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1.
Aran H-Kittikun Poonsuk Prasertsan Wolfgang Zimmermann Phisit Seesuriyachan Thanongsak Chaiyaso 《Applied biochemistry and biotechnology》2012,166(8):1969-1982
The extracellular lipase from Streptomyces thermocarboxydus ME168 was purified to 9.5-fold with 20% yield, following concentration by acetone precipitation, ion exchange chromatography
(Resource Q) and gel filtration chromatography (Superdex 200), respectively. The purified enzyme had an apparent molecular
mass of 21 kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The N-terminal sequence of the lipase
was ASDFDDQILG and was different from most other reported lipase. The enzyme showed maximum activity at 50 °C with the half-life
of 180 min at 65 °C. It showed high stability at a broad pH range of 5.5–9.5 and was thermostable at the temperature range
of 25–60 °C. The K
m
and V
max were 0.28 mM and 1,428 U/mg, respectively, using p-nitrophenyl palmitate as substrate. It was active toward p-nitrophenyl ester with medium to long acyl chain (C8–C16). Lipase activity was inhibited by Zn2+, dithiothreitol (DTT), EDTA and some organic solvents, e.g., ethanol, acetone, dioxane, acetronitrile, tert-butanol and pyridine. Immobilized crude lipase of S. thermocarboxydus ME168 on celite could be used to synthesize sugar esters from glucose and vinyl acetate, vinyl butyrate or vinyl caproate
in tert-butanol:pyridine (55:45 v/v) at 45 °C with conversion yields of 93, 67 and 55%, respectively. 相似文献
2.
Purification and partial characterization of a lipase from Bacillus coagulans ZJU318 总被引:1,自引:0,他引:1
An extracellular lipase was purified from the fermentation broth of Bacillus coagulans ZJU318 by CM-Sepharose chromatography, followed by Sephacryl S-200 chromatography. The lipase was purified 14.7-fold with
18% recovery and a specific activity of 141.1 U/mg. The molecular weight of the homogeneous enzyme was (32 kDa), determined
by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The enzyme activity was maximum at pH 9.0 and was stable
over a pH range of 7.0–10.0, and the optimum temperature for the enzyme reaction was 45°C. Little activity loss (6.2%) was
observed after 1 h of incubation at 40°C. However, the stability of the lipase decreased sharply at 50 and 60°C. The enzyme
activity was strongly inhibited by Ag+ and Cu2+, whereas EDTA caused no inhibition. SDS, Brij 30, and Tween-80 inhibited lipase, whereas Triton X-100 did not significantly
inhibit lipase activity. 相似文献
3.
An extracellular lipase secreted by Pseudomonas aeruginosa CS-2 was purified to homogeneity about 25.5-fold with an overall yield of 45.5%. The molecular mass of the lipase was estimated
to be 33.9 kDa by SDS-PAGE and 36 kDa by gel filtration. The optimum temperature and pH were 50 °C and 8.0. The lipase was
found to be stable at pH 4–10 and below 50 °C. Its hydrolytic activity was highest against p-nitrophenyl palmitate (p-NPP) among p-nitrophenyl esters of fatty acids with various chain lengths. The lipase was activated in the presence of Ca2+, while it was inactivated by other metal ions more or less. EDTA significantly reduced the lipase activity, indicating the
lipase was a metalloenzyme. Gum Arabic and polyvinyl alcohol 124 enhanced lipase activity but Tween-20, Tween-80, and hexadecyltrimethyl
ammonium bromide strongly inhibited the lipase. It exhibited stability in some organic solvents. The lipase was activated
in the presence of acetonitrile. Conversely, it was drastically inactivated by methanol and ethanol. 相似文献
4.
Characterization of Thermo-stable Endoinulinase from a New Strain <Emphasis Type="Italic">Bacillus Smithii</Emphasis> T7 总被引:1,自引:0,他引:1
A new thermophilic inulinase-producing strain, which grows optimally at 60 °C, was isolated from soil samples with medium
containing inulin as a sole carbon source. It was identified as a Bacillus smithii by analysis of 16s rDNA. Maximum inulinase yield of 135.2 IU/ml was achieved with medium pH7.0, containing inulin 2.0%, (NH4)H2PO4 0.5%, yeast extract 0.5%, at 50 °C 200 rpm shaker for 72-h incubation. The purified inulinase from the extracellular extract
of B. smithii T7 shows endoinulinolytic activity. The optimum pH for this endoinulinase is 4.5 and stable at pH range of 4.0–8.0. The optimum
temperature for enzyme activity was 70 °C, the half life of the endoinulinase is 9 h and 2.5 h at 70 °C and 80 °C respectively.
