Pub Date : 2019-12-30DOI: 10.15578/squalen.v14i3.414
Akhmad Awaludin Agustiar, Imas Faturrohmah, B. Sari, N. Isnaini, I. D. Puspita, T. Triyanto, A. Husni, Ustadi Ustadi
Chitin hydrolysate is one of the value added product derived from shrimp shell waste. Production of chitin hydrolysate using biological process offers an environmental friendly method compared to chemical process. Serratia marcescens PT-6, a gram negative chitinolytic bacterium isolated from shrimp pond sediment, shows good activity in hydrolyzing chitin. This study aimed to improve the chitinase activity of S. marcescens PT-6 culture by optimizing the component of chitin-containing medium (additional nitrogen source, additional carbon source, and colloidal chitin). The optimization of chitinase by S. marcescens PT-6 culture was done using one variable at a time method. The sequence of the research were to optimize 1) the type of additional carbon source (glucose, lactose, sucrose, and starch), 2) the type of additional nitrogen source (yeast extract, peptone, ammonium sulphate, and ammonium chloride), 3) the concentration of colloidal chitin (0.5; 1; 1.5; 2; and 2.5%), and 4) the concentration of the additional carbon and nitrogen source. The culture of S. marcescens PT-6 was incubated in colloidal chitin medium at 30 oC and chitinase activity from culture supernatant was analyzed. The results showed that starch gave the highest chitinase activity compare to other carbon source, meanwhile yeast extract was chosen as the best nitrogen source among others. The combination of 1.5% colloidal chitin with 0.5% starch and 0.1% yeast extract in medium increased the chitinase activity of S. marcescens PT-6 to 0.021 U/ml. These results indicated that an appropriate medium composition could increase the chitinase activity produced by S. marcescens PT-6 culture.
{"title":"Increasing Chitinase Activity of Serratia marcescens PT-6 through Optimization of Medium Composition","authors":"Akhmad Awaludin Agustiar, Imas Faturrohmah, B. Sari, N. Isnaini, I. D. Puspita, T. Triyanto, A. Husni, Ustadi Ustadi","doi":"10.15578/squalen.v14i3.414","DOIUrl":"https://doi.org/10.15578/squalen.v14i3.414","url":null,"abstract":"Chitin hydrolysate is one of the value added product derived from shrimp shell waste. Production of chitin hydrolysate using biological process offers an environmental friendly method compared to chemical process. Serratia marcescens PT-6, a gram negative chitinolytic bacterium isolated from shrimp pond sediment, shows good activity in hydrolyzing chitin. This study aimed to improve the chitinase activity of S. marcescens PT-6 culture by optimizing the component of chitin-containing medium (additional nitrogen source, additional carbon source, and colloidal chitin). The optimization of chitinase by S. marcescens PT-6 culture was done using one variable at a time method. The sequence of the research were to optimize 1) the type of additional carbon source (glucose, lactose, sucrose, and starch), 2) the type of additional nitrogen source (yeast extract, peptone, ammonium sulphate, and ammonium chloride), 3) the concentration of colloidal chitin (0.5; 1; 1.5; 2; and 2.5%), and 4) the concentration of the additional carbon and nitrogen source. The culture of S. marcescens PT-6 was incubated in colloidal chitin medium at 30 oC and chitinase activity from culture supernatant was analyzed. The results showed that starch gave the highest chitinase activity compare to other carbon source, meanwhile yeast extract was chosen as the best nitrogen source among others. The combination of 1.5% colloidal chitin with 0.5% starch and 0.1% yeast extract in medium increased the chitinase activity of S. marcescens PT-6 to 0.021 U/ml. These results indicated that an appropriate medium composition could increase the chitinase activity produced by S. marcescens PT-6 culture.","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80394041","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-12-30DOI: 10.15578/squalen.v14i3.421
Squalen Bulletin
{"title":"Back Cover Squalen Bulletin Vol. 14 No. 3 Tahun 2019","authors":"Squalen Bulletin","doi":"10.15578/squalen.v14i3.421","DOIUrl":"https://doi.org/10.15578/squalen.v14i3.421","url":null,"abstract":"","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81337664","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-12-30DOI: 10.15578/squalen.v14i3.400
N. D. Fajarningsih, Naomi Intaqta, D. Praseptiangga, C. Anam
Extraction and partial characterization of lectin from Indonesian Padina australis and Padina minor had been carried out. The crude extract of the P. australis and P. minor were examined for hemagglutination activity (HA) using native and trypsin-treated of rabbit and human A, B, O type erythrocytes. Both extracts agglutinated all of the trypsin-treated erythrocytes tested in the HA assay. Strong HA was detected in the crude extract of P. minor with trypsin-treated of human type A and O erythrocytes. However, the sugar-binding specificity study through the quantitative hemagglutination inhibition (HI) assay showed that P. minor extract could not specifically recognize the glycans tested. Apparently, the HA of the P. minor was more due to its co-extracted polyphenols content than its lectin content. On the other hand, the HI assay showed that asialo transferrin human (aTf) and asialo porcine thyroglobulin (aPTG) were the most powerful in inhibiting the HA of P. australis. Those indicated that P. australis protein extract was able to specifically recognized aTf and aPTG. The stability of P. australis and P. minor HA over various temperatures, pH ranges, and divalent cations studies showed that the P. minor HA was stable on a wide range of pH and temperature; not affected by the presence of EDTA, but decreased by Ca2+ and Mg2+ additions showed that P. minor protein extract was not a metallic protein. The HA of P. australis decreased at 60 oC and was inactivated at 90 oC; increased at strong acidic (pH 3 & 4) and strong basic (pH 9 & 10) and dependent by the presence of either EDTA or Ca2+ and Mg2+ divalent cation.
