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Large-scale production and application of leucine aminopeptidase produced by <Emphasis Type="Italic">Aspergillus oryzae</Emphasis> LL1 for hydrolysis of chicken breast meat
Authors:Shie-Jea Lin  Yi-Hong Chen  Li-Lin Chen  Hsiao-Hui Feng  Chu-Chin Chen  Wen-Shen Chu
Affiliation:(1) Bioresource Collection and Research Center, Food Industry Research and Development Institute, 331 Shih-Ping Road, Hsinchu, 300, Taiwan;(2) Product and Process Research Center, Food Industry Research and Development Institute, Hsinchu, 300, Taiwan
Abstract:Leucine aminopeptidase (LAP) production by Aspergillus oryzae LL1 (LAP LL1) was scaled up by varying fermenting conditions. The maximal LAP activity for 5, 20, 250, and 2,000 L fermenters were 0.22, 0.16, 0.19, and 0.12 U mL−1, respectively. LAP LL1 production coincides with increasing pH for all scale cases. A pilot plant scale hydrolysis experiment using LAP LL1 was prepared by removing the cells from 1,000 L of A. oryzae LL1 culture and concentrating the supernatant to ∼60 L, with a LAP LL1 activity yield of ∼20% and a specific LAP activity of 0.054 U mg−1, comparable to Flavourzyme. Using a casein substrate, LAP LL1 specific protease activity (50.9 U mg−1) is 43% higher than Flavourzyme (35.6 U mg−1). We believe LAP LL1 has potential use as an industrial enzyme for food processing. Comparing the hydrolysis effects on chopped chicken breast meat (100 g), the degree of hydrolysis (DH) of LAP LL1 (50.6%) was about twice as effective as Flavourzyme (25.6%). On a pilot-plant scale hydrolysis experiment of chopped chicken breast meat (54 kg), the DH of LAP LL1 was 45.6%. Adding 30 μmol L−1 zinc increased DH by 33.3% for LAPs LL1 but zinc did not enhance Flavourzyme hydrolysis. Together, this study provides possibility that LAP LL1 has significant potential for application in the food industry. Shie-Jea Lin and Yi-Hong Chen have contributed equally to this work.
Keywords:Aspergillus           oryzae LL1  Fermentation  Leucine aminopeptidases  Meat hydrolysis  Zn2+
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