Comparatively lower Michaelis–Menten constant (4.17 mM) and higher maximum reaction velocity (833 IU/mg protein) demonstrate
the endoinulinase’s greater affinity for inulin substrate. These findings are significant for its potential industrial application. 相似文献
5.
A bacterial strain isolated from spoiled coconut and identified as Bacillus cereus was found capable of producing alkaline thermostable extracellular lipase. Optimum temperature, time, and pH for enzyme substrate
reaction were found to be 60 °C, 10 min, and 8.0 respectively. Common surfactants except Triton X 100 and cetyltrimethylammonium
bromide have no or very little inhibitory effects on enzyme activity. The enzyme was found to be stable in presence of oxidizing
agents and protease enzyme. The maximum lipase production was achieved at 30–33 °C, pH 8.0 on 24 h of fermentation using 50 ml
medium in a 250-ml Erlenmeyer flask. The superior carbon and nitrogen sources for lipase production were starch (2%) and ammonium
sulfate (nitrogen level 21.2 mg/100 ml), peptone (nitrogen level 297 mg/100 ml), and urea (nitrogen level 46.62 mg/100 ml)
in combination, respectively. The maximum enzyme activity obtained was 33 ± 0.567 IU/ml. 相似文献
6.
Taibi Z Saoudi B Boudelaa M Trigui H Belghith H Gargouri A Ladjama A 《Applied biochemistry and biotechnology》2012,166(3):663-679
An extracellular thermostable xylanase from a newly isolated thermophilic Actinomadura sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption–ionization time-of-flight mass
spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 Da. The 19 residue N-terminal sequence
of the enzyme showed 84% homology with those of actinomycete endoxylanases. The optimum pH and temperature values for xylanase
activity were pH 10 and 80 °C, respectively. This xylanase was stable within a pH range of 5–10 and up to a temperature of
90 °C. It showed high thermostability at 60 °C for 5 days and half-life times at 90 °C and 100 °C were 2 and 1 h, respectively.
The xylanase was specific for xylans, showing higher specific activity on soluble oat-spelt xylan followed by beechwood xylan.
This enzyme obeyed the Michaelis–Menten kinetics, with the K
m and k
cat values being 1.55 mg soluble oat-spelt xylan/ml and 388 min−1, respectively. While the xylanase from Actinomadura sp. Cpt20 was activated by Mn2+, Ca2+, and Cu2+, it was, strongly inhibited by Hg2+, Zn2+, and Ba2+. These properties make this enzyme a potential candidate for future use in biotechnological applications particularly in
the pulp and paper industry. 相似文献
7.
Chitinase was purified from the culture medium of Bacillus licheniformis SK-1 by colloidal chitin affinity adsorption followed by diethylamino ethanol-cellulose column chromatography. The purified
enzyme showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular size and pI of chitinase 72 (Chi72) were 72 kDa and 4.62 (Chi72) kDa, respectively. The purified chitinase revealed two activity optima
at pH 6 and 8 when colloidal chitin was used as substrate. The enzyme exhibited activity in broad temperature range, from
40 to 70°C, with optimum at 55°C. It was stable for 2 h at temperatures below 60°C and stable over a broad pH range of 4.0–9.0
for 24 h. The apparent K
m and V
max of Chi72 for colloidal chitin were 0.23 mg ml−1 and 7.03 U/mg, respectively. The chitinase activity was high on colloidal chitin, regenerated chitin, partially N-acetylated chitin, and chitosan. N-bromosuccinamide completely inhibited the enzyme activity. This enzyme should be a good candidate for applications in the
recycling of chitin waste. 相似文献
8.
