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Enzymatic Modification (enzymatic + modification)
Selected AbstractsEnzymatic modification as a tool to improve the functional properties of heat-processed soy flourJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 2 2008Cheruppanpullil Radha Abstract BACKGROUND: There are a number of antinutritional factors present in soybeans that exert a negative impact on the nutritional quality of the protein. Among those factors that are destroyed by heat treatment are protease inhibitors and lectins. Protease inhibitors show antinutritional effect and moreover the digestibility of the protein is limited by the presence of these antinutrients. The aims of the present study are (1) to study the effect of autoclaving on the trypsin inhibitor inactivation, nitrogen solubility and protein digestibility of defatted soy flour and (2) to study the effect of enzymatic modification on the functional properties of autoclaved soy flour. RESULTS: The solubility of the soy flour decreased with increase in autoclaving time. Partial hydrolysis of the autoclaved soy flour increased its acid solubility (pH 4.5) from 17% to 56% over a control value of 24% without affecting its functional properties. Inactivation of trypsin inhibitors improved the protein digestibility of soy flour from 25% to 95%. Particle size analysis of the autoclaved flour indicated the formation of soy protein aggregates, which resulted in poor solubility. The enzymatic modification of autoclaved soy flour resulted in its property as a good emulsifying agent with an emulsion capacity of 118 ± 4 mL. CONCLUSION: Enzymatic modification of the heat-processed soy flour increased its solubility and other functional attributes. The increased acid solubility would be advantageous in the utilization of soy proteins in acidic foods. Thus the autoclaved and partially modified soy flour is a potential source for specific functional foods. Copyright © 2007 Society of Chemical Industry [source] Effects of citraconylation on enzymatic modification of human proinsulin using trypsin and carboxypeptidase BBIOTECHNOLOGY PROGRESS, Issue 4 2009Young-Jin Son Abstract Insulin is a polypeptide hormone which is produced by the ,-cell of pancreas and controls the blood glucose level in the human body. Enzymatic modification of human proinsulin using trypsin and carboxypeptidase B generally causes high accumulation of insulin derivatives, leading to more complicated purification processes. A simple method including citraconylation and decitraconylation in the enzymatic modification process was developed for the reduction of a major derivative, des-threonine human insulin. Addition of 3.0 g citraconic anhydride per g protein into the reaction solution led to the citraconylation of lysine residues in human proinsulin and reduction of relative des-threonine insulin content from 13.5 to 1.0%. After the enzymatic hydrolysis of the citraconylated proinsulin, 100% of lysine residues can be decitraconylated and restored by adjusting pH to 2,3 at 25 °C. Combination of hydrogen peroxide addition and citraconylation of proinsulin expressed in recombinant Escherichia coli remarkably improved the conversion yield of insulin from 52.7 to 77.7%. Consequently, citraconylation of lysine residues blocked the unexpected cleavage of human proinsulin by trypsin, minimized the formation of des-threonine insulin and hence increased the production yield of active insulin. © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009 [source] Structured lipids from rice bran oil and stearic acid using immobilized lipase from Rhizomucor mieheiEUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY, Issue 1 2008Rajni Chopra Abstract The major objective of the present study was to prepare structured lipids rich in stearic acid from rice bran oil (RBO) using immobilized lipase (IM,60) from Rhizomucor miehei. The effects of incubation time and temperature, substrate molar ratio, and enzyme load on incorporation of stearic acid were studied. Acidolysis reactions were performed in hexane. Pancreatic lipase-catalyzed sn -2 positional analysis and tocopherol analyses were performed before and after enzymatic modification. The kinetics of the reaction was studied and maximum incorporation of stearic acid was observed at 6,h, at 37,°C, when the triacylglycerol and stearic acid molar ratio was maintained at 1,:,6 and the enzyme concentration was 10% of total substrates weight. Stearic acid in RBO after acidolysis was increased from 2.28 to 48.5%, with a simultaneous decrease in palmitic, oleic and linoleic acids. HPLC analysis of tocopherols and tocotrienols was carried out