Purification and Characterization of a Trypsin-Like Protease from Flatfish (<i>Paralichthys olivaceus</i>) Intestine

Kim, Misook; Jeong, Yoonhwa

doi:10.1111/j.1745-4514.2012.00672.x

Cited by 9 publications

(5 citation statements)

References 52 publications

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“…However, an increase up to 75 °C resulted in decreased activity (Figure 7). These are similarly to previous studies on Paralichthys olivaceus (Kim and Jeong, 2013), Sardenella longiceps (Khandagale et al, 2017), and Acanthopagrus latus (Namjou et al, 2019). However, they are different from Helicoverpa armigera (Grover et al, 2018) and O. niloticus (Prihanto et al, 2019) which have optimal alkaline protease activity at 50 °C and 35 °C and decreased at 60 °C.…”

Section: Pepsin and Trypsin-like Activitiessupporting

confidence: 91%

Digestive Enzyme Activities in Barred Loach (Nemacheilus fasciatus, Val., 1846.): Effect of pH and Temperature

Susilo

Rachmawati

Wibowo

et al. 2022

molekul

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This study aims to determine the total protease, lipase, and amylase activities at different pHs, as well as pepsin and trypsin-like at different temperatures. A total of 240 individuals have been used in this study. Enzyme activity was measured by the spectrophotometer method. The effect of pH was evaluated on protease, lipase, and amylase activity, while the effect of temperature was evaluated on pepsin and trypsin-like activities.The results showed that the total protease activity at pH 7.0-10.0 was significantly higher than pH 1.7-5.0 (P <0.05). Furthermore, the activity of lipase was significantly higher at pH 5.0-7.0 than pH 1.7, 3.4, and 10.0. Also, the activity of amylase at pH 7.0-8.0 was significantly higher (p <0.05) than pH 1.7-5.0 and pH 10.0. Moreover, the pepsin-like activity in the anterior gut was significantly higher (p <0.05) than the posterior gut.Conversely, trypsin-like activity in the posterior gut was significantly higher (p <.05) than the anterior gut. Additionally, the pepsin-like activity was significantly higher at 45°C compared to different temperatures (p <0.05), whereas trypsin-like was significantly (p <0.05) higher at 60 °C than othertemperatures. Conclusively, the total protease and amylase activity was higher under neutral to slightly alkaline conditions, while lipase was higher under acidic to neutral conditions. Furthermore, the pepsin-like activity was only found in the anterior gut, whereas trypsin-like was higher in the posterior gut. The optimal temperature for pepsin-like and trypsin-like activity was 45 °C and 60 °C, respectively.

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Section: Pepsin and Trypsin-like Activitiessupporting

confidence: 91%

Digestive Enzyme Activities in Barred Loach (Nemacheilus fasciatus, Val., 1846.): Effect of pH and Temperature

Susilo

Rachmawati

Wibowo

et al. 2022

molekul

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“…In this study, trypsin activity presented optimal activity at pH 9.5. For Thunnus orientalist, the highest trypsin activity was observed at pH 8.0, while the same was observed for Paralichthys olivaceus at pH 7.5 (Parra et al, 2007;Kim and Jeong, 2013).…”

Section: Effect Of Phmentioning

confidence: 52%

“…Peptidase inhibition patterns observed here were not similar to those observed in other species of fish, and neither were the degrees of inhibition. Kim and Jeong (2013) observed complete inhibition for purified trypsin using PMSF, benzamidine and TLCK in olive flounder intestine. Klomklao et al (2007Klomklao et al ( , 2010) also found complete inhibition in both TLCK and for TPCK for Katsuwonus pelamis and Cololabis saira.…”

