Biochemical Properties of Recombinant Leucine Aminopeptidase II from Bacillus stearothermophilus and Potential Applications in the Hydrolysis of Chinese Anchovy (Engraulis japonicus) Proteins
The effects of various factors on the activity and conformation of recombinant leucine aminopeptidase II (rLAP II) from Bacillus stearothermophilus and its potential utilization in the hydrolysis of anchovy proteins were investigated. The optimal temperature and pH of rLAP II were 55 °C and 8.0 in p...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2012-01, Vol.60 (1), p.165-172 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Wang, Fanghua Ning, Zhengxiang Lan, Dongming Liu, Yuanyuan Yang, Bo Wang, Yonghua |
| description | The effects of various factors on the activity and conformation of recombinant leucine aminopeptidase II (rLAP II) from Bacillus stearothermophilus and its potential utilization in the hydrolysis of anchovy proteins were investigated. The optimal temperature and pH of rLAP II were 55 °C and 8.0 in phosphate buffer, and its activity was strongly stimulated by Co2+. Conformational studies indicated that maintaining the α-helical structure had a critical effect on rLAP II activity. rLAP II was used to hydrolyze anchovy proteins, and it exhibited high specificity for peptides with molecular weight between 6000 and 1000 Da and positive coordination with endogenous enzymes and commercial Flavourzyme. Its use will enhance protein hydrolysis in species of aquatic animals. rLAP II could potentially be used to remove bitterness in the protein hydrolysis industry. |
| doi_str_mv | 10.1021/jf204002e |
| format | Article |
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The optimal temperature and pH of rLAP II were 55 °C and 8.0 in phosphate buffer, and its activity was strongly stimulated by Co2+. Conformational studies indicated that maintaining the α-helical structure had a critical effect on rLAP II activity. rLAP II was used to hydrolyze anchovy proteins, and it exhibited high specificity for peptides with molecular weight between 6000 and 1000 Da and positive coordination with endogenous enzymes and commercial Flavourzyme. 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Agric. Food Chem</addtitle><description>The effects of various factors on the activity and conformation of recombinant leucine aminopeptidase II (rLAP II) from Bacillus stearothermophilus and its potential utilization in the hydrolysis of anchovy proteins were investigated. The optimal temperature and pH of rLAP II were 55 °C and 8.0 in phosphate buffer, and its activity was strongly stimulated by Co2+. Conformational studies indicated that maintaining the α-helical structure had a critical effect on rLAP II activity. rLAP II was used to hydrolyze anchovy proteins, and it exhibited high specificity for peptides with molecular weight between 6000 and 1000 Da and positive coordination with endogenous enzymes and commercial Flavourzyme. Its use will enhance protein hydrolysis in species of aquatic animals. rLAP II could potentially be used to remove bitterness in the protein hydrolysis industry.</description><subject>Animals</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Enzyme Stability</subject><subject>Fish Proteins - chemistry</subject><subject>Fishes</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Geobacillus stearothermophilus - chemistry</topic><topic>Geobacillus stearothermophilus - enzymology</topic><topic>Geobacillus stearothermophilus - genetics</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>Leucyl Aminopeptidase - chemistry</topic><topic>Leucyl Aminopeptidase - genetics</topic><topic>Leucyl Aminopeptidase - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Fanghua</creatorcontrib><creatorcontrib>Ning, Zhengxiang</creatorcontrib><creatorcontrib>Lan, Dongming</creatorcontrib><creatorcontrib>Liu, Yuanyuan</creatorcontrib><creatorcontrib>Yang, Bo</creatorcontrib><creatorcontrib>Wang, Yonghua</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Fanghua</au><au>Ning, Zhengxiang</au><au>Lan, Dongming</au><au>Liu, Yuanyuan</au><au>Yang, Bo</au><au>Wang, Yonghua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical Properties of Recombinant Leucine Aminopeptidase II from Bacillus stearothermophilus and Potential Applications in the Hydrolysis of Chinese Anchovy (Engraulis japonicus) Proteins</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2012-01-11</date><risdate>2012</risdate><volume>60</volume><issue>1</issue><spage>165</spage><epage>172</epage><pages>165-172</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The effects of various factors on the activity and conformation of recombinant leucine aminopeptidase II (rLAP II) from Bacillus stearothermophilus and its potential utilization in the hydrolysis of anchovy proteins were investigated. The optimal temperature and pH of rLAP II were 55 °C and 8.0 in phosphate buffer, and its activity was strongly stimulated by Co2+. Conformational studies indicated that maintaining the α-helical structure had a critical effect on rLAP II activity. rLAP II was used to hydrolyze anchovy proteins, and it exhibited high specificity for peptides with molecular weight between 6000 and 1000 Da and positive coordination with endogenous enzymes and commercial Flavourzyme. Its use will enhance protein hydrolysis in species of aquatic animals. rLAP II could potentially be used to remove bitterness in the protein hydrolysis industry.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>22148180</pmid><doi>10.1021/jf204002e</doi><tpages>8</tpages></addata></record> |
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| subjects | Animals Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological and medical sciences Enzyme Stability Fish Proteins - chemistry Fishes Food industries Fundamental and applied biological sciences. Psychology Geobacillus stearothermophilus - chemistry Geobacillus stearothermophilus - enzymology Geobacillus stearothermophilus - genetics Hydrolysis Kinetics Leucyl Aminopeptidase - chemistry Leucyl Aminopeptidase - genetics Leucyl Aminopeptidase - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Substrate Specificity |
| title | Biochemical Properties of Recombinant Leucine Aminopeptidase II from Bacillus stearothermophilus and Potential Applications in the Hydrolysis of Chinese Anchovy (Engraulis japonicus) Proteins |
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