PROPERTIES OF COMMERCIAL MICROBIAL PROTEINASE PREPARATIONS Export

@article{citeulike:5984120, abstract = {Twenty three commercial microbial proteinase preparations derived from various <i>Bacillus</i> or <i>Aspergillus</i> spp. or from <i>Rhizomucor niveus</i> were assessed for proteolytic activity on azocasein at pH 5.5 or 7.0, or specificity on sodium caseinate at pH 5.5 and semi-quantitatively assessed for esterase, lipase, trypsin, chymotrypsin, general aminopeptidase, phosphatase and glycosidase activities using the API-ZYM system. Selected preparations were further assayed for peptidase, esterase and lipase activities at pH 7.0. The proteolytic activity of the <i>Bacillus</i> preparations was greater at pH 7.0, while that of the <i>Aspergillus</i> and <i>Rhizomucor</i> preparations was greater at pH 5.5. All the <i>Bacillus</i> preparations contained one of two main proteolytic activities, thought to be either bacillolysin or subtilisin. Most of the <i>Aspergillus</i> preparations contained the same proteinase, thought to be aspergillopepsin I, but two preparations appeared to contain a different unidentified proteinase. The proteolytic specificity of the <i>Rhizomucor</i> preparation was different from the <i>Bacillus</i> or <i>Aspergillus</i> preparations; thought to be rhizopuspepsin. According to the results of the API-ZYM system, all preparations contained enzyme activities in addition to their main proteolytic activity, with the <i>Aspergillus</i> and <i>Rhizomucor</i> preparations containing the highest levels and widest range of activities. Generally preparations derived from <i>Aspergillus</i> contained the highest level of general, proline and endopeptidase activities, with the <i>Bacillus</i> preparations conspicuous by the absence of general and proline-specific peptidase activities, while the <i>Rhizomucor niveus</i> preparation contained little or no general or endopeptidase activity. Esterase activity was found in all of the preparations evaluated, with only two <i>Aspergillus</i> preparations containing lipase activity.}, author = {Kilcawley, K. N. and Wilkinson, M. G. and Fox, P. F.}, citeulike-article-id = {5984120}, citeulike-linkout-0 = {http://dx.doi.org/10.1081/FBT-120004200}, doi = {10.1081/FBT-120004200}, journal = {Food Biotechnology}, keywords = {activity, protease, review}, number = {1}, pages = {29--55}, posted-at = {2009-10-22 08:44:24}, priority = {2}, publisher = {Taylor \& Francis}, title = {PROPERTIES OF COMMERCIAL MICROBIAL PROTEINASE PREPARATIONS}, url = {http://dx.doi.org/10.1081/FBT-120004200}, volume = {16}, year = {2002} }

TY - JOUR ID - citeulike:5984120 L3 - citeulike-article-id:5984120 N2 - Twenty three commercial microbial proteinase preparations derived from various <i>Bacillus</i> or <i>Aspergillus</i> spp. or from <i>Rhizomucor niveus</i> were assessed for proteolytic activity on azocasein at pH 5.5 or 7.0, or specificity on sodium caseinate at pH 5.5 and semi-quantitatively assessed for esterase, lipase, trypsin, chymotrypsin, general aminopeptidase, phosphatase and glycosidase activities using the API-ZYM system. Selected preparations were further assayed for peptidase, esterase and lipase activities at pH 7.0. The proteolytic activity of the <i>Bacillus</i> preparations was greater at pH 7.0, while that of the <i>Aspergillus</i> and <i>Rhizomucor</i> preparations was greater at pH 5.5. All the <i>Bacillus</i> preparations contained one of two main proteolytic activities, thought to be either bacillolysin or subtilisin. Most of the <i>Aspergillus</i> preparations contained the same proteinase, thought to be aspergillopepsin I, but two preparations appeared to contain a different unidentified proteinase. The proteolytic specificity of the <i>Rhizomucor</i> preparation was different from the <i>Bacillus</i> or <i>Aspergillus</i> preparations; thought to be rhizopuspepsin. According to the results of the API-ZYM system, all preparations contained enzyme activities in addition to their main proteolytic activity, with the <i>Aspergillus</i> and <i>Rhizomucor</i> preparations containing the highest levels and widest range of activities. Generally preparations derived from <i>Aspergillus</i> contained the highest level of general, proline and endopeptidase activities, with the <i>Bacillus</i> preparations conspicuous by the absence of general and proline-specific peptidase activities, while the <i>Rhizomucor niveus</i> preparation contained little or no general or endopeptidase activity. Esterase activity was found in all of the preparations evaluated, with only two <i>Aspergillus</i> preparations containing lipase activity. IS - 1 JF - Food Biotechnology EP - 55 TI - PROPERTIES OF COMMERCIAL MICROBIAL PROTEINASE PREPARATIONS PB - Taylor & Francis VL - 16 SP - 29 KW - activity KW - protease KW - review AU - Kilcawley, KN AU - Wilkinson, MG AU - Fox, PF PY - 2002/// UR - http://dx.doi.org/10.1081/FBT-120004200 ER -