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Griselda Herman Natadiputri,Antonius Suwanto,김형권 한국응용생명화학회 2015 Applied Biological Chemistry (Appl Biol Chem) Vol.58 No.2
We investigated transesterification activity of methanol-stable lipase from Staphylococcus haemolyticus L62. Lipase L62 transesterified olive oil and menhaden oil using various alcohols including methanol, ethanol, 1-propanol, and 1-butanol. Based on the high stability of lipase L62 toward alcohols, high molar ratios (3:1 or 6:1) of alcohol to oil were employed in the reaction systems. Lipase L62 produced fatty acid esters efficiently by onestep transesterification. Reaction conditions for production of fatty acid methyl esters (FAMEs) and omega-3 fatty acid ethyl esters were further optimized. Lipase L62 produced those esters efficiently when 30–40 % water content was present in the reaction medium. The lipase L62 conversion yield was as high as 92 % for FAME and omega-3 ethyl ester production. These results indicate that lipase L62 is a suitable catalyst for producing an omega-3 ethyl ester concentrate in the pharmaceutical industry as well as for producing biodiesel in the bio-refinery industry.
( Xie Winny ),( Vivia Khosasih ),( Antonius Suwanto ),( Hyung Kwoun Kim ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.1
Two staphylococcal lipases were obtained from Staphylococcus epidermidis S2 and Staphylococcus aureus S11 isolated from sebaceous areas on the skin of the human face. The molecular mass of both enzymes was estimated to be 45 kDa by SDS-PAGE. S2 lipase displayed its highest activity in the hydrolysis of olive oil at 32oC and pH 8, whereas S11 lipase showed optimal activity at 31oC and pH 8.5. The S2 lipase showed the property of cold-adaptation, with activation energy of 6.52 kcal/mol. In contrast, S11 lipase`s activation energy, at 21 kcal/mol, was more characteristic of mesophilic lipases. S2 lipase was stable up to 45oC and within the pH range from 5 to 9, whereas S11 lipase was stable up to 50oC and from pH 6 to 10. Both enzymes had high activity against tributyrin, waste soybean oil, and fish oil. Sequence analysis of the S2 lipase gene showed an open reading frame of 2,067 bp encoding a signal peptide (35 aa), a pro-peptide (267 aa), and a mature enzyme (386 aa); the S11 lipase gene, at 2,076 bp, also encoded a signal peptide (37 aa), pro-peptide (255 aa), and mature enzyme (399 aa). The two enzymes maintained amino acid sequence identity of 98-99% with other similar staphylococcal lipases. Their microbial origins and biochemical properties may make these staphylococcal lipases isolated from facial sebaceous skin suitable for use as catalysts in the cosmetic, medicinal, food, or detergent industries.
Natadiputri, Griselda Herman,Suwanto, Antonius,Kim, Hyung Kwoun The Korean Society for Applied Biological Chemistr 2015 Applied Biological Chemistry (Appl Biol Chem) Vol.58 No.2
We investigated transesterification activity of methanol-stable lipase from Staphylococcus haemolyticus L62. Lipase L62 transesterified olive oil and menhaden oil using various alcohols including methanol, ethanol, 1-propanol, and 1-butanol. Based on the high stability of lipase L62 toward alcohols, high molar ratios (3:1 or 6:1) of alcohol to oil were employed in the reaction systems. Lipase L62 produced fatty acid esters efficiently by one-step transesterification. Reaction conditions for production of fatty acid methyl esters (FAMEs) and omega-3 fatty acid ethyl esters were further optimized. Lipase L62 produced those esters efficiently when 30-40 % water content was present in the reaction medium. The lipase L62 conversion yield was as high as 92 % for FAME and omega-3 ethyl ester production. These results indicate that lipase L62 is a suitable catalyst for producing an omega-3 ethyl ester concentrate in the pharmaceutical industry as well as for producing biodiesel in the bio-refinery industry.
Dominant Enterobacteriaceae in tempeh were primarily originated from soybean
Horizon M. Ilham,Michael Wijaya,Antonius Suwanto,Iman Rusmana 한국식품과학회 2021 Food Science and Biotechnology Vol.30 No.6
During tempeh production, boiling was consideredas heat treatment that could significantly reduce oreliminate bacterial population in soybean before fungalinoculation. The objective of this study was to enumerateand trace Enterobacteriaceae communities in pre-boilingsoybean, post-boiling soybean, and fresh tempeh designatedas RTI and EMP. Standard plate count and qRT-PCRwere employed to determine the culturable and non-culturablebacteria, while Enterobacterial Repetitive IntragenicConsensus PCR was conducted to determine theintraspecies genomic variations. Fresh tempeh from bothRTI and EMP contained approximately 107 and 108 CFU/gof Enterobacteriaceae respectively. The number of bacteriain pre-boiling soybean were 10,000 times lower than infresh tempeh. Our study showed that most Enterobacteriaceaewere severely injured or quiescent during boilingprocess and quickly recovered up to 109 CFU/g in freshtempeh. Some Klebsiella isolates found in tempeh weregenetically identical to isolates in soybean, but differentfrom those of medical isolates. This study suggested thatsoybean could be the main origin of Klebsiella in freshtempeh.