and their content in modified RBO was not significantly affected compared to that of native RBO. The oryzanol content of the modified RBO was reduced from 1.02 to 0.68%. Melting and crystallizing characteristics of the modified fat were studied using differential scanning calorimetry. The total solid fat content at 25,°C increased from 26.12 to 34.8% with an increase in stearic acid incorporation into RBO from 38 to 48%, but it was comparatively less than for cocoa butter and vanaspati. However, the modified RBO completely melted at 37,°C and was useful as plastic fat for various culinary purposes, bakery and confectionary applications. The results of the present study indicated that structured lipids prepared from RBO rich in stearic acid retained their beneficial nutraceuticals; in addition, they do not contain any trans fatty acids. [source] The expansion of mechanistic and organismic diversity associated with non-ribosomal peptidesFEMS MICROBIOLOGY LETTERS, Issue 2 2000Michelle C Moffitt Abstract Non-ribosomal peptides are a group of secondary metabolites with a wide range of bioactivities, produced by prokaryotes and lower eukaryotes. Recently, non-ribosomal synthesis has been detected in diverse microorganisms, including the myxobacteria and cyanobacteria. Peptides biosynthesized non-ribosomally may often play a primary or secondary role in the producing organism. Non-ribosomal peptides are often small in size and contain unusual or modified amino acids. Biosynthesis occurs via large modular enzyme complexes, with each module responsible for the activation and thiolation of each amino acid, followed by peptide bond formation between activated amino acids. Modules may also be responsible for the enzymatic modification of the substrate amino acid. Recent analysis of biosynthetic gene clusters has identified novel integrated, mixed and hybrid enzyme systems. These diverse mechanisms of biosynthesis result in the wide variety of non-ribosomal peptide structures and bioactivities seen today. Knowledge of these biosynthetic systems is rapidly increasing and methods of genetically engineering these systems are being developed. In the future, this may lead to rational drug design through combinatorial biosynthesis of these enzyme systems. [source] The biology of lantibiotics from the lacticin 481 group is coming of ageFEMS MICROBIOLOGY REVIEWS, Issue 2 2007Alain Dufour Abstract Lantibiotics are antimicrobial peptides from the bacteriocin family, secreted by Gram-positive bacteria. These peptides differ from other bacteriocins by the presence of (methyl)lanthionine residues, which result from enzymatic modification of precursor peptides encoded by structural genes. Several groups of lantibiotics have been distinguished, the largest of which is the lacticin 481 group. This group consists of at least 16 members, including lacticin 481, streptococcin A-FF22, mutacin II, nukacin ISK-1, and salivaricins. We present the first review devoted to this lantibiotic group, knowledge of which has increased significantly within the last few years. After updating the group composition and defining the common properties of these lantibiotics, we highlight the most recent developments. The latter concern: transcriptional regulation of the lantibiotic genes; understanding the biosynthetic machinery, in particular the ability to perform in vitro prepeptide maturation; characterization of a novel type of immunity protein; and broad application possibilities. This group differs in many aspects from the best known lantibiotic group (nisin group), but shares properties with less-studied groups such as the mersacidin, cytolysin and lactocin S groups. [source] Transglutaminase Catalysis of Modified Whey Protein DispersionsJOURNAL OF FOOD SCIENCE, Issue 4 2010Debra A. Clare ABSTRACT:, Transglutaminase (TGase) cross-linking reactions were accomplished using a heat-modified whey protein concentrate (mWPC) substrate after pH adjustment to 8. Based on earlier reports, the degree of lactosylation with respect to ,-lactoglobulin was lower in mWPC dispersions than measured in commercial whey concentrate (cWPC) protein solutions. In this study, a higher concentration of free sulfhydryl groups was detected in soluble supernatant fractions. Both factors potentially impact the availability of reactive lysine/glutaminyl residues required for TGase reactivity. The addition of 10 mM dithiothreitol (DTT) to the substrate mix, CBZ-glutaminyl glycine and hydroxylamine, revealed a 3.6-fold increase in TGase activity, likely due in part to maintenance of the catalytic cysteine residue in a reduced state. Furthermore, inclusion of DTT to mWPC dispersions