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  • 1
    Electronic Resource
    Electronic Resource
    INHIBITING THE ACTIVITY OF ACTINIDIN BY ORYZACYSTATIN FOR THE APPLICATION OF FRESH KIWIFRUIT TO GELATIN-BASED FOODS (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 19 (1995), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Fresh kiwifruit has potent proteinase activity that can be ascribed to actinidin, a cysteine proteinase. Without regulating this activity, kiwifruit can not be used satisfactorily as a food ingredient for protein-based foods. We found that oryzacystatin, a rice seed cysteine proteinase inhibitor, stoichiometrically inhibits the actinidin activity and can be used in making gelatin jellies with fresh kiwifruit slices. We also found that a gelatin solution mixed with an actinidin preparation did not form a gel because 118 kd and 130 kd components in the gelatin had undergone degradation. However, gelation occurred with no appreciable degradation in these two major gelatin components when oryzacystatin was added to this actinidin preparation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1995.tb00540.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    MODULATING THE CONDITIONING OF MEAT BY THE USE OF ORYZACYSTATIN, A CYSTEINE PROTEINASE INHIBITOR OF RICE SEED ORIGIN (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 15 (1991), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A new process was developed to regulate the papain-induced overtenderization of meat by using oryzacystatin, a cysteine proteinase inhibitor of rice seed origin. Meat cubes (2 × 2 × 2 cm each), aged 3 days, were treated with a 0.1 fold weight of papain solution and incubated at 8°C. The most favorable degree of tenderization resulted when a 2% papain solution was used for 2 h at 8°C. When the incubation was made for 24 h or longer, overtenderization resulted. The incubation of a meat cube with papain for the first 2 h and then with an adequate amount of added oryzacystatin for the subsequent 22 h was effective in regulating overtenderization. It was also confirmed by SDS-polyacrylamide gel electro-phoresis that the use of oryzacystatin under similar incubation conditions regulated the papain-aided hydrolysis of myofibrillar proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1991.tb00160.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    PURIFICATION AND CHARACTERIZATION OF A NEUTRAL PROTEASE THAT CONTRIBUTES TO THE UNIQUE FLAVOR AND TEXTURE OF TOFU-MISOZUKE (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 21 (1997), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Tofu-misozuke, a food inherent to the Fukuoka district of Japan is a type of soybean curd fermented in miso (soybean paste), possessing a unique taste and texture. A cheese-like taste and softness also develops in Tofu-misozuke during ripening. The changes in Tofu-misozuke are caused by proteases originating from Koji, one of the raw materials of miso. We examined which of the proteases is the cause of taste and textural-alterations. The protease was purified by DE52, Sephacryl S-300, Mono Q, and Superose 12 chromatography. The amino terminal sequence of the purified enzyme is TEVTDXKGDA, in agreement with the sequence of neutral protease II from Aspergillus oryzae. The purified enzyme is a heat stable metallo-protease. These results indicate that the purified enzyme is highly similar to the neutral protease II of Aspergillus oryzae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1997.tb00214.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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