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Process Biochem., Volume 41, Issue 9, September 2006, Pages 2097-2100 | https://doi.org/10.1016/j.procbio.2006.05.008 Recovery of a novel Ca-binding peptide from Alaska Pollack (Theragra chalcogramma) backbone by pepsinolytic hydrolysis

Won-Kyo Jung^a, Rohan Karawita^b, Soo-Jin Heo^b, Bae-Jin Lee^c, Se-Kwon Kim^a, You-Jin Jeon^b,*

^aDepartment of Chemistry, Pukyong National University, Busan 608-737, South Korea
^bFaculty of Applied Marine Science, Cheju National University, Jeju 690-756, South Korea
^cMarine Bioprocess Co. Ltd., Pukyong National University, Busan 608-737, South Korea

^*Corresponding author

Abstract

Low molecular weight peptide with a high affinity to calcium was recovered from pepsinolytic hydrolysates of Theragra chalcogramma backbone discarded from fish processing using a hydroxyapatite affinity chromatography. T. chalcogramma backbone peptide (TBP), Val-Leu-Ser-Gly-Gly-Thr-Thr-Met-Ala-Met-Tyr-Thr-Leu-Val (M_W: 1442 Da), exhibited the highest affinity to calcium ion on the surface of hydroxyapaptite (HA) crystals. In vitro calcium-binding assay elucidated that TBP can solublize a similar content of calcium with casein phosphopeptide (CPP). In the present study, it is possible to provide utilization of fish backbones in a novel nutraceutical material with a high solubility for calcium to oriental people with lactose indigestion and intolerance.

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