significantly raised the apparent viscosity, independently of enzyme modification, while the rate of polymerization increased 2-fold based on OPA assay measurements. Limited cross-linking slightly increased the apparent viscosity, whereas extensive coupling lowered these values compared to equivalent nonenzyme-treated mWPC samples. Carbohydrate-staining revealed formation of glyco-polymers due to covalent linkages between glucosamine and mWPC proteins after TGase processing. Again, the apparent viscosity decreased after extensive enzymatic modification. Larger particles, sized 11.28 ,m, were observed in the structural matrix of TGase-mWPC-fixed samples compared to 8 ,m particles in control mWPC samples as viewed in scanning electron micrographs. Ultimately, the functional characteristics of TGase-mWPC ingredients may be custom-designed to deliver alternative functional attributes by adjusting the experimental reaction conditions under which catalysis is achieved. Practical Application: Taken together, these results suggest that unique TGase-mWPC and/or TGase-mWPC-glucosamine ingredients may be designed to provide novel, value-added, polymeric/glyco-polymeric protein products that afford added benefit for the milk industry. [source] Enzymatic modification as a tool to improve the functional properties of heat-processed soy flourJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 2 2008Cheruppanpullil Radha Abstract BACKGROUND: There are a number of antinutritional factors present in soybeans that exert a negative impact on the nutritional quality of the protein. Among those factors that are destroyed by heat treatment are protease inhibitors and lectins. Protease inhibitors show antinutritional effect and moreover the digestibility of the protein is limited by the presence of these antinutrients. The aims of the present study are (1) to study the effect of autoclaving on the trypsin inhibitor inactivation, nitrogen solubility and protein digestibility of defatted soy flour and (2) to study the effect of enzymatic modification on the functional properties of autoclaved soy flour. RESULTS: The solubility of the soy flour decreased with increase in autoclaving time. Partial hydrolysis of the autoclaved soy flour increased its acid solubility (pH 4.5) from 17% to 56% over a control value of 24% without affecting its functional properties. Inactivation of trypsin inhibitors improved the protein digestibility of soy flour from 25% to 95%. Particle size analysis of the autoclaved flour indicated the formation of soy protein aggregates, which resulted in poor solubility. The enzymatic modification of autoclaved soy flour resulted in its property as a good emulsifying agent with an emulsion capacity of 118 ± 4 mL. CONCLUSION: Enzymatic modification of the heat-processed soy flour increased its solubility and other functional attributes. The increased acid solubility would be advantageous in the utilization of soy proteins in acidic foods. Thus the autoclaved and partially modified soy flour is a potential source for specific functional foods. Copyright © 2007 Society of Chemical Industry [source] Effects of citraconylation on enzymatic modification of human proinsulin using trypsin and carboxypeptidase BBIOTECHNOLOGY PROGRESS, Issue 4 2009Young-Jin Son Abstract Insulin is a polypeptide hormone which is produced by the ,-cell of pancreas and controls the blood glucose level in the human body. Enzymatic modification of human proinsulin using trypsin and carboxypeptidase B generally causes high accumulation of insulin derivatives, leading to more complicated purification processes. A simple method including citraconylation and decitraconylation in the enzymatic modification process was developed for the reduction of a major derivative, des-threonine human insulin. Addition of 3.0 g citraconic anhydride per g protein into the reaction solution led to the citraconylation of lysine residues in human proinsulin and reduction of relative des-threonine insulin content from 13.5 to 1.0%. After the enzymatic hydrolysis of the citraconylated proinsulin, 100% of lysine residues can be decitraconylated and restored by adjusting pH to 2,3 at 25 °C. Combination of hydrogen peroxide addition and citraconylation of proinsulin expressed in recombinant Escherichia coli remarkably improved the conversion yield of insulin from 52.7 to 77.7%. Consequently, citraconylation of lysine residues blocked the unexpected cleavage of human proinsulin by trypsin, minimized the formation of des-threonine insulin and hence increased the production yield of active insulin. © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009 [source] | |||||||||||||