lipase (free-CRL) and lipase immobilized on nanoporous mica (NER-CRL) as a biocatalyst, was evaluated through a kinetic study. The apparent kinetic parameters, K(m) and V(max), were determined by means of the Michaelis-Menten kinetic model. The Ping-Pong Bi-Bi mechanism with single substrate inhibition was adopted as it best explains the experimental findings. The kinetic results show lower K(m) values with NER-CRL than with free-CRL, indicating the higher affinity of NER-CRL towards both substrates at the maximum reaction velocity (V(max,app)>V(max)). The kinetic parameters deduced from this model were used to simulate reaction rate data which were in close agreement with the experimental values.
    Matched MeSH terms: Lipase/metabolism*
  19. Dietary berberine regulates lipid metabolism in muscle and liver of black sea bream (Acanthopagrus schlegelii) fed normal or high-lipid diets
    Wang L, Xu B, Sagada G, Ng WK, Chen K, Zhang J, et al.
    Br J Nutr, 2021 Mar 14;125(5):481-493.
    PMID: 32718379 DOI: 10.1017/S0007114520003025
    The present study investigated the influence of berberine (BBR) supplementation in normal and high-lipid (HL) diets on lipid metabolism and accumulation in black sea bream (Acanthopagrus schlegelii). BBR was supplemented at 50 mg/kg to control (Con, 11·1 % crude lipid) and high-lipid (HL, 20·2 % crude lipid) diets and named as ConB and HLB, respectively. After the 8-week feeding trial, fish body length and specific growth rate were significantly reduced by HL diets (P < 0·05). Muscle and whole-body crude lipid contents were significantly influenced by both BBR supplementation and dietary lipid level. Fish fed the HLB diet had significantly lower serum TAG, LDL-cholesterol contents and alanine aminotransferase activity compared with the HL group. The HL group presented vast lipid accumulation in the liver, and hypertrophied hepatocytes along with large lipid droplets, and translocation of nuclear to the cell periphery. These abnormalities in black sea bream were alleviated in the HLB group. BBR supplementation in the HL diet significantly down-regulated the hepatic expression levels of acetyl-CoA carboxylase α, sterol regulatory element-binding protein-1, 6-phosphogluconate dehydrogenase, glucose 6-phosphate dehydrogenase and pparγ, whereas the lipoprotein lipase, hormone-sensitive lipase and carnitine palmitoyltransferase 1a expression levels were significantly up-regulated. However, the expression levels of these genes showed opposite trends in muscle (except for pparγ). In conclusion, dietary BBR supplementation in the HL diet reduced hepatic lipid accumulation by down-regulating lipogenesis gene expression and up-regulating lipolysis gene expression, and it increased muscle lipid contents with opposite trends of the mechanism observed in the liver.
    Matched MeSH terms: Lipase; Lipoprotein Lipase
  20. Association of glucokinase regulatory gene polymorphisms with risk and severity of non-alcoholic fatty liver disease: an interaction study with adiponutrin gene
    Tan HL, Zain SM, Mohamed R, Rampal S, Chin KF, Basu RC, et al.
    J Gastroenterol, 2014 Jun;49(6):1056-64.
    PMID: 23800943 DOI: 10.1007/s00535-013-0850-x
    BACKGROUND: Recent genome-wide association studies demonstrated an association between single nucleotide polymorphisms (SNPs) on the glucokinase regulatory gene (GCKR) with hepatic steatosis. This study attempted to investigate the association of GCKR rs780094 and rs1260326 with susceptibility to non-alcoholic fatty liver disease (NAFLD) and its severity.

    METHODS: The genotypes were assessed on 144 histologically confirmed NAFLD patients and 198 controls using a Sequenom MassARRAY platform.

    RESULTS: The GCKR rs1260326 and rs780094 allele T were associated with susceptibility to NAFLD (OR 1.49, 95 % CI 1.09-2.05, p = 0.012; and OR 1.51, 95 % CI 1.09-2.09, p = 0.013, respectively), non-alcoholic steatohepatitis (NASH) (OR 1.55, 95 % CI 1.10-2.17, p = 0.013; and OR 1.56, 95 % CI 1.10-2.20, p = 0.012, respectively) and NASH with significant fibrosis (OR 1.50, 95 % CI 1.01-2.21, p = 0.044; and OR 1.52, 95 % CI 1.03-2.26, p = 0.038, respectively). Following stratification by ethnicity, significant association was seen in Indian patients between the two SNPs and susceptibility to NAFLD (OR 2.64, 95 % CI 1.28-5.43, p = 0.009; and OR 4.35, 95 % CI 1.93-9.81, p < 0.0001, respectively). The joint effect of GCKR with adiponutrin rs738409 indicated greatly increased the risk of NAFLD (OR 4.14, 95 % CI 1.41-12.18, p = 0.010). Histological data showed significant association of GCKR rs1260326 with high steatosis grade (OR 1.76, 95 % CI 1.08-2.85, p = 0.04).

    CONCLUSION: This study suggests that risk allele T of the GCKR rs780094 and rs1260326 is associated with predisposition to NAFLD and NASH with significant fibrosis. The GCKR and PNPLA3 genes interact to result in increased susceptibility to NAFLD.

    Matched MeSH terms: Lipase/genetics*
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