Lokendra Kumar Balvinder Singh Dilip Kumar Adhikari Joydeep Mukherjee Debashish Ghosh 《Applied biochemistry and biotechnology》2012,166(7):1723-1735
Purification and characterization of halotolerant, thermostable alkaline l-glutaminase from a Bacillus sp. LKG-01 (MTCC 10401), isolated from Gangotri region of Uttarakhand Himalaya, is being reported in this paper. Enzyme has
been purified 49-fold from cell-free extract with 25% recovery (specific activity 584.2 U/mg protein) by (NH4)2SO4 precipitation followed by anion exchange chromatography and gel filtration. Enzyme has a molecular weight of 66 kDa. l-Glutaminase is most active at pH 11.0 and stable in the pH range 8.0–11.0. Temperature optimum is 70 °C and is completely
stable after 3 h pre-incubation at 50 °C. Enzyme reflects more enhanced activity with 1–20% (w/v) NaCl, which is further reduced to 80% when NaCl concentration was increased up to 25%. l-Glutaminase is almost active with K+, Zn2+, and Ni2+ ions and K
m and V
max values of 240 μM and 277.77 ± 1.1 U/mg proteins, respectively. Higher specific activity, purification fold, better halo-tolerance,
and thermostability would make this enzyme more attractive for food fermentation with respect to other soil microbe derived
l-glutaminase reported so far. 相似文献
9.
Qi Wu Chen Li Chenglei Li Hui Chen Liu Shuliang 《Applied biochemistry and biotechnology》2010,160(1):129-139
The collagenase, produced extracellular by Bacillus pumilus Col-J, was purified by ammonium sulfate precipitation followed by two gel filtrations, involving Sephadex G-100 column and
Sepharose Fast Flow column. Purified collagenase has a 31.53-fold increase in specific activity of 87.33 U/mg and 7.00% recovery.
The collagenase has a relative molecular weight of 58.64 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
The optimal temperature for the enzyme reaction was 45 °C. More than 50% of the original activity still remained after 5 min
of incubation at 70 °C or 10 min at 60 °C. The maximal enzyme activity of collagenase was obtained at pH 7.5, and it was stable
over a pH range of 6.5–8.0. The collagenase activity was strongly inhibited by Mn2+, Pb2+, ethylenediamine tetraacetic acid, ethylene glycol tetraacetic acid, and β-mercaptoethanol. However, Ca2+ and Mg2+ greatly increased its activity. The collagenase from B. pumilus Col-J showed highly specific activity towards the native collagen from calf skin. The K
m and V
max of the enzyme for collagen were 0.79 mg/mL and 129.5 U, respectively. 相似文献
10.
Mervat Morsy A. El-Gendy 《Applied biochemistry and biotechnology》2010,162(3):780-794
Among all endophytic keratinolytic fungal isolates recovered from marine soft coral Dendronephthya hemprichii, Penicillium spp. Morsy1 was selected as the hyperactive keratinolytic strain under solid substrate fermentation of different agriculture
and poultry wastes. The optimization of extraction process, physicochemical parameters affecting the keratinase production
in solid-state fermentation, and the purified keratinase parameters were studied. Maximum keratinase activity (1,600 U g−1, initial dry substrate) was recovered from moldy bran with 0.1% Tween 80. The optimized production conditions were rice straw
as carbon source, pH of medium 6, growth temperature 26 °C, initial moisture content of 80% (v/w), inoculum size of 105 spores ml−1, and an average particle size of the substrate 0.6 mm (3,560 U g−1, initial dry substrate after 5 days of fermentation). Two types of keratinase (Ahm1 and Ahm2) were purified from the culture
supernatant through ammonium sulfate precipitation, DEAE-Sepharose, and gel filtration chromatography. Enzyme molecular weights
were 19 kDa (Ahm1) and 40 kDa (Ahm2). The kinetic parameters of purified keratinases were optimized for the hydrolysis of
azokeratin by Ahm1 (pH 7.0–8.0, stable in pH range of 6.0 to 8.0 at 50 °C) and Ahm2 enzymes (pH 10.0–11.0, stable in pH range
of 6.0 to 11.0 at 60–65 °C). Whereas inhibitors of serine (phenylmethylsulfonyl fluoride) and cysteine (iodoacetamide) proteases
had minor effects on both Ahm1 and Ahm2 activity, both keratinases were strongly inhibited by chelating agents EDTA and EGTA.
These findings suggest that serine and cysteine residues are not involved in the catalytic mechanisms, and they are metalloproteases. 相似文献
11.