( Ludwinardo Putra ),( Griselda Herman Natadiputri ),( Anja Meryandini ),( Antonius Suwanto ) 한국미생물생명공학회(구 한국산업미생물학회) 2019 Journal of microbiology and biotechnology Vol.29 No.6
Lipases are industrial enzymes that catalyze both triglyceride hydrolysis and ester synthesis. The overexpression of lipase genes is considered one of the best approaches to increase the enzymatic production for industrial applications. Subfamily I.2. lipases require a chaperone or foldase in order to become a fully-activated enzyme. The goal of this research was to isolate, clone, and co-express genes that encode lipase and foldase from Burkholderia territorii GP3, a lipolytic bacterial isolate obtained from Mount Papandayan soil via growth on Soil Extract Rhodamine Agar. Genes that encode for lipase (lipBT) and foldase (lifBT) were successfully cloned from this isolate and co-expressed in the E. coli BL21 background. The highest expression was shown in E. coli BL21 (DE3) pLysS, using pET15b expression vector. LipBT was particulary unique as it showed highest activity with optimum temperature of 80°C at pH 11.0. The optimum substrate for enzyme activity was C10, which is highly stable in methanol solvent. The enzyme was strongly activated by Ca<sup>2+</sup>, Mg<sup>2+</sup>, and strongly inhibited by Fe<sup>2+</sup> and Zn<sup>2+</sup>. In addition, the enzyme was stable and compatible in non-ionic surfactant, and was strongly incompatible in ionic surfactant.
Isolation and Biochemical Characterization of Bacillus pumilus Lipases from the Antarctic
( Arifin arild Ranlym ),( Soon Ja Kim ),( Joung Han Yim ),( Antonius Suwanto ),( Hyung Kwoun Kim ) 한국미생물 · 생명공학회 2013 Journal of microbiology and biotechnology Vol.23 No.5
Lipase-producing bacterial strains were isolated from Antarctic soil samples using the tricaprylin agar plate method. Seven strains with relatively strong lipase activities were selected. All of them turned out to be Bacillus pumilus strains by the 16S rRNA gene sequence analysis. Their corresponding lipase genes were cloned, sequenced, and compared. Finally, three different Bacillus pumilus lipases (BPL1, BPL2, and BPL3) were chosen. Their amino acid sequence identities were in the range of 92-98% with the previous Bacillus pumilus lipases. Their optimum temperatures and pHs were measured to be 40oC and pH 9. Lipase BPL1 and lipase BPL2 were stable up to 30oC, whereas lipase BPL3 was stable up to 20oC. Lipase BPL2 was stable within a pH range of 6-10, whereas lipase BPL1 and lipase BPL3 were stable within a pH range of 5-11, showing strong alkaline tolerance. All these lipases exhibited high hydrolytic activity toward pnitrophenyl caprylate (C8). In addition, lipase BPL1 showed high hydrolytic activity toward tributyrin, whereas lipase BPL2 and lipase BPL3 hydrolyzed tricaprylin and castor oil preferentially. These results demonstrated that the three Antarctic Bacillus lipases were alkaliphilic and had a substrate preference toward short- and mediumchain triglycerides. These Antarctic Bacillus lipases might be used in detergent and food industries.
Mohamed Sahrul Tamzil,Yuzer Alfiko,Andhika Faisal Mubarok,Sigit Purwantomo,Suwanto Antonius,Budiarti Sri 한국생물공학회 2021 Biotechnology and Bioprocess Engineering Vol.26 No.4
Explant contamination due to Agrobacterium overgrowth after the co-cultivation stage is a common problem in Agrobacterium-mediated plant transformation. In order to overcome this issue, this research undertook another approach by generating auxotrophic Agrobacterium tumefaciens AGL1 mutants to a specific amino acid by mini Tn5 transposon carrying spectinomycin resistance gene (spcR), and a total of 3315 AGL1 mutants were successfully constructed. Further screening identified 20 putative auxotrophs, and subsequently produced three mutants carried auxotroph properties to one specific amino acid. These mutants were AP5-2-51 threonine auxotroph, AP5- 5-2 cysteine auxotroph, and AP5-7-27 tryptophan auxotroph. The mini Tn5 insertion position in the Agrobacterium genome showed that the insertion position of AP5-2-51 mutants was in the thrB gene (AAK86584.1; locus tag At1D132_04580), while the other two mutants were unable to be identified by TAIL-PCR technique. The effectiveness of these three mutants to transfer T-DNA (pCAMBIA1300- eGFP-hpt) was examined on fresh Nipponbare rice callus explants with AGL1 as control. Results showed that transformation efficiency of the three mutants was not significantly different from AGL1 (Tukey HSD, α = 0.05). The percentages of Agrobacterium overgrowth in control and samples (three mutants) were also measured. Interestingly, the AP5-2-51 mutant indicated the highest ability to prevent overgrowth by reducing Agrobacterium growth to 1.11%, while the other two mutants suppressed the overgrowth to 15.56% (AP5-5-2) and 12.22% (AP5-7-27).