Characterization of Sericin Powder Prepared from Citric Acid-degraded Sericin Polypeptides of the Silkworm,Bombyx Mori | Zendy

Akira Kurioka | Zendy; Fujie Kurioka | Zendy; Masayoshi YAMAZAKI | Zendy

Open Access

Characterization of Sericin Powder Prepared from Citric Acid-degraded Sericin Polypeptides of the Silkworm,Bombyx Mori

Author(s) -

Akira Kurioka,

Fujie Kurioka,

Masayoshi YAMAZAKI

Publication year - 2004

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.68.774

Subject(s) - sericin , bombyx mori , fibroin , citric acid , trypsin , succinic acid , chemistry , bombycidae , aqueous solution , nuclear chemistry , trypsin inhibitor , chromatography , biochemistry , materials science , silk , organic chemistry , enzyme , composite material , gene

Acid-degraded sericin powder (AC-SP) was prepared from aqueous solution containing citric acid-degraded sericin polypeptides of Bombyx mori. The morphological and biochemical properties of AC-SP were compared with those of alkali-degraded sericin powder (AL-SP) and hot-water degraded sericin powder (HW-SP). Based on an SEM analysis, AC-SP showed a thin film structure of 10-100 microm with good dispersity while AL-SP and HW-SP had a much larger thin film structure (<500 microm). The extract of AC-SP showed stronger trypsin inhibitor activity due to cocoon shell trypsin inhibitor (CSTI-IV) than that of HW-SP. The extract of AL-SP showed no CSTI-IV activity. It was found that AC-SP was a trypsin inhibitor complex powder and that the release of CSTI-IV from AC-SP depended on pH and ion strength. Similar powder materials were obtained when such organic acids as tartaric acid and succinic acid were used. These results suggest that the acid-degraded sericin polypeptides work as a protein matrix to which CSTI-IV may bind ionically.

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