Purification,Properties, and Application of a Novel Acid Urease from <Emphasis Type="Italic">Enterobacter</Emphasis> sp. 总被引:1,自引:0,他引:1
It has been demonstrated that acid urease is capable of decomposing urea in fermented beverage and foods. As urea is a precursor
of ethylcarbamate, a potential carcinogenic compound, measures must be taken to control the level of urea. We herein describe
the purification and characterization of a novel acid urease from Enterobacter sp. R-SYB082 and its application to the removal of urea in Chinese rice wine. The enzyme was purified to electrophoretic
homogeneity using ethanol precipitation, Superdex 200 and Mono Q with a fold purification of 21.1 and a recovery of 49%. The
molecular weight of the enzyme was 430,000 Da by gel filtration and 72,000 Da by sodium dodecyl sulfate polyacrylamide gel
electrophoresis, suggesting that it was a hexamer. The activity of this purified enzyme was optimal at pH 4.5 and 35 °C. The
temperature stability was under 55 °C, and the pH stability was 4.0~5.0. The enzyme exhibited an apparent K
m of 19.5 μmol/l and a V
max of 109 μmol urea/mg·min at 35 °C and pH 4.5. When incubating two different kinds of Chinese rice wine with the enzyme (0.08 U/ml)
at 35 °C for 7 days, over 85% of urea was decomposed, and at 20 °C, above 78% was removed. The result showed that the enzyme
is applicable to elimination of urea in Chinese rice wine. 相似文献
12.
Melda Altikatoglu Yeliz Basaran Candan Arioz Ayse Ogan Huriye Kuzu 《Applied biochemistry and biotechnology》2010,160(8):2187-2197
Multipoint covalent bonding of glucose oxidase (EC 1.1.3.4) to hydrophilic natural polymer dextran and optimization of procedures
to obtain, with enhanced temperature and pH stabilities, were studied. Purified enzyme was conjugated with various molecular
weight dextrans (17.5, 75, and188 kD) in a ratio of 20:1, 10:1, 1:1, 1:5, 1:10, 1:15, and 1:20. After 1 h of incubation at
pH 7, the activities of purified enzyme and conjugates were determined at different temperatures (25°C, 30°C, 35°C, 40°C,
50°C, 60°C, 70°C, and 80°C), and the results were evaluated for thermal resistance. Increases in temperature from 25°C to
50°C did not change the activities of the conjugates. The conjugate, which was prepared with 75 kDa dextran in a molar ratio
of 1:5, showed the highest thermal resistance and even the activity still remains at 80°C at pH 7.0. This conjugate also displayed
activity in a wide pH range (pH 4.0–7.0) at high temperatures. Conjugate, which was synthesized with 75 kDa dextran in a molar
ratio of 1:5, appears to be feasible and useful for biotechnological applications. 相似文献
13.
Shivakumar S Jagadish SJ Zatakia H Dutta J 《Applied biochemistry and biotechnology》2011,164(8):1225-1236
A fungal isolate, identified as Penicillium citrinum S2, produced ≈1 U/mL of PHB depolymerase by 72 h when grown in BHM containing 0.2%, w/v PHB, pH 6.0 at 30 °C. Partial purification of an extracellular poly(-β-)hydroxybutyrate (PHB) depolymerase PhaZ
Pen
from P. citrinum S2 by two steps using ammonium sulphate (80% saturation) and affinity chromatography using concanavalin A yielded 16.18-fold
purity and 21.53% recovery of protein. The enzyme was composed of three polypeptide chains of 66, 43 and 20 kDa, respectively,
as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. All the three bands stained positive for glycoprotein
by PAS staining. Optimum enzyme activity was detected at pH 6.0 and 50 °C. The enzyme was stable between pH 4.0 and 7.0 at
50 °C, 2 h. β-hydroxybutyrate monomer was detected as the major end product of PHB hydrolysis. The enzyme also showed distinct
behaviour towards different inhibitors tested, which suggests the role of serine, serine residue, carboxyl group, tyrosine
and sulfhydryl groups in its active site. 相似文献
14.