{"title":"Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor","authors":"N. D. Fajarningsih, Naomi Intaqta, D. Praseptiangga, C. Anam","doi":"10.15578/squalen.v14i3.400","DOIUrl":"https://doi.org/10.15578/squalen.v14i3.400","url":null,"abstract":"Extraction and partial characterization of lectin from Indonesian Padina australis and Padina minor had been carried out. The crude extract of the P. australis and P. minor were examined for hemagglutination activity (HA) using native and trypsin-treated of rabbit and human A, B, O type erythrocytes. Both extracts agglutinated all of the trypsin-treated erythrocytes tested in the HA assay. Strong HA was detected in the crude extract of P. minor with trypsin-treated of human type A and O erythrocytes. However, the sugar-binding specificity study through the quantitative hemagglutination inhibition (HI) assay showed that P. minor extract could not specifically recognize the glycans tested. Apparently, the HA of the P. minor was more due to its co-extracted polyphenols content than its lectin content. On the other hand, the HI assay showed that asialo transferrin human (aTf) and asialo porcine thyroglobulin (aPTG) were the most powerful in inhibiting the HA of P. australis. Those indicated that P. australis protein extract was able to specifically recognized aTf and aPTG. The stability of P. australis and P. minor HA over various temperatures, pH ranges, and divalent cations studies showed that the P. minor HA was stable on a wide range of pH and temperature; not affected by the presence of EDTA, but decreased by Ca2+ and Mg2+ additions showed that P. minor protein extract was not a metallic protein. The HA of P. australis decreased at 60 oC and was inactivated at 90 oC; increased at strong acidic (pH 3 & 4) and strong basic (pH 9 & 10) and dependent by the presence of either EDTA or Ca2+ and Mg2+ divalent cation.","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76499664","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-12-30DOI: 10.15578/squalen.v14i3.404
E. Kurniawati, B. Ibrahim, Desniar Desniar
Fish protein hydrolysate (FPH) is a derivative product of fish proteins containing smaller peptides and amino acids. FPH products have high water solubility, good emulsion capacity, and large expanding ability. With its functional properties, it allows FPH to be used as a raw material in the manufacturing of secondary microbiological reference materials. This study was intended to characterize catfish (Clarias sp.) FPH as a candidate for the matrix of microbial secondary reference. The FPH was prepared through enzymatic hydrolysis, freeze-drying and milling. The hydrolysis processes were carried out using 5% (w/w) papain, 55 °C for 5 hours, then the papain activity was stopped by increasing the temperature to 80 °C for 20 minutes.The FPH was combined with gelatine, sodium glutamate, glucose solution, and was spiked with Salmonella enteritica sv Enteritidis and freeze-dried. Results showed that catfish FPH was yellowish-white powder with a FPH yield of 11.05%. The proximate analysis of FPH revealed the moisture content of 3.77 ± 0.12%, ash content of 7.26 ± 0.03%, protein content of 86.09 ± 0.17%, and fat content of 1.38 ± 0.07%. The protein content of the FPH was greater than skim milk (33.42%). Carbohydrate levels of catfish FPH and skim milk were 1.56% and 57.46%, respectively. The best concentration of catfish FPH to perform as a microbiological reference material was 14%, obtained from highest viability of Salmonella bacteria and homogeny. The candidate for reference material were stable at storage temperatures of -20 oC.
