In vitro stability evaluation of coated lipase
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Objective: The study was conducted to evaluate the stability of commercial coated lipase (CT-LIP) in vitro. Methods: The capsules were tested under different conditions with a range of temperature, pH, dry heat treatment and steaming treatment, simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) in this work, respectively. Free lipase (uncoated lipase, UC-LIP) was the control group. Lipase relative activities measured in various treatments were used as a reference frame to characterize the stability. Results: The lipase activities were decreased with increasing temperatures (p<0.05), and there was a markedly decline (p<0.01) in lipase comparative activities of UC-LIP at 80°C compared with CT-LIP group. Higher relative activities of lipase were observed in CT-LIP group compared with the free one under acidic ambient (pH 3 to 7) and an alkaline medium (pH 8 to 12). Residual lipase activities of CT-LIP group were increased (p<0.05) by 5.67% and 35.60% in dry heat and hydrothermal treatments, respectively. The lipase relative activity profile of CT-LIP was raised at first and dropped subsequently (p<0.05) compared with constantly reduced tendency of UC-LIP exposed to both SGF and SIF. Conclusion: The results suggest that the CT-LIP possesses relatively higher stability in comparison with the UC-LIP in vitro. The CT-LIP could retain the potential property to provide sustained release of lipase and thus improved its bioavailability in the gastrointestinal tract.
Abstract
Objective: The study was conducted to evaluate the stability of commercial coated lipase (CT-LIP) in vitro. Methods: The capsules were tested under different conditions with a range of temperature, pH, dry heat treatment and steaming treatment, simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) in this work, respectively. Free lipase (uncoated lipase, UC-LIP) was the control group. Lipase relative activities measured in various treatments were used as a reference frame to characterize the stability. Results: The lipase activities were decreased with increasing temperatures (p<0.05), and there was a markedly decline (p<0.01) in lipase comparative activities of UC-LIP at 80°C compared with CT-LIP group. Higher relative activities of lipase were observed in CT-LIP group compared with the free one under acidic ambient (pH 3 to 7) and an alkaline medium (pH 8 to 12). Residual lipase activities of CT-LIP group were increased (p<0.05) by 5.67% and 35.60% in dry heat and hydrothermal treatments, respectively. The lipase relative activity profile of CT-LIP was raised at first and dropped subsequently (p<0.05) compared with constantly reduced tendency of UC-LIP exposed to both SGF and SIF. Conclusion: The results suggest that the CT-LIP possesses relatively higher stability in comparison with the UC-LIP in vitro. The CT-LIP could retain the potential property to provide sustained release of lipase and thus improved its bioavailability in the gastrointestinal tract.
참고문헌 (28)
- Dierick NA, "The combined use of triacylglycerols (TAGs) containing medium chain fatty acids (MCFAs) and exogenous lipolytic enzymes as an alternative to nutritional antibiotics in piglet nutrition: II. In vivo release of MCFAs in gastric cannulated and slaughtered piglets by endogenous and exogenous lipases; effects on the luminal gut flora and growth performance", Livest Prod Sci, 76, pp.1~16 (2002)
- S.M. Hong, "Effect of Medium-chain Triglyceride (MCT) on Growth Performance, Nutrient Digestibility, Blood Characteristics in Weanling Pigs", ASIAN-AUSTRALASIAN JOURNAL OF ANIMAL SCIENCES, 25(7), pp.1003~1008 (2012), 아세아·태평양축산학회[DOI]