Maalej I Belhaj I Masmoudi NF Belghith H 《Applied biochemistry and biotechnology》2009,158(1):200-212
A thermostable xylanase from a newly isolated thermophilic fungus Talaromyces thermophilus was purified and characterized. The enzyme was purified to homogeneity by ammonium sulfate precipitation, diethylaminoethyl
cellulose anion exchange chromatography, P-100 gel filtration, and Mono Q chromatography with a 23-fold increase in specific
activity and 17.5% recovery. The molecular weight of the xylanase was estimated to be 25kDa by sodium dodecyl sulfate–polyacrylamide
gel electrophoresis and gel filtration. The enzyme was highly active over a wide range of pH from 4.0 to 10.0. The relative
activities at pH5.0, 9.0, and 10.0 were about 80%, 85.0%, and 60% of that at pH7.5, respectively. The optimum temperature
of the purified enzyme was 75°C. The enzyme showed high thermal stability at 50°C (7days) and the half-life of the xylanase
at 100°C was 60min. The enzyme was free from cellulase activity. K
m and V
max values at 50°C of the purified enzyme for birchwood xylan were 22.51mg/ml and 1.235μmol min−1 mg−1, respectively. The enzyme was activated by Ag+, Co2+, and Cu2+; on the other hand, Hg2+, Ba2+, and Mn2+ inhibited the enzyme. The present study is among the first works to examine and describe a secreted, cellulase-free, and
highly thermostable xylanase from the T. thermophilus fungus whose application as a pre-bleaching aid is of apparent importance for pulp and paper industries. 相似文献
15.
16.
Summary An extracellular lipase was produced by Bacillus coagulans by solid-state fermentation. Solid waste from melon was used as the basic nutrient source and was supplemented with olive
oil. The highest lipase production (78,069 U/g) was achieved after 24h of cultivation with 1% olive oil enrichment. Enzyme
had an optimal activity at 37°C and pH 7.0, and sodium dodecyl sulfate increased lipase activity. NH 4NO3 increased enzyme production, whereas organic nitrogen had no effect. The effect of the type of carbon sources on lipolytic
enzyme production was also studied. The best results were obtained with starch and maltose (148,932 and 141,629 U/g, respectively),
whereas a rather low enzyme activity was found in cultures grown on glucose and galactose (approx 118,769 and 123,622 U/g,
respectively). Enzyme was inhibited with Mn+2 and Ni+2 by 68 and 74%, respectively. By contrast, Ca+2 enhanced enzyme production by 5%. 相似文献
17.
Sawitree Dueramae Preeyanuch Bovornreungroj Toshiki Enomoto Duangporn Kantachote 《Chemical Papers》2017,71(10):1975-1984
A halotolerant Virgibacillus alimentarius LBU20907 isolated from fermented fish (Budu) was found to be an efficient producer of extracellular halophilic lipase enzyme. The enzyme was purified 5.99-fold with a 0.15% final yield to homogeneity by ammonium sulfate precipitation, followed by dialysis, Toyopearl DEAE-650 M ion exchange chromatography, Toyopearl butyl-650 M hydrophobic interaction chromatography, and Toyopearl-HW 55 F gel filtration chromatography. SDS-PAGE of purified lipase exhibited a homogenous single band with a very high molecular weight of 100 kDa. The properties of purified lipase revealed maximum activity at pH 7.0 and 40 °C. It was also highly stable in a pH range of 6.0–7.0, retaining more than 90% activity for 24 h. It was stable at the temperature of 30–50 °C and maintained more than 80% activity for 16 h. The purified lipase performing the maximal activity in the presence of 20.0% NaCl indicated halophilic enzyme properties. Its lipolytic activity was highest against p-nitrophenyl palmitate. The lipase activity was found to be enhanced in hexane. The enzyme activity was stimulated in the presence of Zn2+, Ca2+, Mg2+, and Sr2+; while, it was completely inhibited by Ba2+ and Co2+. The enzyme had a K m and V max of 108.0 mg and 79.1 U mL?1, respectively. 相似文献
18.