{"title":"Potency of Catfish (Clarias sp.) Protein Hydrolysates as Candidates Matrices for Microbiology Reference Material","authors":"E. Kurniawati, B. Ibrahim, Desniar Desniar","doi":"10.15578/squalen.v14i3.404","DOIUrl":"https://doi.org/10.15578/squalen.v14i3.404","url":null,"abstract":"Fish protein hydrolysate (FPH) is a derivative product of fish proteins containing smaller peptides and amino acids. FPH products have high water solubility, good emulsion capacity, and large expanding ability. With its functional properties, it allows FPH to be used as a raw material in the manufacturing of secondary microbiological reference materials. This study was intended to characterize catfish (Clarias sp.) FPH as a candidate for the matrix of microbial secondary reference. The FPH was prepared through enzymatic hydrolysis, freeze-drying and milling. The hydrolysis processes were carried out using 5% (w/w) papain, 55 °C for 5 hours, then the papain activity was stopped by increasing the temperature to 80 °C for 20 minutes.The FPH was combined with gelatine, sodium glutamate, glucose solution, and was spiked with Salmonella enteritica sv Enteritidis and freeze-dried. Results showed that catfish FPH was yellowish-white powder with a FPH yield of 11.05%. The proximate analysis of FPH revealed the moisture content of 3.77 ± 0.12%, ash content of 7.26 ± 0.03%, protein content of 86.09 ± 0.17%, and fat content of 1.38 ± 0.07%. The protein content of the FPH was greater than skim milk (33.42%). Carbohydrate levels of catfish FPH and skim milk were 1.56% and 57.46%, respectively. The best concentration of catfish FPH to perform as a microbiological reference material was 14%, obtained from highest viability of Salmonella bacteria and homogeny. The candidate for reference material were stable at storage temperatures of -20 oC.","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89479997","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-12-28DOI: 10.15578/squalen.v14i3.422
Squalen Bulletin
{"title":"Preface Squalen Bulletin Vol. 14 No. 3 Tahun 2019","authors":"Squalen Bulletin","doi":"10.15578/squalen.v14i3.422","DOIUrl":"https://doi.org/10.15578/squalen.v14i3.422","url":null,"abstract":"","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87102361","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-12-28DOI: 10.15578/squalen.v14i3.420
Squalen Bulletin
The most rapidly expanding areas for seaweed production in the world are the tropics, including Indonesia, yet these areas are also where molecular identification of local marine flora has only been sporadically employed. Furthermore, a goal for the Government of Indonesia is to diversify the types of seaweed that are being utilized, targeting valuable products and, hand in hand, to develop aquaculture techniques for these species. Morphological methods for species identification in algae are complex or unreliable, due to simple morphologies and plasticity. Therefore, it is crucial that the correct identification is made for species and varieties of commercial interest so that growth and biochemical results can be compared and contrasted between locations, across environments and over time without taxonomic ambiguity. This guide presents entry level methodologies for sample collection, DNA preservation, DNA extraction, PCR, and analyses of DNA sequence data, as a first step in the genetic characterization of both well-known cultivated species and identification of different species with potential economic properties.
{"title":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","authors":"Squalen Bulletin","doi":"10.15578/squalen.v14i3.420","DOIUrl":"https://doi.org/10.15578/squalen.v14i3.420","url":null,"abstract":"The most rapidly expanding areas for seaweed production in the world are the tropics, including Indonesia, yet these areas are also where molecular identification of local marine flora has only been sporadically employed. Furthermore, a goal for the Government of Indonesia is to diversify the types of seaweed that are being utilized, targeting valuable products and, hand in hand, to develop aquaculture techniques for these species. Morphological methods for species identification in algae are complex or unreliable, due to simple morphologies and plasticity. Therefore, it is crucial that the correct identification is made for species and varieties of commercial interest so that growth and biochemical results can be compared and contrasted between locations, across environments and over time without taxonomic ambiguity. This guide presents entry level methodologies for sample collection, DNA preservation, DNA extraction, PCR, and analyses of DNA sequence data, as a first step in the genetic characterization of both well-known cultivated species and identification of different species with potential economic properties.","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74119646","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-08-31DOI: 10.15578/squalen.v14i2.403
Squalen Bulletin
{"title":"Preface Squalen Bulletin Vol. 14 No. 2 Tahun 2019","authors":"Squalen Bulletin","doi":"10.15578/squalen.v14i2.403","DOIUrl":"https://doi.org/10.15578/squalen.v14i2.403","url":null,"abstract":"","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-08-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74464162","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-08-30DOI: 10.15578/SQUALEN.V14I2.383
A. Poernomo, F. Ariyani, M. Murdinah
Peptones from fish waste has been widely studied, however information about its shelf life is stilllimited. This study aims to test the storability of dried peptone from tuna and shrimp waste produced through hydrolysis using alcalase enzyme. Peptone powders were packed in HDPE plastic bottles and plastic coated aluminum foil, stored at room temperature, and periodically observed in quality (moisture content, aw, color and appearance). A test was also performed on their ability to support the growth of Staphylococcus aureusbacteria; all were compared to commercial peptone (Difco). Shrimp waste peptone had the highest moisture, ash calcium contents, while tuna peptone has the highest fat content. During five month storage at ambient temperature, all peptones experienced a slight decrease in quality. Aluminum foil performed better than HDPE bottles as a packaging material for peptones, i.e., able to maintain the moisture content, water activity, and appearance. Although the ability to support bacterial growth after five months of storage was slightly affected, the tested peptones were still able to beused as bacterial growing media. It can be concluded that fish waste peptones had comparable quality and shelf-life atambient temperature to commercial peptone.
