2011
DOI: 10.1007/s00217-011-1650-2
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Production and characterization of milk-clotting enzyme from Bacillus amyloliquefaciens JNU002 by submerged fermentation

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Cited by 16 publications
(18 citation statements)
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“…For example, Bacillus licheniformis USC13 has been utilized for the production of milk-clotting enzyme but further inhibition studies revealed that the enzyme was a serine type proteinase (Ageitos et al 2007). Recently, Ding et al (2012) also reported production of a milk-clotting enzyme by Bacillus amyloliquefaciens JNU002 but it has also been mentioned that the enzyme was not an aspartic type of proteinase. Cheese making industry seeks for novel microbial enzyme sources; however, more studies are needed for elucidation of structural characteristic of these enzymes and their proteolytic patterns during cheese ripening.…”
Section: Microbial Aspartic Proteinasesmentioning
confidence: 99%
“…For example, Bacillus licheniformis USC13 has been utilized for the production of milk-clotting enzyme but further inhibition studies revealed that the enzyme was a serine type proteinase (Ageitos et al 2007). Recently, Ding et al (2012) also reported production of a milk-clotting enzyme by Bacillus amyloliquefaciens JNU002 but it has also been mentioned that the enzyme was not an aspartic type of proteinase. Cheese making industry seeks for novel microbial enzyme sources; however, more studies are needed for elucidation of structural characteristic of these enzymes and their proteolytic patterns during cheese ripening.…”
Section: Microbial Aspartic Proteinasesmentioning
confidence: 99%
“…In our previous study, Bacillus amyloliquefaciens JNU002 exhibited high MCA (4,969 SU ml -1 ) and promising enzyme characteristics [11]. In this study, the effects of agitation and aeration on MCE production were investigated, and a two-stage oxygen supply control strategy was proposed and evaluated.…”
Section: Introductionmentioning
confidence: 98%
“…5C. This result was different from the MCEs produced by M. pusillus (49 kDa) and B. amyloliquefaciens JNU002 (28 kDa) (Ding et al, 2012;Nouani et al, 2009), indicating that the MCE from B. methanolicus LB-1 could be a new protease. Based on cross-reference to National Center for Biotechnology Information (NCBI), it shared 50% similarities with a protein secreted by B. firmus, and the one by Paenibacillus sp.…”
Section: Identification Of the Mcementioning
confidence: 63%
“…(Hang et al, 2016a;2016b), have been reported to produce extra-cellular MCEs. Production of bacterial MCEs by submerged fermentation (SMF) was efficient with a high yield of MCE (Ding et al, 2012), and it was simple to operate compared to solid state fermentation (SSF) by fungus (Thakur et al, 1990).…”
Section: Introductionmentioning
confidence: 99%
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