- Cromwell GL, "Why and how antibiotics are used in swine production", Anim Biotechnol, 13, pp.7~27 (2002)
- Roth RZ, "Organic acids as feed additives for young pigs: Nutritional and gastrointestinal effects", J Anim Feed Sci, 7, pp.25~33 (1998)
- Partanen K, "Organic acids for performance enhancement in pig diets", Nutr Res Rev, 12, pp.117~145 (1999)
- Bedford MR, "Exogenous enzymes in monogastric nutrition-their current value and future benefits", Anim Feed Sci Technol, 86, pp.1~13 (2000)
- Yin YL, "Apparent digestibility (ileal and overall) of nutrients and endogenous nitrogen losses in growing pigs fed wheat (var. Soissons) or its by-products without or with xylanase supplementation", Livest Prod Sci, 62, pp.119~132 (2000)
- Kiarie E, "The role of added feed enzymes in promoting gut health in swine and poultry", Nutr Res Rev, 26, pp.71~88 (2013)
- Karjiban RA, "Molecular dynamics of thermoenzymes at high temperature and pressure: a review", Prot J, 33, pp.369~376 (2014)
- Jensen M, "Development of digestive enzymes in pigs with emphasis on lipolytic activity in the stomach and pancreas", J Anim Sci, 75, pp.437~445 (1997)
- Gu X, "Fat nutrition and metabolism in piglets: a review", Anim Feed Sci Technol, 109, pp.151~170 (2003)
- Shi BL, "Effect on Growth Performance of weaning piglets by microbe lipase", Feed Review, 3, pp.1~3 (2010)
- Takada R, "Effects of feeding medium chain triglycerides on growth performance, digestibility, backfat thickness and fatty acid composition in finishing pigs", Jpn J Swine Sci, 29, pp.32~40 (1992)
- Decuypere JA, "The combined use of triacylglycerols containing medium-chain fatty acids and exogenous lipolytic enzymes as an alternative to in-feed antibiotics in piglets: concept, possibilities and limitations", Nutr Res Rev, 16, pp.193~210 (2003)
- Dierick NA, "Endogenous lipolysis in feedstuffs and compound feeds for pigs: effects of storage time and conditions and lipase and", or emulsifier addition, 2002, pp.102, 53~70
- Abbaspourrad A, "Controlling release from pH-responsive microcapsules", Langmuir, 29, pp.12697~12702 (2013)
- Valivety R, "Lipase from different sources vary widely in dependence of catalytic activity on water activity", Biochim Biophys Acta, 1122, pp.143~146 (1992)
- Liu X, "Microspheres of corn protein, zein, for an ivermectin drug delivery system", Biomaterials, 26, pp.109~115 (2005)
- National Pharmacopoeia Commission, "Pharmacopoeia of People’s Republic of China" (2010), Chemical Industry Press
- Luo Y, "Preparation and characterization of zein", chitosan complex for encapsulation of α-tocopherol, and its in vitro controlled release study, 2011, pp.85, 145~152
- Fernandes P, "Enzymes in food processing: a condensed overview on strategies for better biocatalysts", Enzyme Res, 2010, pp.1~19 (2010)
- Bassegoda A, "Lipase improvement: goals and strategies", Comput Struc Biotechnol J, 2, pp.1~8 (2012)
- Tümtürk H, "Preparation and application of poly (N, N- dimethylacrylamide-co-acrylamide) and poly (N-isopropylacrylamide-co-acrylamide)", κ-Carrageenan hydrogels for immobilization of lipase, 2007, pp.40, 281~285
- Nawani N, "Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme", Electron J Biotechnol, 9, pp.559~565 (2006)
- Kenthorai RJ, "Physical and stability characteristics of Burkholderia cepacia lipase encapsulated in κ-carrageenan", J Mol Catal B: Enzym, 58, pp.78~83 (2009)
- Inborr J, "Stability of feed enzymes to steam pelleting during feed processing", Anim Feed Sci Technol, 46, pp.179~196 (1994)
- Su DH, "Increased thermostability of phytase by coated conditions", Chinese J Bioprocess Eng, 3, pp.240~245 (2004)
- Itoh T, "Enhancement in thermal stability and resistance to denaturants of lipase encapsulated in mesoporous silica with alkyltrimethylammonium (CTAB)", Colloids Surf B, 75, pp.478~482 (2010)