{"title":"Storage Stability of Fish Waste Peptone at Ambient Temperature","authors":"A. Poernomo, F. Ariyani, M. Murdinah","doi":"10.15578/SQUALEN.V14I2.383","DOIUrl":"https://doi.org/10.15578/SQUALEN.V14I2.383","url":null,"abstract":"Peptones from fish waste has been widely studied, however information about its shelf life is stilllimited. This study aims to test the storability of dried peptone from tuna and shrimp waste produced through hydrolysis using alcalase enzyme. Peptone powders were packed in HDPE plastic bottles and plastic coated aluminum foil, stored at room temperature, and periodically observed in quality (moisture content, aw, color and appearance). A test was also performed on their ability to support the growth of Staphylococcus aureusbacteria; all were compared to commercial peptone (Difco). Shrimp waste peptone had the highest moisture, ash calcium contents, while tuna peptone has the highest fat content. During five month storage at ambient temperature, all peptones experienced a slight decrease in quality. Aluminum foil performed better than HDPE bottles as a packaging material for peptones, i.e., able to maintain the moisture content, water activity, and appearance. Although the ability to support bacterial growth after five months of storage was slightly affected, the tested peptones were still able to beused as bacterial growing media. It can be concluded that fish waste peptones had comparable quality and shelf-life atambient temperature to commercial peptone.","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80473471","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-08-30DOI: 10.15578/SQUALEN.V14I2.394
W. A. Tanod, D. Dewanto, S. Ndobe, P. H. Riyadi, M. Putra
This study aimed to evaluate the potential antibacterial and antioxidant activities of Sinulariasp. and Sarcophyton sp. from the Palu Bay, Central Sulawesi, Indonesia. Soft corals were identified as Sinulariasp. (SC1), Sinularia sp. (SC2), andSarcophytonsp. (SC3). Antibacterial activity was examined using agar diffusion well method. Antioxidant activity was measured by the DPPH radical scavenging method. The samples were macerated in MeOH: DCM. The crude extracts were partitioned with DCM, EtOAc, and BuOH. The crude extract of Sinulariasp. (SC2) showed a very strong antibacterial activity as it was able to inhibit the growth of Staphylococcus aureusand Escherichia coliup to 10 mg/mL. Sinularia sp. (SC1) crude extract showed strong activity againstS. aureus, whereas it showed moderate against E. coli.Sarcophyton sp. (SC3) crude extract showed moderate activity against S. aureus, whereas it showed weak against E. coli. The partition fractions of the three soft coral extracts had the potential to be a potent antioxidant agent.
{"title":"Screening of Antibacterial and Antioxidant Activity from the Soft Corals Sinularia sp. and Sarcophyton sp. Origin Palu Bay, Central Sulawesi, Indonesia","authors":"W. A. Tanod, D. Dewanto, S. Ndobe, P. H. Riyadi, M. Putra","doi":"10.15578/SQUALEN.V14I2.394","DOIUrl":"https://doi.org/10.15578/SQUALEN.V14I2.394","url":null,"abstract":"This study aimed to evaluate the potential antibacterial and antioxidant activities of Sinulariasp. and Sarcophyton sp. from the Palu Bay, Central Sulawesi, Indonesia. Soft corals were identified as Sinulariasp. (SC1), Sinularia sp. (SC2), andSarcophytonsp. (SC3). Antibacterial activity was examined using agar diffusion well method. Antioxidant activity was measured by the DPPH radical scavenging method. The samples were macerated in MeOH: DCM. The crude extracts were partitioned with DCM, EtOAc, and BuOH. The crude extract of Sinulariasp. (SC2) showed a very strong antibacterial activity as it was able to inhibit the growth of Staphylococcus aureusand Escherichia coliup to 10 mg/mL. Sinularia sp. (SC1) crude extract showed strong activity againstS. aureus, whereas it showed moderate against E. coli.Sarcophyton sp. (SC3) crude extract showed moderate activity against S. aureus, whereas it showed weak against E. coli. The partition fractions of the three soft coral extracts had the potential to be a potent antioxidant agent.","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86055867","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-08-30DOI: 10.15578/squalen.v14i2.401
Squalen Bulletin
{"title":"Front Cover Squalen Bulletin Vol. 14 No. 2 Tahun 2019","authors":"Squalen Bulletin","doi":"10.15578/squalen.v14i2.401","DOIUrl":"https://doi.org/10.15578/squalen.v14i2.401","url":null,"abstract":"","PeriodicalId":21935,"journal":{"name":"Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89349489","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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