Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. Has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers. Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Optimum pH is 4.5-5.5. Homodimer (PubMed:22128166). May form higher multimers (Probable). Localized to the perinuclear area of the cytoplasm but not to lysosomes. Detected in placenta (at protein level) (PubMed:8383699). Detected in fibroblasts and testis (PubMed:2511208). The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyl hydrolase 35 family. Beta-galactosidase entry