scholarly journals ANALISIS HASIL FRAKSINASI PROTEASE DAN LIPASE YANG BERASAL DARI SALURAN PENCERNAAN UDANG VANAME (Litopenaeus vannamei)

2020 ◽  
Vol 7 (2) ◽  
pp. 194-202
Author(s):  
Hanifah Rahmi ◽  
. Hariyanti ◽  
Rina Putri Ariyanti ◽  
Devi Wulandari
Keyword(s):  
Digestive Tract ◽  
Lipase Activity ◽  
Litopenaeus Vannamei ◽  
Digestive Enzymes ◽  
Gel Filtration ◽  
Lipolytic Enzyme ◽  
Gel Filtration Chromatography ◽  
Sulfate Salt ◽  
High Consumption ◽  
Volume Retention

Analysis of Protease and Lipase Fractionation Originated from the Digestive Tract of Vannamei Shrimp (Litopenaeus vannamei) Vannamei shrimp is a fishery commodity with a high consumption value, so it has an impact of high shrimp waste in the form of head and skin. The digestive tract connected to the head of the vaname shrimp (Litopenaeus vannamei) contains digestive enzymes, including proteases and lipases. This study aims to obtain the protein fraction that has the highest protease and lipase activity. The separation method used was centrifugation followed by precipitation using ammonium sulfate salt and dialysis. The dialysate was purified by gel filtration chromatography at a volume retention of 10 drops per tube. The proteolytic and lipolytic enzyme activity of the fraction was measured using a spectrophotometer. The results showed that fraction 102 had the highest protease activity value of 96.3924 U / mL, while fraction 100 had the highest lipase activity of 531.07 U / mL. This study showed that in the digestive tract of vaname shrimp, protease and lipase activity increased with the level of purity.  Keywords: digestive enzymes, gel filtration chromatography, lipase, protease, vannamei shrimp ABSTRAK Udang vaname merupakan komoditi perikanan dengan nilai konsumsi yang tinggi, sehingga berdampak pula dengan tingginya limbah udang yang berupa kepala dan kulit. Saluran pencernaan yang terhubung dengan kepala udang vaname (Litopenaeus vannamei) mengandung enzim pencernaan, diantaranya protease dan lipase. Penelitian ini bertujuan untuk mendapatkan fraksi protein yang memiliki aktivitas protease dan lipase tertinggi. Metode pemisahan yang dilakukan adalah sentrifugasi dilanjutkan dengan pengendapan menggunakan garam ammonium sulfat dan dialisis. Dialisat dimurnikan dengan kromatografi filtrasi gel pada retensi volume sebanyak 10 tetes tiap tabung. Aktivitas enzim proteolitik dan lipolitik fraksi diukur menggunakan spektrofotometer. Hasil menunjukkan bahwa fraksi 102 memiliki nilai aktivitas protease tertinggi sebesar 96,3924 U mL–1, sedangkan fraksi 100 memiliki aktivitas lipase tertinggi sebesar 531,07 U mL–1. Penelitian ini menunjukkan bahwa pada saluran pencernaan udang vaname terdapat aktivitas protease dan lipase yang meningkat seiring dengan tingkat kemurniannya.

scholarly journals Identification of amylase activity from vannamei shrimps’ (Litopenaeus vannamei) digestive tract using size exclusion chromatography method

2021 ◽  
Vol 21 (3) ◽  
pp. 123-127
Author(s):  
HARIYANTI HARIYANTI ◽  
HANIFAH RAHMI
Keyword(s):  
Protein Content ◽  
Digestive Tract ◽  
Size Exclusion Chromatography ◽  
Litopenaeus Vannamei ◽  
Amylase Activity ◽  
Gel Filtration ◽  
Size Exclusion ◽  
Font Size ◽  
Chromatography Method ◽  
Exclusion Chromatography

