Purification and characterization of trypsin from the pyloric caeca of rainbow trout (Oncorhynchus mykiss)

Kristjánsson, Magnús M.

doi:10.1021/jf00010a009

Cited by 88 publications

(92 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These results show that the partially purified enzyme from anchovy digestive tract exhibit protease characteristics. Our results are similar with other data in the study of Martinez et al (1988), Kristjansson (1991), Bougatef et al (2007), Shi et al (2007) and Lu et al (2008) enzyme was not affected by β-mercaptoethanol. Based on the results, metallo-protease inhibitor EDTA, which chelates the metals ions required for the enzyme, partially inhibited enzyme activity by 19%, indicating the importance of some metal ions in enzyme stabilization.…”

Section: Effect Of Enzyme Inhibitorssupporting

confidence: 93%

Partial purification and characterization of alkaline proteases from the Black Sea anchovy(Engraulis encrasicholus) digestive tract

Temiz¹,

Üstün²,

Turhan³

et al. 2013

Afr. J. Biotechnol.

View full text Add to dashboard Cite

Alkaline proteases from the digestive tract of anchovy were partially purified by ammonium sulfate fractionation, dialysis and Sephadex G-75 gel filtration. The purification fold and yield were 6.23 and 4.49%, respectively. The optimum activities of partially purified alkaline proteases were observed at 60°C and at pH 11.0. The alkaline proteases were stable within the temperature range of 40 to 50°C and pH range of 9.0 to 11.0. They were inhibited by the serine-protease inhibitor phenylmethylsulfonyl fluoride (PMSF) and trypsin specific inhibitor benzamidine, but were not inhibited by the β-mercaptoethanol. The enzymes were slightly activated by metal ions such as Na +

show abstract

Section: Effect Of Enzyme Inhibitorssupporting

confidence: 93%

Partial purification and characterization of alkaline proteases from the Black Sea anchovy(Engraulis encrasicholus) digestive tract

Temiz¹,

Üstün²,

Turhan³

et al. 2013

Afr. J. Biotechnol.

View full text Add to dashboard Cite

show abstract

“…It is also speculated that differences in the level of purification fold after ATPS process among tuna species might be related to different physicochemical and enzyme properties. Most of the methods reported for proteinase purification from fish digestive organs involved several steps, including ammonium sulfate precipitation, size-exclusion and ion-exchange chromatography [14,15], hydrophobic interaction chromatography [5] and affinity chromatography [29,38]. In view of their characteristics, these multi-step methods result in high cost and time consuming purification process.…”

Section: Recovery Of Spleen Proteinase From Other Tuna Speciesmentioning

confidence: 99%

“…in the detergent, food, pharmaceutical, leather and silk industries [3][4][5][6][7]. The use of alkaline proteinases has increased remarkably since they are both stable and active under harsh conditions such as at temperatures of 50 to 60°C, high pHs and in the presence of surfactants or oxidizing agents [7,8].…”

mentioning

confidence: 99%

Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems

Klomklao

Benjakul

Visessanguan

et al. 2005

Process Biochemistry

102

View full text Add to dashboard Cite

Partitioning of spleen proteinase from yellowfin tuna (Thunnus albacores) in an aqueous two-phase system (ATPS) was investigated. Phase compositions including PEG molecular mass and concentration as well as types and concentration of salts affected the protein partitioning. ATPS comprising PEG1000 (15% w/w) and magnesium sulfate (20% w/w) provided the best condition for the maximum partitioning of the proteinase into the top phase and gave a highest specific activity (47.0 units/µg protein) and purification fold (6.61). The yield of 69.0% was obtained.Under the same ATPS condition used, the partitioning of proteinase of splenic extract from three tuna species involving skipjack tuna, yellowfin tuna and tongol tuna were compared. The purity of splenic extract from all tuna species increased after ATPS process. Among all species tested, yellowfin tuna showed the highest purification fold, followed by tongol tuna and skipjack tuna, respectively. SDS-substrate gel electrophoresis revealed that the band intensity of major proteinase in ATPS fraction from all tuna species slightly increased with the concomitant decrease in band intensity of other contaminating proteins, indicating the greater specific activity of splenic extract. Therefore, ATPS was an effective method for partitioning and recovery of proteinases from tuna spleen.

show abstract

“…Enzymes from cold adapted fish species thus often have higher emzymatic activities at low temperatures than their counterparts from warm-blooded animals (Asgeirsson et al, 1989;Kristjansson, 1991). High activity of fish enzymes at low temperatures may be interesting for several industrial applications of enzymes, such as in certain food processing operations that require low processing temperatures.…”

Section: Introductionmentioning

confidence: 99%

Characteristics of trypsins from the viscera of true sardine (Sardinops melanostictus) and the pyloric ceca of arabesque greenling (Pleuroprammus azonus)

et al. 2006

View full text Add to dashboard Cite

Trypsins, TR-S and TR-P, from the viscera of true sardine (Sardinops melanostictus) and from the pyloric ceca of arabesque greenling (Pleuroprammus azonus), respectively, were purified by gel filtration and anion-exchange chromatography. Final enzyme preparations were nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the molecular weights of both enzymes were estimated to be 24,000 Da by SDS-PAGE. The N-terminal amino acid sequences of the TR-S, IVGGYECKAYSQPWQVSLNS, and TR-P, IVGGYECTPHTQAHQVSLNS, were found. The TR-S and TR-P had maximal activities at around pH 8.0 for hydrolysis of N α -p-tosyl-L-arginine methyl ester. Optimum temperature of the TR-S and TR-P were 60 ℃ and 50 ℃, respectively. The TR-S and TR-P were unstable at above 50 ℃ and 30 ℃, respectively, and below pH 5.0. Both TR-S and TR-P were stabilized by calcium ion.

show abstract

Purification and characterization of trypsin from the pyloric caeca of rainbow trout (Oncorhynchus mykiss)

Cited by 88 publications

References 17 publications

Partial purification and characterization of alkaline proteases from the Black Sea anchovy(Engraulis encrasicholus) digestive tract

Partial purification and characterization of alkaline proteases from the Black Sea anchovy(Engraulis encrasicholus) digestive tract

Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems

Characteristics of trypsins from the viscera of true sardine (Sardinops melanostictus) and the pyloric ceca of arabesque greenling (Pleuroprammus azonus)

Contact Info

Product

Resources

About