Section: Effect Of Inhibitorsmentioning

confidence: 99%

Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus

et al. 2017

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Knowledge of specific enzyme activity, along with animal habits and digestive capacity is essential in formulating an appropriate diet for any species. In this study, we evaluated and characterized the activity of digestive enzymes present in the liver, intestine, and stomach of Paralichthys orbignyanus. The effects of pH and temperature on enzyme activity were also evaluated via the use of specific substrates. The use of specific substrates and inhibitors showed strong evidence of the presence of trypsin (BApNA= 0.51 ± 0.2 mU mg -1 ), chimotrypsin (SApNA= 2.62 ± 1.8 mU mg -1 ), and aminopeptidases (Leu-p-Nan =0.9709 ± 0.83 mU mg -1 ) in the intestine. Optimum pH for the activity of trypsin, chemotrypsin, leucino aminopeptidase, amilase, and pepsin were 9.5, 9.0, 8.0, 7.5, and 3.5, respectively, while optimum temperatures were 50, 50, 50, 40, and 45 °C, respectively. These results provide additional information regarding the biology of Brazilian flounder and can be used as a basis for further studies regarding fish feeding physiology.Keywords: trypsin, protease, digestive tract. Caracterização de enzimas digestivas do linguado brasileiro de cativeiro Paralichthys orbignyanusResumo O conhecimento da atividade enzimática é essencial para formular uma correta dieta específica para espécie, além de estarem correlacionadas com o hábito da alimentação e capacidade digestive. Neste estudo determinamos e caracterizamos a atividade enzimática presente no intestino, estômago e fígado do linguado Paralichthys orbignyanus. Os efeitos da temperatura e pH sobre a atividade enzimática também foram avaliados utilizando substratos específicos. O uso de substratos e inibidores específicos mostrou uma forte evidência da presença da tripsina (BApNA = 0,51 ± 0,2 mU mg-1), quimotripsina (SAPNA = 2,62 ± 1,8 mU mg-1), e as aminopeptidases (Leu-p-Nan = 0,97 ± 0,83 mU mg-1) no intestino. O pH ótimo observado para a atividade de tripsina, quimotripsina, leucino aminopeptidase, amilase e pepsina foi 9,5, 9,0, 8,0, 7,5 e 3,5, respectivamente. A temperatura ótima observada foi 50, 50, 50, 40 e 45 °C, respectivamente. Estes resultados fornecem informações adicionais sobre a biologia do linguado brasileiro e pode ser usado como base para novos estudos sobre fisiologia alimentar.Palavras-chave: tripsina, proteases, trato digestório.Candiotto, F.B. et al.

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“…The specific activity of the enzyme was 0.256 U/mg. The unit (U) indicates the quantity of the enzyme that catalyzes the reaction of 1 mol of substrate per minute at optimum conditions [19]. Table 1 shows that the activity of the trypsin isolated from yellowfin tuna is almost the same as that isolated from the intestines of little tuna (0.290 U/mg) [20].…”

Section: Trypsin Activity Crude Extract and Trypsin Powder Without Mi...mentioning

confidence: 99%

Microencapsulation of trypsin from the intestine of yellowfin tuna (Thunnus Albacares)

Nurhayati

Ramadhan

Raharja

2022

IOP Conf. Ser.: Earth Environ. Sci.

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Fish viscera is one of the waste products from fisheries that have not been widely used it tends to be disposed of more. Whereas in fish innards there are some enzymes including the trypsin found in the intestines. To increase the added value of fish viscera, a study on the extraction and microencapsulation of trypsin from fish intestines was carried out. This study aimed to analyze the activity of the trypsin from tuna intestine microencapsulated using maltodextrin. The concentrations of maltodextrin used were 0%, 1%, 2%, and 3% w/v. The microencapsulated enzymes were then dried using a spray dryer. The results showed that the crude extract of the trypsin had a specific activity value of 0.250 U/mg with a Vmax value of 0.0379 mmol/s and Km 0.2299 mM. Trypsin microencapsulated with 1% (w/v) maltodextrin was the best treatment because it has the highest specific activity (0.235±0.013 U/mg) with Vmax values of 0,0208 mmol/s and Km of 0,8581 mM. After going through the drying process with a spray dryer, the enzyme activity decreased by 10±1%.

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Purification and Characterization of a Trypsin-Like Protease from Flatfish (Paralichthys olivaceus) Intestine

Cited by 9 publications

References 52 publications

Digestive Enzyme Activities in Barred Loach (Nemacheilus fasciatus, Val., 1846.): Effect of pH and Temperature

Digestive Enzyme Activities in Barred Loach (Nemacheilus fasciatus, Val., 1846.): Effect of pH and Temperature

Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus

Microencapsulation of trypsin from the intestine of yellowfin tuna (Thunnus Albacares)

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