Vannamei shrimps (Litopenaeus vannamei), also known as white leg shrimps are widely cultivated and consumed by many people. However, most consumers have removed the shrimp’s head which integrates with its digestive tract. The digestive tract of white leg shrimp contains digestive enzymes, including amylase. This study aimed to determine the protein content and amylase activity from Vannamei shrimps’ digestive tract using the size exclusion chromatography method. The protein isolation of size exclusion chromatography was prepared in three steps, namely; centrifugation, precipitation, and dialysis. The protein from the dialysis step was purified by using gel filtration chromatography. Each obtained fraction was determined the protein content and amylase activity by using spectrophotometer UV-Vis method. The results showed that the fraction of 108th had the highest protein content and amylase activity with a value of 0.85 mg/ml and 25.66U/ml respectively. @font-face {font-family:"Cambria Math"; panose-1:2 4 5 3 5 4 6 3 2 4; mso-font-charset:0; mso-generic-font-family:roman; mso-font-pitch:variable; mso-font-signature:-536869121 1107305727 33554432 0 415 0;}p.MsoNormal, li.MsoNormal, div.MsoNormal {mso-style-unhide:no; mso-style-qformat:yes; mso-style-parent:""; margin:0cm; mso-pagination:widow-orphan; font-size:12.0pt; font-family:"Times New Roman",serif; mso-fareast-font-family:"Times New Roman"; mso-ansi-language:EN-US;}.MsoChpDefault {mso-style-type:export-only; mso-default-props:yes; font-size:10.0pt; mso-ansi-font-size:10.0pt; mso-bidi-font-size:10.0pt; mso-ansi-language:IN; mso-fareast-language:IN;}div.WordSection1 {page:WordSection1;}

scholarly journals Analysis of serum lipoproteins by high performance gel filtration chromatography.

1996 ◽  
Vol 45 (1) ◽  
pp. 103-106 ◽  
Author(s):  
Takashi KITAMURA ◽  
Seiji ITO ◽  
Yoshio KATO ◽  
Keiko SASAMOTO ◽  
Mitsuyo OKAZAKI
Keyword(s):  
High Performance ◽  
Gel Filtration ◽  
Serum Lipoproteins ◽  
Gel Filtration Chromatography

scholarly journals Structural and Functional Conversion of Molecular Chaperone ClpB from the Gram-Positive Halophilic Lactic Acid Bacterium Tetragenococcus halophilus Mediated by ATP and Stress

2006 ◽  
Vol 188 (23) ◽  
pp. 8070-8078 ◽  
Author(s):  
Shinya Sugimoto ◽  
Hiroyuki Yoshida ◽  
Yoshimitsu Mizunoe ◽  
Keigo Tsuruno ◽  
Jiro Nakayama ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacterium ◽  
Molecular Chaperone ◽  
Thermal Inactivation ◽  
Gel Filtration ◽  
Ring Structure ◽  
Stress Conditions ◽  
Gel Filtration Chromatography ◽  
Gram Positive ◽  
Tetragenococcus Halophilus

ABSTRACT In this study, we report the purification, initial structural characterization, and functional analysis of the molecular chaperone ClpB from the gram-positive, halophilic lactic acid bacterium Tetragenococcus halophilus. A recombinant T. halophilus ClpB (ClpB Tha ) was overexpressed in Escherichia coli and purified by affinity chromatography, hydroxyapatite chromatography, and gel filtration chromatography. As demonstrated by gel filtration chromatography, chemical cross-linking with glutaraldehyde, and electron microscopy, ClpB Tha forms a homohexameric single-ring structure in the presence of ATP under nonstress conditions. However, under stress conditions, such as high-temperature (>45°C) and high-salt concentrations (>1 M KCl), it dissociated into dimers and monomers, regardless of the presence of ATP. The hexameric ClpB Tha reactivated heat-aggregated proteins dependent upon the DnaK system from T. halophilus (KJE Tha ) and ATP. Interestingly, the mixture of dimer and monomer ClpB Tha , which was formed under stress conditions, protected substrate proteins from thermal inactivation and aggregation in a manner similar to those of general molecular chaperones. From these results, we hypothesize that ClpB Tha forms dimers and monomers to function as a holding chaperone under stress conditions, whereas it forms a hexamer ring to function as a disaggregating chaperone in cooperation with KJE Tha and ATP under poststress conditions.

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