S. Shanmughapriya G. Seghal Kiran Joseph Selvin T. Anto Thomas C. Rani 《Applied biochemistry and biotechnology》2010,162(3):625-640
Marinobacter sp. (MSI032) isolated from the marine sponge Dendrilla nigra was optimized for the production of extracellular cellulolytic enzyme (CMCase) by submerged fermentation. Initial experiments
showed that the culture medium containing 1% maltose as carbon source and 1% peptone and casein as nitrogen source supported
maximal enzyme production at 27 °C and at a pH of 9.0. Further optimization carried out showed the maximal enzyme production
was supported by the presence of 2% NaCl and 10 mM Zn2+ ions in the production media. The production of enzyme cellulase occurred at 48 h of incubation which proved the importance
of this strain for cellulase production in large scale. Further, the enzyme was purified to 12.5-fold with a 37% yield and
a specific activity of 2,548.75 U/mg. The purified enzyme displayed maximum activity at mesophilic temperature (27–35 °C)
and at a broad pH range with optimal activity at pH 9.0. The purified enzyme was stable even at a higher alkaline pH of 12.0
which is greater than the pH stability that has not been reported in any of the cellulolytic isolates studied so far. Thus,
from the present study, it is crucial that, instead of exploring the thermophilic resource that is limited in natural environments,
the mesophilic bacteria that occurs commonly in nature can be added up to the database of cellulolytic bacteria. Thus, it
is possible that a wide diversity of mesophilic bacteria associated with marine sponges opens up a new doorstep for the degradation
of cellulosic waste material for the production of liquid fuels. This is the first report elucidating the prospects of sponge-associated
marine bacterium for the production of extracellular alkaline cellulase. 相似文献
19.
Dengeti Shrinivas Gunashekaran Savitha Kumar Raviranjan Gajanan Ramchandra Naik 《Applied biochemistry and biotechnology》2010,162(7):2049-2057
A highly thermostable alkaline xylanase was purified to homogeneity from culture supernatant of Bacillus sp. JB 99 using DEAE-Sepharose and Sephadex G-100 gel filtration with 25.7-fold increase in activity and 43.5% recovery.
The molecular weight of the purified xylanase was found to be 20 kDA by SDS-PAGE and zymogram analysis. The enzyme was optimally
active at 70 °C, pH 8.0 and stable over pH range of 6.0–10.0.The relative activity at 9.0 and 10.0 were 90% and 85% of that
of pH 8.0, respectively. The enzyme showed high thermal stability at 60 °C with 95% of its activity after 5 h. The K
m and V
max of enzyme for oat spelt xylan were 4.8 mg/ml and 218.6 μM min−1 mg−1, respectively. Analysis of N-terminal amino acid sequence revealed that the xylanase belongs to glycosyl hydrolase family
11 from thermoalkalophilic Bacillus sp. with basic pI. Substrate specificity showed a high activity on xylan-containing substrate and cellulase-free nature. The hydrolyzed product
pattern of oat spelt xylan on thin-layer chromatography suggested xylanase as an endoxylanase. Due to these properties, xylanase
from Bacillus sp. JB 99 was found to be highly compatible for paper and pulp industry. 相似文献
20.
Xiao Yan Wu Sanna JÄÄskelÄinen Wu-Yen Linko 《Applied biochemistry and biotechnology》1996,59(2):145-158
A commercialRhizomucor miehei lipase was purified by ammonium sulfate precipitation. Phenyl Sepharose 6 Fast Row hydrophobic interaction chromatography,
and DEAE Sepharose Fast Flow anion-exchange chromatography. The recovery of lipase activity was 32% with a 42-fold purification.
The molecular size of the purified enzyme was 31,600 Dalton and the pI 3.8. The enzyme was stable for at least 24 h within
a pH range of 7.0-10.0, and 96.8% of the enzyme activity remained when kept at 30‡C for 24 h. Further, about 10–30% of the
lipase activity was inhibited by K+, Li+, Ni+, Co2+, Zn2+, Mg2+, Sn2+, Cu2+, Ba2+, Ca2+, and Fe2+ ions and by SDS, but EDTA had no effect. Under the experimental conditions, the optimum temperature for the hydrolysis of
olive oil was 50‡C (pH 8.0), and for the synthesis of 1-butyl oleate, 37‡C. It was concluded that hydrolytic activity of lipase
alone is not a sufficient criterion for its synthetic potential. The optimal molar ratio of oleic acid and 1-butanol was 2:1
for 1-butyl oleate synthesis. The 1-butyl oleate yield was unaffected by purification of the enzyme after 12 h. 相似文献